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Block Report for: C

ACHE, BCHE, Carb_B_Annelida, Carb_B_Arthropoda, Carb_B_Bacteria, Carb_B_Brachiopoda, Carb_B_Chordata, Carb_B_Mollusca, Carb_B_Nematoda, Carb_B_Root, Carboxylesterase, Cholesterol_esterase, Cholinesterase, Cholinesterase-like, Fungal_carboxylesterase_lipase, Gliotactin, Glutactin, Juvenile_hormone_esterase, Neuroligin, Neurotactin, Non-catalytic_C, OtherNon-catalytic_C, Thyroglobulin

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FamilyACHEParent FamilyCholinesterase
CommentAcetylcholinesterase (ACHE; EC 3.1.1.7) controls synaptic and neurohumoral cholinergic activity by hydrolyzing the neurotransmitter acetylcholine. ACHE function relies on precise regulation of its expression and localization. In particular, alternative splicing of the 3-prime region of ACHE results in ACHE isoforms with distinct C-terminal peptides that determine posttranslational maturation and oligomeric assembly. Acetylcholinesterase is also found on the red blood cell membranes, where it constitutes the Yt blood group antigen.
InterproIPR000997 (Cholinesterase), IPR002018 (Carboxylesterase, type B)Pdoc PDOC00112
PFamPF00135 (COesterase), PF08674 (AChE_tetra)Prints PR00878Prosite PS00122, PS00941
ECAt KYOTO 3.1.1.7 at NYCEZYME 3.1.1.7Tables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Old and new questions about cholinesterases
    Massoulie J, Perrier N, Noureddine H, Liang D, Bon S
    Ref: Chemico-Biological Interactions, 175:30, 2008 : PubMed

            

    Title: Acetylcholinesterase genes within the Diptera: takeover and loss in true flies
    Huchard E, Martinez M, Alout H, Douzery EJ, Lutfalla G, Berthomieu A, Berticat C, Raymond M, Weill M
    Ref: Proc Biol Sci, 273:2595, 2006 : PubMed

            

    Title: The cholinesterases: from genes to proteins
    Taylor P, Radic Z
    Ref: Annual Review of Pharmacology & Toxicology, 34:281, 1994 : PubMed

            

    Title: Molecular and cellular biology of cholinesterases
    Massoulie J, Pezzementi L, Bon S, Krejci E, Vallette FM
    Ref: Prog Neurobiol, 41:31, 1993 : PubMed

            

    Title: Comparison of butyrylcholinesterase and acetylcholinesterase.
    Chatonnet A, Lockridge O
    Ref: Biochemical Journal, 260:625, 1989 : PubMed

            

> Structure scheme for ACHE
> Structures for ACHE (315)
> List of Gene_Locus for ACHE (538)


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FamilyBCHEParent FamilyCholinesterase
CommentAcylcholine acylhydrolase, Butyrylcholine esterase, Choline esterase II, Pseudocholinesterase. Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters. BChE deficiency is a metabolic disorder characterized by prolonged apnoea after the use of certain anesthetic drugs, including the muscle relaxants succinylcholine or mivacurium and other ester local anesthetics.Various autosomal recessive mutations of the gene exist in human population
InterproIPR000997 (Cholinesterase), IPR002018 (Carboxylesterase, type B)Pdoc PDOC00112
PFamPF00135 (COesterase)Prints PR00878Prosite PS00122, PS00941
ECAt KYOTO 3.1.1.8 at NYCEZYME 3.1.1.8Tables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Old and new questions about cholinesterases
    Massoulie J, Perrier N, Noureddine H, Liang D, Bon S
    Ref: Chemico-Biological Interactions, 175:30, 2008 : PubMed

            

    Title: The cholinesterases: from genes to proteins
    Taylor P, Radic Z
    Ref: Annual Review of Pharmacology & Toxicology, 34:281, 1994 : PubMed

            

    Title: Molecular and cellular biology of cholinesterases
    Massoulie J, Pezzementi L, Bon S, Krejci E, Vallette FM
    Ref: Prog Neurobiol, 41:31, 1993 : PubMed

            

    Title: Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine.
    Lockridge O
    Ref: Pharmacol Ther, 47:35, 1990 : PubMed

            

    Title: Comparison of butyrylcholinesterase and acetylcholinesterase.
    Chatonnet A, Lockridge O
    Ref: Biochemical Journal, 260:625, 1989 : PubMed

            

> Structure scheme for BCHE
> Structures for BCHE (91)
> List of Gene_Locus for BCHE (91)


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FamilyCarb_B_AnnelidaParent FamilyCarboxylesterase
CommentThis family was extracted from the previous Carboxylesterase COesterase family.
InterproIPR002018 (Carboxylesterase, type B)Pdoc PDOC00112
PFamPF00135 (COesterase)PrintsProsite PS00122, PS00941
ECAt KYOTO 3.1.1.1 at NYCEZYME 3.1.1.1Tables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Insights into bilaterian evolution from three spiralian genomes
    Simakov O, Marletaz F, Cho SJ, Edsinger-Gonzales E, Havlak P, Hellsten U, Kuo DH, Larsson T, Lv J and Rokhsar DS <16 more author(s)>
    Ref: Nature, 493:526, 2013 : PubMed

            

    Title: Evolution of cholinesterases in the animal kingdom
    Pezzementi L, Chatonnet A
    Ref: Chemico-Biological Interactions, 187:27, 2010 : PubMed

            

&gt; Structure scheme for Carb_B_Annelida
no Structure
&gt; List of Gene_Locus for Carb_B_Annelida (10)


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FamilyCarb_B_ArthropodaParent FamilyCarboxylesterase
CommentCarboxylesterases of insects have been subdivided in clades A to M (Claudianos 2006 Ranson 2002). With the Dietary class (clades ABC), the Pheromone/hormone processing class (clades D to G), the Neuro/developmental class (H to M). The present family Carb_B_Arthropoda corresponds to clades ABC. Members of these clades are important in detoxifixtion of insecticides .Gene amplifications or point mutations leading to resistance. Clades D to M have their own family (AChE, JHE, Glutactin Neuroligin, Neurotactin). This family was extracted from the previous Carboxylesterase COesterase family. This family corresponds to the Carbohydrate Esterase family CE10 in CAZy - Carbohydrate-Active enZYmes database (CE_10).
InterproIPR002018 (Carboxylesterase, type B)Pdoc PDOC00112
PFamPF00135 (COesterase)PrintsProsite PS00122, PS00941
ECAt KYOTO 3.1.1.1 at NYCEZYME 3.1.1.1Tables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Mapping the Accessible Conformational Landscape of an Insect Carboxylesterase Using Conformational Ensemble Analysis and Kinetic Crystallography
    Correy GJ, Carr PD, Meirelles T, Mabbitt PD, Fraser NJ, Weik M, Jackson CJ
    Ref: Structure, 24:977, 2016 : PubMed

            

    Title: Identification of biotransformation enzymes in the antennae of codling moth Cydia pomonella
    Huang X, Liu L, Su X, Feng J
    Ref: Gene, 580:73, 2016 : PubMed

            

    Title: Functional characterization of an alpha-esterase gene involving malathion detoxification in Bactrocera dorsalis (Hendel)
    Wang LL, Lu XP, Meng LW, Huang Y, Wei D, Jiang HB, Smagghe G, Wang JJ
    Ref: Pestic Biochem Physiol, 130:44, 2016 : PubMed

            

    Title: Characteristics of carboxylesterase genes and their expression-level between acaricide-susceptible and resistant Tetranychus cinnabarinus (Boisduval)
    Wei P, Shi L, Shen G, Xu Z, Liu J, Pan Y, He L
    Ref: Pestic Biochem Physiol, 131:87, 2016 : PubMed

            

    Title: Structure and function of an insect alpha-carboxylesterase (alphaEsterase7) associated with insecticide resistance
    Jackson CJ, Liu JW, Carr PD, Younus F, Coppin C, Meirelles T, Lethier M, Pandey G, Ollis DL and Oakeshott JG <2 more author(s)>
    Ref: Proc Natl Acad Sci U S A, 110:10177, 2013 : PubMed

            

    Title: A deficit of detoxification enzymes: pesticide sensitivity and environmental response in the honeybee
    Claudianos C, Ranson H, Johnson RM, Biswas S, Schuler MA, Berenbaum MR, Feyereisen R, Oakeshott JG
    Ref: Insect Molecular Biology, 15:615, 2006 : PubMed

            

    Title: Quantitative polymerase chain reaction to estimate the number of amplified esterase genes in insecticide-resistant mosquitoes
    Weill M, Berticat C, Raymond M, Chevillon C
    Ref: Analytical Biochemistry, 285:267, 2000 : PubMed

            

    Title: Carboxyl/cholinesterases: a case study of the evolution of a successful multigene family
    Oakeshott JG, Claudianos C, Russell RJ, Robin GC
    Ref: Bioessays, 21:1031, 1999 : PubMed

            

    Title: A new esterase gene amplification involved in OP resistance in Culex pipiens mosquitoes from China
    Qiao CL, Marquine M, Pasteur N, Raymond M
    Ref: Biochemical Genetics, 36:417, 1998 : PubMed

            

    Title: A single amino acid substitution converts a carboxylesterase to an organophosphorus hydrolase and confers insecticide resistance on a blowfly
    Newcomb RD, Campbell PM, Ollis DL, Cheah E, Russell RJ, Oakeshott JG
    Ref: Proceedings of the National Academy of Sciences of the United States of America, 94:7464, 1997 : PubMed

            

    Title: Action of Esterase B1 on Chlorpyrifos in Organophosphate-Resistant Culex Mosquitos
    Cuany A, Handani J, Berge J, Fournier D, Raymond M, Georghiou GP, Pasteur N
    Ref: Pesticide Biochemistry and Physiology, 45:1, 1993 : PubMed

            

    Title: Worldwide migration of amplified insecticide resistance genes in mosquitoes.
    Raymond M, Callaghan A, Fort P, Pasteur N
    Ref: Nature, 350:151, 1991 : PubMed

            

    Title: On the origins of esterases
    Myers M, Richmond RC, Oakeshott JG
    Ref: Molecular Biology Evolution, 5:113, 1988 : PubMed

            

    Title: Amplification of an esterase gene is responsible for insecticide resistance in a California Culex mosquito
    Mouches C, Pasteur N, Berge JB, Hyrien O, Raymond M, de Saint Vincent BR, de Silvestri M, Georghiou GP
    Ref: Science, 233:778, 1986 : PubMed

            

&gt; Structure scheme for Carb_B_Arthropoda
&gt; Structures for Carb_B_Arthropoda (32)
&gt; List of Gene_Locus for Carb_B_Arthropoda (1570)


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FamilyCarb_B_BacteriaParent FamilyCarboxylesterase
CommentThis family was extracted from the previous Carboxylesterase COesterase family. Not all bacteria possess esterase with the SEDCLYLN signature. This family corresponds to the Carbohydrate Esterase family CE10 in CAZy - Carbohydrate-Active enZYmes database (CE_10). As bacterial enzymes this family correspond to family VII of the classification of Arpigny et al 1999
InterproIPR002018 (Carboxylesterase, type B)Pdoc PDOC00112
PFamPF00135 (COesterase)PrintsProsite PS00122, PS00941
ECAt KYOTO 3.1.1.1 at NYCEZYME 3.1.1.1Tables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Crystal structure of the Geobacillus stearothermophilus carboxylesterase Est55 and its activation of prodrug CPT-11
    Liu P, Ewis HE, Tai PC, Lu CD, Weber IT
    Ref: Journal of Molecular Biology, 367:212, 2007 : PubMed

            

    Title: Molecular cloning and characterization of two thermostable carboxyl esterases from Geobacillus stearothermophilus
    Ewis HE, Abdelal AT, Lu CD
    Ref: Gene, 329:187, 2004 : PubMed

            

    Title: A structural view of evolutionary divergence
    Spiller B, Gershenson A, Arnold FH, Stevens RC
    Ref: Proceedings of the National Academy of Sciences of the United States of America, 96:12305, 1999 : PubMed

            

    Title: The Bacillus subtilis pnbA gene encoding p-nitrobenzyl esterase: cloning, sequence and high-level expression in Escherichia coli
    Zock J, Cantwell C, Swartling J, Hodges R, Pohl T, Sutton K, Rosteck P, Jr., McGilvray D, Queener S
    Ref: Gene, 151:37, 1994 : PubMed

            

&gt; Structure scheme for Carb_B_Bacteria
&gt; Structures for Carb_B_Bacteria (10)
&gt; List of Gene_Locus for Carb_B_Bacteria (4340)


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FamilyCarb_B_BrachiopodaParent FamilyCarboxylesterase
CommentThis family was extracted from the previous Carboxylesterase COesterase family. This family corresponds to the Carbohydrate Esterase family CE10 in CAZy - Carbohydrate-Active enZYmes database (CE_10).
InterproIPR002018 (Carboxylesterase, type B)Pdoc PDOC00112
PFamPF00135 (COesterase)PrintsProsite PS00122, PS00941
ECAt KYOTO 3.1.1.1 at NYCEZYME 3.1.1.1Tables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
no reference
&gt; Structure scheme for Carb_B_Brachiopoda
no Structure
&gt; List of Gene_Locus for Carb_B_Brachiopoda (61)


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FamilyCarb_B_ChordataParent FamilyCarboxylesterase
CommentThis family was extracted from the previous Carboxylesterase COesterase family. This family corresponds to the Carbohydrate Esterase family CE10 in CAZy - Carbohydrate-Active enZYmes database (CE_10). Mammalian liver carboxylesterases (CESs; EC 3.1.1.1) hydrolyze various xenobiotics and endogenous substrates with ester, thioester, or amide bonds and are thought to function mainly in drug metabolism and detoxication of harmful chemicals. CES1 is also responsible for hydrolysis of stored cholesterol esters in macrophage foam cells and release of free cholesterol for high density lipoprotein-mediated cholesterol efflux
InterproIPR002018 (Carboxylesterase, type B)Pdoc PDOC00112
PFamPF00135 (COesterase)PrintsProsite PS00122, PS00941
ECAt KYOTO 3.1.1.1 at NYCEZYME 3.1.1.1Tables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Carboxylesterases in lipid metabolism: from mouse to human
    Lian J, Nelson R, Lehner R
    Ref: Protein Cell, 9:178, 2018 : PubMed

            

    Title: Nomenclature for alleles of the human carboxylesterase 1 gene
    Rasmussen HB, Madsen MB, Hansen PR
    Ref: Pharmacogenet Genomics, 27:78, 2017 : PubMed

            

    Title: Comparison of substrate specificity among human arylacetamide deacetylase and carboxylesterases
    Fukami T, Kariya M, Kurokawa T, Iida A, Nakajima M
    Ref: Eur J Pharm Sci, 78:47, 2015 : PubMed

            

    Title: Human carboxylesterase 1 stereoselectively binds the nerve agent cyclosarin and spontaneously hydrolyzes the nerve agent sarin
    Hemmert AC, Otto TC, Wierdl M, Edwards CC, Fleming CD, MacDonald M, Cashman JR, Potter PM, Cerasoli DM, Redinbo MR
    Ref: Molecular Pharmacology, 77:508, 2010 : PubMed

            

    Title: Recommended nomenclature for five mammalian carboxylesterase gene families: human, mouse, and rat genes and proteins
    Holmes RS, Wright MW, Laulederkind SJ, Cox LA, Hosokawa M, Imai T, Ishibashi S, Lehner R, Miyazaki M and Maltais LJ <9 more author(s)>
    Ref: Mamm Genome, 21:427, 2010 : PubMed

            

    Title: Carboxylesterases: structure, function and polymorphism in mammals
    Satoh T, Hosokawa M
    Ref: Journal of Pesticide Science, 35:218, 2010 : PubMed

            

    Title: Genomic analysis of the carboxylesterases: identification and classification of novel forms
    Williams ET, Wang H, Wrighton SA, Qian YW, Perkins EJ
    Ref: Mol Phylogenet Evol, 57:23, 2010 : PubMed

            

    Title: Crystal structures of human carboxylesterase 1 in covalent complexes with the chemical warfare agents soman and tabun
    Fleming CD, Edwards CC, Kirby SD, Maxwell DM, Potter PM, Cerasoli DM, Redinbo MR
    Ref: Biochemistry, 46:5063, 2007 : PubMed

            

    Title: Multisite promiscuity in the processing of endogenous substrates by human carboxylesterase 1
    Bencharit S, Edwards CC, Morton CL, Howard-Williams EL, Kuhn P, Potter PM, Redinbo MR
    Ref: Journal of Molecular Biology, 363:201, 2006 : PubMed

            

    Title: Structure, function and regulation of carboxylesterases
    Satoh T, Hosokawa M
    Ref: Chemico-Biological Interactions, 162:195, 2006 : PubMed

            

    Title: Structural insights into drug processing by human carboxylesterase 1: tamoxifen, mevastatin, and inhibition by benzil
    Fleming CD, Bencharit S, Edwards CC, Hyatt JL, Tsurkan L, Bai F, Fraga C, Morton CL, Howard-Williams EL and Redinbo MR <1 more author(s)>
    Ref: Journal of Molecular Biology, 352:165, 2005 : PubMed

            

    Title: Crystal structure of human carboxylesterase 1 complexed with the Alzheimer's drug tacrine: from binding promiscuity to selective inhibition
    Bencharit S, Morton CL, Hyatt JL, Kuhn P, Danks MK, Potter PM, Redinbo MR
    Ref: Chemical Biology, 10:341, 2003 : PubMed

            

    Title: Structural insights into CPT-11 activation by mammalian carboxylesterases
    Bencharit S, Morton CL, Howard-Williams EL, Danks MK, Potter PM, Redinbo MR
    Ref: Nat Struct Biol, 9:337, 2002 : PubMed

            

    Title: On the origins of esterases
    Myers M, Richmond RC, Oakeshott JG
    Ref: Molecular Biology Evolution, 5:113, 1988 : PubMed

            

&gt; Structure scheme for Carb_B_Chordata
&gt; Structures for Carb_B_Chordata (21)
&gt; List of Gene_Locus for Carb_B_Chordata (543)


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FamilyCarb_B_MolluscaParent FamilyCarboxylesterase
CommentThis family was extracted from the previous Carboxylesterase COesterase family. This family corresponds to the Carbohydrate Esterase family CE10 in CAZy - Carbohydrate-Active enZYmes database (CE_10).
InterproIPR002018 (Carboxylesterase, type B)Pdoc PDOC00112
PFamPF00135 (COesterase)PrintsProsite PS00122, PS00941
ECAt KYOTO 3.1.1.1 at NYCEZYME 3.1.1.1Tables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Carboxyl/cholinesterases: a case study of the evolution of a successful multigene family
    Oakeshott JG, Claudianos C, Russell RJ, Robin GC
    Ref: Bioessays, 21:1031, 1999 : PubMed

            

    Title: On the origins of esterases
    Myers M, Richmond RC, Oakeshott JG
    Ref: Molecular Biology Evolution, 5:113, 1988 : PubMed

            

&gt; Structure scheme for Carb_B_Mollusca
no Structure
&gt; List of Gene_Locus for Carb_B_Mollusca (60)


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FamilyCarb_B_NematodaParent FamilyCarboxylesterase
CommentThis family was extracted from the previous Carboxylesterase COesterase family. This family corresponds to the Carbohydrate Esterase family CE10 in CAZy - Carbohydrate-Active enZYmes database (CE_10). A subset of this family is isolated as Esterase CM06B1-like family in Interpro IPR043187.
InterproIPR002018 (Carboxylesterase, type B), IPR043187 (Esterase CM06B1-like)Pdoc PDOC00112
PFamPF00135 (COesterase)PrintsProsite PS00122, PS00941
ECAt KYOTO 3.1.1.1 at NYCEZYME 3.1.1.1Tables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: A carboxylesterase from the parasitic nematode Ascaris suum homologous to the intestinal-specific ges-1 esterase of Caenorhabditis elegans
    Azzaria M, Henzel WJ, McGhee JD
    Ref: Comparative Biochemistry & Physiology B Biochem Mol Biol, 109:225, 1994 : PubMed

            

    Title: cDNA sequence, gene structure, and cholinesterase-like domains of an esterase from Caenorhabditis elegans mapped to chromosome V
    Fedon Y, Cousin X, Toutant JP, Thierry-Mieg D, Arpagaus M
    Ref: DNA Sequence, 3:347, 1993 : PubMed

            

    Title: The gut esterase gene (ges-1) from the nematodes Caenorhabditis elegans and Caenorhabditis briggsae
    Kennedy BP, Aamodt EJ, Allen FL, Chung MA, Heschl MF, McGhee JD
    Ref: Journal of Molecular Biology, 229:890, 1993 : PubMed

            

    Title: On the origins of esterases
    Myers M, Richmond RC, Oakeshott JG
    Ref: Molecular Biology Evolution, 5:113, 1988 : PubMed

            

&gt; Structure scheme for Carb_B_Nematoda
no Structure
&gt; List of Gene_Locus for Carb_B_Nematoda (378)


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FamilyCarb_B_RootParent FamilyCarboxylesterase
CommentThis family was extracted from the previous Carboxylesterase COesterase family. it contains putative esterase from eucaryotes (not insects nematodes or chordates)
InterproIPR002018 (Carboxylesterase, type B)Pdoc PDOC00112
PFamPF00135 (COesterase)PrintsProsite PS00122, PS00941
ECAt KYOTO 3.1.1.1 at NYCEZYME 3.1.1.1Tables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Molecular characterization of Hydra acetylcholinesterase and its catalytic activity
    Takahashi T, Hamaue N
    Ref: FEBS Letters, 584:511, 2010 : PubMed

            

    Title: Acetylcholinesterase activity in Clytia hemisphaerica (Cnidaria)
    Denker E, Chatonnet A, Rabet N
    Ref: Chemico-Biological Interactions, 175:125, 2008 : PubMed

            

&gt; Structure scheme for Carb_B_Root
no Structure
&gt; List of Gene_Locus for Carb_B_Root (147)


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FamilyCarboxylesteraseChildren FamilyCarb_B_Bacteria, Carb_B_Root, Carb_B_Arthropoda, Carb_B_Mollusca, Carb_B_Nematoda, Carb_B_Chordata, Carb_B_Annelida, Cholesterol_esterase, Fungal_carboxylesterase_lipase, Juvenile_hormone_esterase, Carb_B_Brachiopoda
CommentHigher eukaryotes have many distinct esterases. The different types include those that act on carboxylic esters (EC 3.1.1). Carboxyl-esterases have been classified into three categories (A, B and C) on the basis of differential patterns of inhibition by organophosphates. Here are B type. WARNING There is no Plant carboxylesterases in this family except an EST from sorgho (sorbi-cxest) which could be a contaminant. Plant carboxylesterases do not possess SEDCLYLN and are included in a specific family: Plant_carboxylesterase. This family corresponds to the Carbohydrate Esterase family CE10 in CAZy - Carbohydrate-Active enZYmes database (CE_10). For bacterial enzymes this family correspond to family VII of the classification of Arpigny and Jaeger (1999)
InterproIPR002018 (Carboxylesterase, type B)Pdoc PDOC00112
PFamPF00135 (COesterase)PrintsProsite PS00122, PS00941
ECAt KYOTO 3.1.1.1 at NYCEZYME 3.1.1.1Tables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Carboxyl ester lipase: structure-function relationship and physiological role in lipoprotein metabolism and atherosclerosis
    Hui DY, Howles PN
    Ref: J Lipid Res, 43:2017, 2002 : PubMed

            

    Title: Carboxyl/cholinesterases: a case study of the evolution of a successful multigene family
    Oakeshott JG, Claudianos C, Russell RJ, Robin GC
    Ref: Bioessays, 21:1031, 1999 : PubMed

            

    Title: The mammalian carboxylesterases: from molecules to functions
    Satoh T, Hosokawa M
    Ref: Annual Review of Pharmacology & Toxicology, 38:257, 1998 : PubMed

            

&gt; Structure scheme for Carboxylesterase
&gt; Structures for Carboxylesterase (90)
&gt; List of Gene_Locus for Carboxylesterase (12256)


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FamilyCholesterol_esteraseParent FamilyCarboxylesterase
CommentThe human lactating mammary gland and pancreas produce a lipolytic enzyme, carboxyl-ester lipase, earlier called bile salt-stimulated lipase. Carboxyl-ester lipase is a major component of pancreatic juice and is responsible for the hydrolysis of cholesterol esters as well as a variety of other dietary esters. The enzyme is activated when mixed with bile salts, and plays an important role in the digestion of milk fat in newborn infants. This enzyme combines properties of esterases (activity on esters soluble in water) and lipases (activity on insoluble long chain acylglycerols) Numerous repeats at the c-term excluded in ESTHER (only n-term Pfam A COesterase 1 544)
InterproIPR002018 (Carboxylesterase, type B), IPR033560 (Bile salt-activated lipase BAL)Pdoc PDOC00112
PFamPF00135 (COesterase)PrintsProsite PS00122, PS00941
ECAt KYOTO 3.1.1.13 at NYCEZYME 3.1.1.13Tables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Comparative Study of the Molecular Characterization, Evolution, and Structure Modeling of Digestive Lipase Genes Reveals the Different Evolutionary Selection Between Mammals and Fishes
    Tang SL, Liang XF, He S, Li L, Alam MS, Wu J
    Ref: Front Genet, 13:909091, 2022 : PubMed

            

    Title: Comparative Structures and Evolution of Vertebrate Carboxyl Ester Lipase (CEL) Genes and Proteins with a Major Role in Reverse Cholesterol Transport
    Holmes RS, Cox LA
    Ref: Cholesterol, 2011:781643, 2011 : PubMed

            

    Title: The structure of truncated recombinant human bile salt-stimulated lipase reveals bile salt-independent conformational flexibility at the active-site loop and provides insights into heparin binding
    Moore SA, Kingston RL, Loomes KM, Hernell O, Blackberg L, Baker HM, Baker EN
    Ref: Journal of Molecular Biology, 312:511, 2001 : PubMed

            

    Title: Crystal structure of the catalytic domain of human bile salt activated lipase
    Terzyan S, Wang CS, Downs D, Hunter B, Zhang XC
    Ref: Protein Science, 9:1783, 2000 : PubMed

            

    Title: Structure of bovine pancreatic cholesterol esterase at 1.6 A: novel structural features involved in lipase activation
    Chen JC, Miercke LJ, Krucinski J, Starr JR, Saenz G, Wang X, Spilburg CA, Lange LG, Ellsworth JL, Stroud RM
    Ref: Biochemistry, 37:5107, 1998 : PubMed

            

    Title: The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism
    Wang X, Wang CS, Tang J, Dyda F, Zhang XC
    Ref: Structure, 5:1209, 1997 : PubMed

            

&gt; Structure scheme for Cholesterol_esterase
&gt; Structures for Cholesterol_esterase (10)
&gt; List of Gene_Locus for Cholesterol_esterase (128)


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FamilyCholinesteraseChildren FamilyACHE, BCHE, Cholinesterase-like
CommentAcetylcholinesterase (ACHE; EC 3.1.1.7) controls synaptic and neurohumoral cholinergic activity by hydrolyzing the neurotransmitter acetylcholine. ACHE function relies on precise regulation of its expression and localization. In particular, alternative splicing of the 3-prime region of ACHE results in ACHE isoforms with distinct C-terminal peptides that determine posttranslational maturation and oligomeric assembly
InterproIPR000997 (Cholinesterase), IPR002018 (Carboxylesterase, type B)Pdoc
PFamPF00135 (COesterase)Prints PR00878Prosite
EC no EC numberTables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Old and new questions about cholinesterases
    Massoulie J, Perrier N, Noureddine H, Liang D, Bon S
    Ref: Chemico-Biological Interactions, 175:30, 2008 : PubMed

            

    Title: The cholinesterases: from genes to proteins
    Taylor P, Radic Z
    Ref: Annual Review of Pharmacology & Toxicology, 34:281, 1994 : PubMed

            

    Title: Molecular and cellular biology of cholinesterases
    Massoulie J, Pezzementi L, Bon S, Krejci E, Vallette FM
    Ref: Prog Neurobiol, 41:31, 1993 : PubMed

            

    Title: Comparison of butyrylcholinesterase and acetylcholinesterase.
    Chatonnet A, Lockridge O
    Ref: Biochemical Journal, 260:625, 1989 : PubMed

            

no Image
&gt; Structures for Cholinesterase (406)
&gt; List of Gene_Locus for Cholinesterase (1184)


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FamilyCholinesterase-likeParent FamilyCholinesterase
CommentAnalysis of the complete genome sequences of numerous representatives of the various metazoan phyla show that moderate amplification of cholinesterase genes is not uncommon in molluscs, echinoderms, hemichordates, prochordates or lepidosauria. Amplification of acetylcholinesterase genes is also a feature of parasitic nematodes or ticks. This family is now called Cholinesterase like. It also contains sequences very close to AChE but which are either incomplete or are missing W84 or one of the residue of the catalytic triad or are pseudogenes with deletions or errors of conceptual splicing Before this family was called Dictyostelium_crys as it contained only Dict proteins. These proteins have an active site serine and have probably an esterase activity but are in membrane-enclosed crystals and probably have non catalytic functions.
InterproIPR000997 (Cholinesterase), IPR002018 (Carboxylesterase, type B)Pdoc
PFamPF00135 (COesterase)PrintsProsite
EC no EC numberTables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Molecular biology of tick acetylcholinesterases
    Temeyer KB
    Ref: Front Biosci (Landmark Ed), 23:1320, 2018 : PubMed

            

    Title: Natural genomic amplification of cholinesterase genes in animals
    Chatonnet A, Lenfant N, Marchot P, Selkirk ME
    Ref: Journal of Neurochemistry, 142 Suppl 2:73, 2017 : PubMed

            

    Title: Nematode acetylcholinesterases are encoded by multiple genes and perform non-overlapping functions
    Selkirk ME, Lazari O, Hussein AS, Matthews JB
    Ref: Chemico-Biological Interactions, 157-158:263, 2005 : PubMed

            

    Title: Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid
    Krejci E, Duval N, Chatonnet A, Vincens P, Massoulie J
    Ref: Proceedings of the National Academy of Sciences of the United States of America, 88:6647, 1991 : PubMed

            

    Title: Membrane-enclosed crystals in Dictyostelium discoideum cells, consisting of developmentally regulated proteins with sequence similarities to known esterases
    Bomblies L, Biegelmann E, Doring V, Gerisch G, Krafft-Czepa H, Noegel AA, Schleicher M, Humbel BM
    Ref: Journal of Cell Biology, 110:669, 1990 : PubMed

            

    Title: Molecular analysis of a developmentally regulated gene required for Dictyostelium aggregation
    Rubino S, Mann SK, Hori RT, Pinko C, Firtel RA
    Ref: Developmental Biology, 131:27, 1989 : PubMed

            

no Image
no Structure
&gt; List of Gene_Locus for Cholinesterase-like (555)


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FamilyFungal_carboxylesterase_lipaseParent FamilyCarboxylesterase
CommentThis family was extracted from the previous Carboxylesterase COesterase family. Carboxylesterase, type B (COesterase) is very successful in fungi. Grouped with Lipase_3 in Family Fungal lipases in scop database. This family corresponds to the Carbohydrate Esterase family CE10 in CAZy - Carbohydrate-Active enZYmes database (CE_10) LED_Database abH03 abH02. The presence of a water/lipid interface dramatically enhances the hydrolytic activity of lipases. The activation is associated with a conformational change. The Ser-His-Asp/Glu catalytic triad is occluded by a polypeptide flap (lid) and is not exposed to the solvent until the lid is open. A protein of this family lacking the catalytic serine is a dirigent protein which controls the stereoselectivity of multicopper oxidase(VdtB)-catalyzed phenol coupling in viriditoxin biosynthesis (Hu et al. 2019)
InterproIPR002018 (Carboxylesterase, type B)Pdoc PDOC00112
PFamPF00135 (COesterase)PrintsProsite PS00122, PS00941
ECAt KYOTO 3.1.1.3 at NYCEZYME 3.1.1.3Tables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Fungal Dirigent Protein Controls the Stereoselectivity of Multicopper Oxidase-Catalyzed Phenol Coupling in Viriditoxin Biosynthesis
    Hu J, Li H, Chooi YH
    Ref: Journal of the American Chemical Society, 141:8068, 2019 : PubMed

            

    Title: Structural traits and catalytic versatility of the lipases from the Candida rugosa-like family: A review
    Barriuso J, Vaquero ME, Prieto A, Martinez MJ
    Ref: Biotechnol Adv, 34:874, 2016 : PubMed

            

    Title: Crystal structures of Ophiostoma piceae sterol esterase: Structural insights into activation mechanism and product release
    Gutierrez-Fernandez J, Vaquero ME, Prieto A, Barriuso J, Martinez MJ, Hermoso JA
    Ref: J Struct Biol, 187:215, 2014 : PubMed

            

    Title: Insights into the molecular basis of chiral acid recognition by Candida rugosa lipase from an X-ray crystal structure of a bound phosphonate transition state analog
    Colton IJ, Yin DT, Grochulski P, Kazlauskas RJ
    Ref: Adv Synth Catal, 353:2529, 2011 : PubMed

            

    Title: Aspergillus niger protein EstA defines a new class of fungal esterases within the alpha/beta hydrolase fold superfamily of proteins
    Bourne Y, Hasper AA, Chahinian H, Juin M, De Graaff LH, Marchot P
    Ref: Structure, 12:677, 2004 : PubMed

            

    Title: Defining substrate characteristics from 3D structure; perspective on EstA structure
    Schrag JD, Cygler M
    Ref: Structure, 12:521, 2004 : PubMed

            

    Title: Structural insights into the lipase/esterase behavior in the Candida rugosa lipases family: crystal structure of the lipase 2 isoenzyme at 1.97A resolution
    Mancheno JM, Pernas MA, Martinez MJ, Ochoa B, Rua ML, Hermoso JA
    Ref: Journal of Molecular Biology, 332:1059, 2003 : PubMed

            

    Title: Three-dimensional structure of homodimeric cholesterol esterase-ligand complex at 1.4 A resolution
    Pletnev V, Addlagatta A, Wawrzak Z, Duax W
    Ref: Acta Crystallographica D Biol Crystallogr, 59:50, 2003 : PubMed

            

    Title: Structure of uncomplexed and linoleate-bound Candida cylindracea cholesterol esterase
    Ghosh D, Wawrzak Z, Pletnev VZ, Li N, Kaiser R, Pangborn W, Jornvall H, Erman M, Duax WL
    Ref: Structure, 3:279, 1995 : PubMed

            

    Title: A structural basis for the chiral preferences of lipases
    Cygler M, Grochulski P, Kazlauskas RJ, Schrag JD, Bouthillier F, Rubin B, Serreqi AN, Gupta AK
    Ref: Journal of the American Chemical Society, 116:3180, 1994 : PubMed

            

    Title: Analogs of reaction intermediates identify a unique substrate binding site in Candida rugosa lipase
    Grochulski P, Bouthillier F, Kazlauskas RJ, Serreqi AN, Schrag JD, Ziomek E, Cygler M
    Ref: Biochemistry, 33:3494, 1994 : PubMed

            

    Title: Insights into interfacial activation from an open structure of Candida rugosa lipase
    Grochulski P, Li Y, Schrag JD, Bouthillier F, Smith P, Harrison D, Rubin B, Cygler M
    Ref: Journal of Biological Chemistry, 268:12843, 1993 : PubMed

            

    Title: 1.8 A refined structure of the lipase from Geotrichum candidum
    Schrag JD, Cygler M
    Ref: Journal of Molecular Biology, 230:575, 1993 : PubMed

            

&gt; Structure scheme for Fungal_carboxylesterase_lipase
&gt; Structures for Fungal_carboxylesterase_lipase (16)
&gt; List of Gene_Locus for Fungal_carboxylesterase_lipase (4895)


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FamilyGliotactinParent FamilyNon-catalytic_C
CommentGliotactin, a transmembrane protein on peripheral glia, is required to form the blood-nerve barrier in Drosophila. It is a marker of tricellular junctions, is necessary for septate junction development in Drosophila. Gliotactin and Discs large form a protein complex at the tricellular junction of polarized epithelial cells in Drosophila. The intracellular domain of gliotactin, is natively unfolded. Control of Gliotactin localization and levels by tyrosine phosphorylation and endocytosis is necessary for survival of polarized epithelia
InterproIPR002018 (Carboxylesterase, type B)Pdoc
PFamPF00135 (COesterase)PrintsProsite
EC no EC numberTables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Interplay between Anakonda, Gliotactin, and M6 for Tricellular Junction Assembly and Anchoring of Septate Junctions in Drosophila Epithelium
    Esmangart de Bournonville T, Le Borgne R
    Ref: Current Biology, 30:4245, 2020 : PubMed

            

    Title: The Transmembrane Proteins M6 and Anakonda Cooperate to Initiate Tricellular Junction Assembly in Epithelia of Drosophila
    Wittek A, Hollmann M, Schleutker R, Luschnig S
    Ref: Current Biology, 30:4254, 2020 : PubMed

            

    Title: Mutations in Caenorhabditis elegans neuroligin-like glit-1, the apoptosis pathway and the calcium chaperone crt-1 increase dopaminergic neurodegeneration after 6-OHDA treatment
    Offenburger SL, Jongsma E, Gartner A
    Ref: PLoS Genet, 14:e1007106, 2018 : PubMed

            

    Title: C-terminal Src kinase (Csk) regulates the tricellular junction protein Gliotactin independent of Src
    Samarasekera G, Auld VJ
    Ref: Mol Biology of the cell, 29:123, 2018 : PubMed

            

    Title: The Drosophila tricellular junction protein Gliotactin regulates its own mRNA levels through BMP-mediated induction of miR-184
    Sharifkhodaei Z, Padash-Barmchi M, Gilbert MM, Samarasekera G, Fulga TA, Van Vactor D, Auld VJ
    Ref: Journal of Cell Science, 129:1477, 2016 : PubMed

            

    Title: Control of Gliotactin localization and levels by tyrosine phosphorylation and endocytosis is necessary for survival of polarized epithelia
    Padash-Barmchi M, Browne K, Sturgeon K, Jusiak B, Auld VJ
    Ref: Journal of Cell Science, 123:4052, 2010 : PubMed

            

    Title: Gliotactin and Discs large form a protein complex at the tricellular junction of polarized epithelial cells in Drosophila
    Schulte J, Charish K, Que J, Ravn S, MacKinnon C, Auld VJ
    Ref: Journal of Cell Science, 119:4391, 2006 : PubMed

            

    Title: Neuroglian, Gliotactin, and the Na+/K+ ATPase are essential for septate junction function in Drosophila
    Genova JL, Fehon RG
    Ref: Journal of Cell Biology, 161:979, 2003 : PubMed

            

    Title: Gliotactin, a novel marker of tricellular junctions, is necessary for septate junction development in Drosophila
    Schulte J, Tepass U, Auld VJ
    Ref: Journal of Cell Biology, 161:991, 2003 : PubMed

            

    Title: The intracellular domain of the Drosophila cholinesterase-like neural adhesion protein, gliotactin, is natively unfolded
    Zeev-Ben-Mordehai T, Rydberg EH, Solomon A, Toker L, Auld VJ, Silman I, Botti SA, Sussman JL
    Ref: Proteins, 53:758, 2003 : PubMed

            

    Title: Gliotactin, a novel transmembrane protein on peripheral glia, is required to form the blood-nerve barrier in Drosophila
    Auld VJ, Fetter RD, Broadie K, Goodman CS
    Ref: Cell, 81:757, 1995 : PubMed

            

no Image
no Structure
&gt; List of Gene_Locus for Gliotactin (108)


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FamilyGlutactinParent FamilyNon-catalytic_C
CommentInsect specific protein. Glutactin has a signal peptide and an amino domain of greater than 500 residues that strongly resembles acetylcholine esterases and other serine esterases, but lacks the catalytically critical serine residue. It is located at embryonic basement membranes, particularly to the sequentially invaginated envelope of the central nervous system, muscle apodemes and dorsal median cell processes. Ectopic expression of Glutactin inhibits synapse formation by motor neurons that normally innervate M12 muscle. Only the N-terminal part of Glutactin is a member of the alpha/beta hydrolase family. The C-terminal part is not included in ESTHER
InterproIPR002018 (Carboxylesterase, type B)Pdoc
PFamPF00135 (COesterase)PrintsProsite
EC no EC numberTables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Wnt4 is a local repulsive cue that determines synaptic target specificity.
    Inaki M, Yoshikawa S, Thomas JB, Aburatani H, Nose A
    Ref: Current Biology, 17:1574, 2007 : PubMed

            

    Title: The structure-function relationships in Drosophila neurotactin show that cholinesterasic domains may have adhesive properties
    Darboux I, Barthalay Y, Piovant M, Hipeau-Jacquotte R
    Ref: EMBO Journal, 15:4835, 1996 : PubMed

            

    Title: Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid
    Krejci E, Duval N, Chatonnet A, Vincens P, Massoulie J
    Ref: Proceedings of the National Academy of Sciences of the United States of America, 88:6647, 1991 : PubMed

            

    Title: Glutactin, a novel Drosophila basement membrane-related glycoprotein with sequence similarity to serine esterases
    Olson PF, Fessler LI, Nelson RE, Sterne RE, Campbell AG, Fessler JH
    Ref: EMBO Journal, 9:1219, 1990 : PubMed

            

no Image
no Structure
&gt; List of Gene_Locus for Glutactin (49)


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FamilyJuvenile_hormone_esteraseParent FamilyCarboxylesterase
CommentJuvenile hormone JH is an insect hormone containing an alpha,beta-unsaturated ester consisting of a small alcohol and long hydrophobic acid. JH degradation is required for proper insect development. One pathway of this degradation is through juvenile hormone esterase JHE which cleaves the JH ester bond to produce methanol and JH acid. Another way of degradation of JH is epoxyde hydrolysis. Most insect species contain only juvenile hormone (JH) III. To date JH 0, JH I, and JH II have been identified only in the Lepidoptera (butterflies and moths). The form JHB3 (JH III bisepoxide) appears to be the most important JH in the Diptera, or flies. Certain species of crustaceans have been shown to produce and secrete methyl farnesoate, which is juvenile hormone III lacking the epoxide group. Methyl farnesoate is believed to play a role similar to that of JH in crustaceans. In drosophila DmJHE is the hormone esterase with precise regulation and highly specific activity for its substrate, juvenile hormone. DmJHEdup is an odorant degrading esterase (ODE) responsible for processing various kairomones in antennae
InterproIPR002018 (Carboxylesterase, type B)Pdoc
PFamPF00135 (COesterase)PrintsProsite PS00122, PS00941
ECAt KYOTO 3.1.1.59 at NYCEZYME 3.1.1.59Tables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: The molecular basis for the neofunctionalization of the juvenile hormone esterase duplication in Drosophila
    Hopkins DH, Rane RV, Younus F, Coppin CW, Pandey G, Jackson CJ, Oakeshott JG
    Ref: Insect Biochemistry & Molecular Biology, 106:10, 2019 : PubMed

            

    Title: Juvenile hormone esterase: biochemistry and structure
    Kamita SG, Hammock BD
    Ref: Journal of Pesticide Science, 35:265, 2010 : PubMed

            

    Title: Structural studies of a potent insect maturation inhibitor bound to the juvenile hormone esterase of Manduca sexta
    Wogulis M, Wheelock CE, Kamita SG, Hinton AC, Whetstone PA, Hammock BD, Wilson DK
    Ref: Biochemistry, 45:4045, 2006 : PubMed

            

no Image
&gt; Structures for Juvenile_hormone_esterase (1)
&gt; List of Gene_Locus for Juvenile_hormone_esterase (124)


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FamilyNeuroliginParent FamilyNon-catalytic_C
CommentNeuroligins constitute a family of proteins thought to mediate cell-to-cell interactions between neurons. Neuroligins function as ligands for the neurexin family and MADD-4. This interaction is necessary for GABA receptors clustering. Mammals have four Nlgn proteins, with the Nlgn3 and Nlgn4 gene in humans localised to the X-chromosome. In humans, the Nlgn4 gene is complemented on the Y-chromosome by a similar Nlgn4Y gene.(from OMIM) In 2 brothers with autism, one with typical autism and the other with Asperger syndrome, Jamain et al. (2003) identified a frameshift mutation (1186T) in the human-NLGN4X gene, resulting in a stop codon at position 396 and premature truncation of the protein before the transmembrane domain. The mutation was present in the mother and absent in an unaffected brother and 350 controls. See other contradictory results Gauthier et al. Vincent et al., but other mutations found Laumonnier et al. Yan et al. Incomplete penetrance suspected for some mutations. In 2 brothers with autism, one with typical autism and the other with Asperger syndrome, Jamain et al. (2003) identified a mutation R451C in the human-NLGN3 gene. arg451 in NLGN3, arg386 in BCHE, and arg395 in ACHE are conserved in mammalian species. In cellular transfection studies, De Jaco et al. (2006) inserted mutations homologous to the NLGN3 R451C mutation in BCHE and ACHE cDNAs and found that these mutations resulted in endoplasmic reticulum retention of the 2 proteins, similar to that observed with the NLGN3 R451C mutant protein. Tabuchi et al. (2007) introduced the R451C substitution in neuroligin-3 into mice. R451C mutant mice showed impaired social interactions but enhanced spatial learning abilities. Unexpectedly these behavioral changes were accompanied by an increase in inhibitory synaptic transmission with no apparent effect on excitatory synapses. Deletion of neuroligin-3, in contrast, did not cause such changes, indicating that the R451C substitution represents a gain-of-function mutation. Tabuchi et al. (2007) concluded that increased inhibitory synaptic transmission may contribute to human autism spectrum disorders and that the R451C knockin mice may be a useful model for studying autism-related behaviors. Recently Venkatesh et al. showed that neuronal activity promotes glioma growth through Neuroligin-3 secretion. Recently Neuroligin 2 mutations were associated with anxiety, autism, intellectual disability, hyperphagia, and obesity.Many mutations on X-linked cell NLGN4X result in ASD or intellectual disability. NLGN4Y cannot compensate for the functional deficits due to NLGN4X mutations
InterproIPR000460 (Neuroligin), IPR030022 (Neuroligin-1), IPR030023 (Neuroligin-2), IPR030024 (Neuroligin-3), IPR030025 (Neuroligin-4), IPR002018 (Carboxylesterase, type B)Pdoc
PFamPF00135 (COesterase)PrintsProsite
EC no EC numberTables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Of Humans and Gerbils- Independent Diversification of Neuroligin-4 Into X- and Y-Specific Genes in Primates and Rodents
    Maxeiner S, Benseler F, Brose N, Krasteva-Christ G
    Ref: Front Mol Neurosci, 15:838262, 2022 : PubMed

            

    Title: Cochlear ribbon synapse maturation requires Nlgn1 and Nlgn3
    Ramirez MA, Ninoyu Y, Miller C, Andrade LR, Edassery S, Bomba-Warczak E, Ortega B, Manor U, Rutherford MA and Savas JN <1 more author(s)>
    Ref: iScience, 25:104803, 2022 : PubMed

            

    Title: A Cluster of Autism-Associated Variants on X-Linked NLGN4X Functionally Resemble NLGN4Y
    Nguyen TA, Wu K, Pandey S, Lehr AW, Li Y, Bemben MA, Badger JD, 2nd, Lauzon JL, Wang T and Roche KW <4 more author(s)>
    Ref: Neuron, 106:759, 2020 : PubMed

            

    Title: The neuroligins and the synaptic pathway in Autism Spectrum Disorder
    Trobiani L, Meringolo M, Diamanti T, Bourne Y, Marchot P, Martella G, Dini L, Pisani A, De Jaco A, Bonsi P
    Ref: Neurosci Biobehav Rev, 119:37, 2020 : PubMed

            

    Title: Neuroligin 2 nonsense variant associated with anxiety, autism, intellectual disability, hyperphagia, and obesity
    Parente DJ, Garriga C, Baskin B, Douglas G, Cho MT, Araujo GC, Shinawi M
    Ref: American Journal of Medicine Genet A, 173:213, 2017 : PubMed

            

    Title: MADD-4/Punctin and Neurexin Organize C. elegans GABAergic Postsynapses through Neuroligin
    Maro GS, Gao S, Olechwier AM, Hung WL, Liu M, Ozkan E, Zhen M, Shen K
    Ref: Neuron, 86:1420, 2015 : PubMed

            

    Title: C. elegans Punctin Clusters GABA Receptors via Neuroligin Binding and UNC-40/DCC Recruitment
    Tu H, Pinan-Lucarre B, Ji T, Jospin M, Bessereau JL
    Ref: Neuron, 86:1407, 2015 : PubMed

            

    Title: Neuronal Activity Promotes Glioma Growth through Neuroligin-3 Secretion
    Venkatesh HS, Johung TB, Caretti V, Noll A, Tang Y, Nagaraja S, Gibson EM, Mount CW, Polepalli J and Monje M <6 more author(s)>
    Ref: Cell, 161:803, 2015 : PubMed

            

    Title: Tracking the origin and divergence of cholinesterases and neuroligins: the evolution of synaptic proteins
    Lenfant N, Hotelier T, Bourne Y, Marchot P, Chatonnet A
    Ref: Journal of Molecular Neuroscience, 53:362, 2014 : PubMed

            

    Title: Beyond the random coil: stochastic conformational switching in intrinsically disordered proteins
    Choi UB, McCann JJ, Weninger KR, Bowen ME
    Ref: Structure, 19:566, 2011 : PubMed

            

    Title: Identification and functional characterization of rare mutations of the neuroligin-2 gene (NLGN2) associated with schizophrenia
    Sun C, Cheng MC, Qin R, Liao DL, Chen TT, Koong FJ, Chen G, Chen CH
    Ref: Hum Mol Genet, 20:3042, 2011 : PubMed

            

    Title: Neurexin Ibeta and neuroligin are localized on opposite membranes in mature central synapses
    Berninghausen O, Rahman MA, Silva JP, Davletov B, Hopkins C, Ushkaryov YA
    Ref: Journal of Neurochemistry, 103:1855, 2007 : PubMed

            

    Title: Neuroligin-3 is a neuronal adhesion protein at GABAergic and glutamatergic synapses
    Budreck EC, Scheiffele P
    Ref: European Journal of Neuroscience, 26:1738, 2007 : PubMed

            

    Title: Synaptic arrangement of the neuroligin/beta-neurexin complex revealed by X-ray and neutron scattering
    Comoletti D, Grishaev A, Whitten AE, Tsigelny I, Taylor P, Trewhella J
    Ref: Structure, 15:693, 2007 : PubMed

            

    Title: Neurexin-neuroligin signaling in synapse development
    Craig AM, Kang Y
    Ref: Current Opinion in Neurobiology, 17:43, 2007 : PubMed

            

    Title: Medicine. Testing hypotheses about autism
    Crawley JN
    Ref: Science, 318:56, 2007 : PubMed

            

    Title: Neuroscience. Autism's cause may reside in abnormalities at the synapse
    Garber K
    Ref: Science, 317:190, 2007 : PubMed

            

    Title: Adhesion molecules in the nervous system: structural insights into function and diversity
    Shapiro L, Love J, Colman DR
    Ref: Annual Review of Neuroscience, 30:451, 2007 : PubMed

            

    Title: A neuroligin-3 mutation implicated in autism increases inhibitory synaptic transmission in mice
    Tabuchi K, Blundell J, Etherton MR, Hammer RE, Liu X, Powell CM, Sudhof TC
    Ref: Science, 318:71, 2007 : PubMed

            

    Title: Neuroligins 3 and 4X interact with syntrophin-gamma2, and the interactions are affected by autism-related mutations
    Yamakawa H, Oyama S, Mitsuhashi H, Sasagawa N, Uchino S, Kohsaka S, Ishiura S
    Ref: Biochemical & Biophysical Research Communications, 355:41, 2007 : PubMed

            

    Title: Control of excitatory and inhibitory synapse formation by neuroligins
    Chih B, Engelman H, Scheiffele P
    Ref: Science, 307:1324, 2005 : PubMed

            

    Title: NLGN3/NLGN4 gene mutations are not responsible for autism in the Quebec population
    Gauthier J, Bonnel A, St-Onge J, Karemera L, Laurent S, Mottron L, Fombonne E, Joober R, Rouleau GA
    Ref: American Journal of Medicine Genet B Neuropsychiatr Genet, 132B:74, 2005 : PubMed

            

    Title: Neuroligins mediate excitatory and inhibitory synapse formation: involvement of PSD-95 and neurexin-1beta in neuroligin-induced synaptic specificity
    Levinson JN, Chery N, Huang K, Wong TP, Gerrow K, Kang R, Prange O, Wang YT, El-Husseini A
    Ref: Journal of Biological Chemistry, 280:17312, 2005 : PubMed

            

    Title: Selective capability of SynCAM and neuroligin for functional synapse assembly
    Sara Y, Biederer T, Atasoy D, Chubykin AA, Mozhayeva MG, Sudhof TC, Kavalali ET
    Ref: Journal of Neuroscience, 25:260, 2005 : PubMed

            

    Title: Analysis of the neuroligin 3 and 4 genes in autism and other neuropsychiatric patients
    Yan J, Oliveira G, Coutinho A, Yang C, Feng J, Katz C, Sram J, Bockholt A, Jones IR and Sommer SS <3 more author(s)>
    Ref: Mol Psychiatry, 10:329, 2005 : PubMed

            

    Title: Analysis of four neuroligin genes as candidates for autism
    Ylisaukko-oja T, Rehnstrom K, Auranen M, Vanhala R, Alen R, Kempas E, Ellonen P, Turunen JA, Makkonen I and Jarvela I <4 more author(s)>
    Ref: Eur J Hum Genet, 13:1285, 2005 : PubMed

            

    Title: Disorder-associated mutations lead to functional inactivation of neuroligins
    Chih B, Afridi SK, Clark L, Scheiffele P
    Ref: Hum Mol Genet, 13:1471, 2004 : PubMed

            

    Title: The Arg451Cys-neuroligin-3 mutation associated with autism reveals a defect in protein processing
    Comoletti D, De Jaco A, Jennings LL, Flynn RE, Gaietta G, Tsigelny I, Ellisman MH, Taylor P
    Ref: Journal of Neuroscience, 24:4889, 2004 : PubMed

            

    Title: Excessive expression of acetylcholinesterase impairs glutamatergic synaptogenesis in hippocampal neurons
    Dong H, Xiang YY, Farchi N, Ju W, Wu Y, Chen L, Wang Y, Hochner B, Yang B and Lu WY <1 more author(s)>
    Ref: Journal of Neuroscience, 24:8950, 2004 : PubMed

            

    Title: Synaptic targeting of neuroligin is independent of neurexin and SAP90/PSD95 binding
    Dresbach T, Neeb A, Meyer G, Gundelfinger ED, Brose N
    Ref: Molecular & Cellular Neurosciences, 27:227, 2004 : PubMed

            

    Title: Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins
    Graf ER, Zhang X, Jin SX, Linhoff MW, Craig AM
    Ref: Cell, 119:1013, 2004 : PubMed

            

    Title: Synaptic scaffolding molecule interacts with axin
    Hirabayashi S, Nishimura W, Iida J, Kansaku A, Kishida S, Kikuchi A, Tanaka N, Hata Y
    Ref: Journal of Neurochemistry, 90:332, 2004 : PubMed

            

    Title: Structural characterization of recombinant soluble rat neuroligin 1: mapping of secondary structure and glycosylation by mass spectrometry
    Hoffman RC, Jennings LL, Tsigelny I, Comoletti D, Flynn RE, Sudhof TC, Taylor P
    Ref: Biochemistry, 43:1496, 2004 : PubMed

            

    Title: Synaptic scaffolding molecule is involved in the synaptic clustering of neuroligin
    Iida J, Hirabayashi S, Sato Y, Hata Y
    Ref: Molecular & Cellular Neurosciences, 27:497, 2004 : PubMed

            

    Title: X-linked mental retardation and autism are associated with a mutation in the NLGN4 gene, a member of the neuroligin family
    Laumonnier F, Bonnet-Brilhault F, Gomot M, Blanc R, David A, Moizard MP, Raynaud M, Ronce N, Lemonnier E and Briault S <9 more author(s)>
    Ref: American Journal of Human Genetics, 74:552, 2004 : PubMed

            

    Title: The complexity of PDZ domain-mediated interactions at glutamatergic synapses: a case study on neuroligin
    Meyer G, Varoqueaux F, Neeb A, Oschlies M, Brose N
    Ref: Neuropharmacology, 47:724, 2004 : PubMed

            

    Title: A balance between excitatory and inhibitory synapses is controlled by PSD-95 and neuroligin
    Prange O, Wong TP, Gerrow K, Wang YT, El-Husseini A
    Ref: Proc Natl Acad Sci U S A, 101:13915, 2004 : PubMed

            

    Title: Do known mutations in neuroligin genes (NLGN3 and NLGN4) cause autism?
    Talebizadeh Z, Bittel DC, Veatch OJ, Butler MG, Takahashi TN, Miles JH
    Ref: J Autism Dev Disord, 34:735, 2004 : PubMed

            

    Title: Neuroligin 2 is exclusively localized to inhibitory synapses
    Varoqueaux F, Jamain S, Brose N
    Ref: European Journal of Cell Biology, 83:449, 2004 : PubMed

            

    Title: Mutation screening of X-chromosomal neuroligin genes: no mutations in 196 autism probands
    Vincent JB, Kolozsvari D, Roberts WS, Bolton PF, Gurling HM, Scherer SW
    Ref: American Journal of Medicine Genet B Neuropsychiatr Genet, 129B:82, 2004 : PubMed

            

    Title: Characterization of the interaction of a recombinant soluble neuroligin-1 with neurexin-1beta
    Comoletti D, Flynn RE, Jennings LL, Chubykin AA, Matsumura T, Hasegawa H, Sudhof TC, Taylor P
    Ref: Journal of Biological Chemistry, 278:50497, 2003 : PubMed

            

    Title: Neurexin mediates the assembly of presynaptic terminals
    Dean C, Scholl FG, Choih J, DeMaria S, Berger J, Isacoff E, Scheiffele P
    Ref: Nat Neurosci, 6:708, 2003 : PubMed

            

    Title: Functional excitatory synapses in HEK293 cells expressing neuroligin and glutamate receptors
    Fu Z, Washbourne P, Ortinski P, Vicini S
    Ref: Journal of Neurophysiology, 90:3950, 2003 : PubMed

            

    Title: Mutations of the X-linked genes encoding neuroligins NLGN3 and NLGN4 are associated with autism
    Jamain S, Quach H, Betancur C, Rastam M, Colineaux C, Gillberg IC, Soderstrom H, Giros B, Leboyer M and Bourgeron T <1 more author(s)>
    Ref: Nat Genet, 34:27, 2003 : PubMed

            

    Title: Synaptic adhesion molecules
    Yamagata M, Sanes JR, Weiner JA
    Ref: Current Opinion in Cell Biology, 15:621, 2003 : PubMed

            

    Title: Expression of neurexin ligands, the neuroligins and the neurexophilins, in the developing and adult rodent olfactory bulb
    Clarris HJ, McKeown S, Key B
    Ref: Int J Developmental Biology, 46:649, 2002 : PubMed

            

    Title: Identification of a novel neuroligin in humans which binds to PSD-95 and has a widespread expression
    Bolliger MF, Frei K, Winterhalter KH, Gloor SM
    Ref: Biochemical Journal, 356:581, 2001 : PubMed

            

    Title: Neuroligin 3 is a vertebrate gliotactin expressed in the olfactory ensheathing glia, a growth-promoting class of macroglia
    Gilbert M, Smith J, Roskams AJ, Auld VJ
    Ref: Glia, 34:151, 2001 : PubMed

            

    Title: A stoichiometric complex of neurexins and dystroglycan in brain
    Sugita S, Saito F, Tang J, Satz J, Campbell K, Sudhof TC
    Ref: Journal of Cell Biology, 154:435, 2001 : PubMed

            

    Title: Synapse formation: if it looks like a duck and quacks like a duck
    Cantallops I, Cline HT
    Ref: Current Biology, 10:R620, 2000 : PubMed

            

    Title: The structure and expression of the human neuroligin-3 gene
    Philibert RA, Winfield SL, Sandhu HK, Martin BM, Ginns EI
    Ref: Gene, 246:303, 2000 : PubMed

            

    Title: Neuroligation: building synapses around the neurexin-neuroligin link
    Rao A, Harms KJ, Craig AM
    Ref: Nat Neurosci, 3:747, 2000 : PubMed

            

    Title: Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons
    Scheiffele P, Fan J, Choih J, Fetter R, Serafini T
    Ref: Cell, 101:657, 2000 : PubMed

            

    Title: Common EF-hand motifs in cholinesterases and neuroligins suggest a role for Ca2+ binding in cell surface associations
    Tsigelny I, Shindyalov IN, Bourne PE, Sudhof TC, Taylor P
    Ref: Protein Science, 9:180, 2000 : PubMed

            

    Title: Synaptic cell adhesion proteins and synaptogenesis in the mammalian central nervous system
    Brose N
    Ref: Naturwissenschaften, 86:516, 1999 : PubMed

            

    Title: Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses
    Song JY, Ichtchenko K, Sudhof TC, Brose N
    Ref: Proc Natl Acad Sci U S A, 96:1100, 1999 : PubMed

            

    Title: Functional redundancy of acetylcholinesterase and neuroligin in mammalian neuritogenesis
    Grifman M, Galyam N, Seidman S, Soreq H
    Ref: Proc Natl Acad Sci U S A, 95:13935, 1998 : PubMed

            

    Title: CIPP, a novel multivalent PDZ domain protein, selectively interacts with Kir4.0 family members, NMDA receptor subunits, neurexins, and neuroligins
    Kurschner C, Mermelstein PG, Holden WT, Surmeier DJ
    Ref: Molecular & Cellular Neurosciences, 11:161, 1998 : PubMed

            

    Title: The making of neurexins
    Missler M, Fernandez-Chacon R, Sudhof TC
    Ref: Journal of Neurochemistry, 71:1339, 1998 : PubMed

            

    Title: Acetylcholinesterase-transgenic mice display embryonic modulations in spinal cord choline acetyltransferase and neurexin Ibeta gene expression followed by late-onset neuromotor deterioration
    Andres C, Beeri R, Friedman A, Lev-Lehman E, Henis S, Timberg R, Shani M, Soreq H
    Ref: Proc Natl Acad Sci U S A, 94:8173, 1997 : PubMed

            

    Title: Binding of neuroligins to PSD-95
    Irie M, Hata Y, Takeuchi M, Ichtchenko K, Toyoda A, Hirao K, Takai Y, Rosahl TW, Sudhof TC
    Ref: Science, 277:1511, 1997 : PubMed

            

    Title: Binding properties of neuroligin 1 and neurexin 1beta reveal function as heterophilic cell adhesion molecules
    Nguyen T, Sudhof TC
    Ref: Journal of Biological Chemistry, 272:26032, 1997 : PubMed

            

    Title: Structures, alternative splicing, and neurexin binding of multiple neuroligins
    Ichtchenko K, Nguyen T, Sudhof TC
    Ref: Journal of Biological Chemistry, 271:2676, 1996 : PubMed

            

    Title: Neuroligin 1: a splice site-specific ligand for beta-neurexins
    Ichtchenko K, Hata Y, Nguyen T, Ullrich B, Missler M, Moomaw C, Sudhof TC
    Ref: Cell, 81:435, 1995 : PubMed

            

&gt; Structure scheme for Neuroligin
&gt; Structures for Neuroligin (14)
&gt; List of Gene_Locus for Neuroligin (517)


Top
FamilyNeurotactinParent FamilyNon-catalytic_C
CommentOnly the C-terminal part of Neurotactin is a member of the alpha/beta hydrolase family. The N-terminal part of Neurotactin has low complexity is desordered and is intracellular. Neurotactin is found only in arthropods Neurotactin is only detected during cell proliferation and differentiation, and it is found mainly in neural tissue and also in mesoderm and imaginal discs. Neurotactin has a large cytoplasmic domain rich in charged residues and an extracellular domain similar to cholinesterase that lacks the active site serine required for esterase activity. Amalgam is a ligand for the transmembrane receptor neurotactin and is required for neurotactin-mediated cell adhesion and axon fasciculation in Drosophila. Mutants of neurotactin revealed specific requirements for neurotactin during axon outgrowth, fasciculation, and guidance.
InterproIPR002018 (Carboxylesterase, type B)Pdoc
PFamPF00135 (COesterase)PrintsProsite
EC no EC numberTables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: The quaternary structure of amalgam, a Drosophila neuronal adhesion protein, explains its dual adhesion properties
    Zeev-Ben-Mordehai T, Mylonas E, Paz A, Peleg Y, Toker L, Silman I, Svergun DI, Sussman JL
    Ref: Biophysical Journal, 97:2316, 2009 : PubMed

            

    Title: Amalgam, an axon guidance Drosophila adhesion protein belonging to the immunoglobulin superfamily: over-expression, purification and biophysical characterization
    Zeev-Ben-Mordehai T, Paz A, Peleg Y, Toker L, Wolf SG, Rydberg EH, Sussman JL, Silman I
    Ref: Protein Expr Purif, 63:147, 2009 : PubMed

            

    Title: Developmental architecture of adult-specific lineages in the ventral CNS of Drosophila
    Truman JW, Schuppe H, Shepherd D, Williams DW
    Ref: Development, 131:5167, 2004 : PubMed

            

    Title: Interactions between the secreted protein Amalgam, its transmembrane receptor Neurotactin and the Abelson tyrosine kinase affect axon pathfinding
    Liebl EC, Rowe RG, Forsthoefel DJ, Stammler AL, Schmidt ER, Turski M, Seeger MA
    Ref: Development, 130:3217, 2003 : PubMed

            

    Title: Amalgam is a ligand for the transmembrane receptor neurotactin and is required for neurotactin-mediated cell adhesion and axon fasciculation in Drosophila
    Fremion F, Darboux I, Diano M, Hipeau-Jacquotte R, Seeger MA, Piovant M
    Ref: EMBO Journal, 19:4463, 2000 : PubMed

            

    Title: Neurotactin functions in concert with other identified CAMs in growth cone guidance in Drosophila
    Speicher S, Garci-Alonso L, Carmena A, Martin-Bermudo MD, de la Escalera S, Jimenez F
    Ref: Neuron, 20:221, 1998 : PubMed

            

    Title: The structure-function relationships in Drosophila neurotactin show that cholinesterasic domains may have adhesive properties
    Darboux I, Barthalay Y, Piovant M, Hipeau-Jacquotte R
    Ref: EMBO Journal, 15:4835, 1996 : PubMed

            

    Title: Drosophila neurotactin mediates heterophilic cell adhesion
    Barthalay Y, Hipeau-Jacquotte R, de la Escalera S, Jimenez F, Piovant M
    Ref: EMBO Journal, 9:3603, 1990 : PubMed

            

    Title: Drosophila neurotactin, a surface glycoprotein with homology to serine esterases, is dynamically expressed during embryogenesis
    Hortsch M, Patel NH, Bieber AJ, Traquina ZR, Goodman CS
    Ref: Development, 110 (4):1327, 1990 : PubMed

            

    Title: Characterization and gene cloning of neurotactin, a Drosophila transmembrane protein related to cholinesterases
    de la Escalera S, Bockamp EO, Moya F, Piovant M, Jimenez F
    Ref: EMBO Journal, 9:3593, 1990 : PubMed

            

no Image
no Structure
&gt; List of Gene_Locus for Neurotactin (60)


Top
FamilyNon-catalytic_CChildren FamilyOtherNon-catalytic_C, Neuroligin, Thyroglobulin, Neurotactin, Gliotactin, Glutactin
CommentThis family contains genes/protein of the COesterase group which lack some of the active site residues (neuroligins, neurotactin, gliotactin, glutactin)
InterproIPR002018 (Carboxylesterase, type B)Pdoc PDOC00112
PFamPF00135 (COesterase)PrintsProsite PS00122, PS00941
EC no EC numberTables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: The structure-function relationships in Drosophila neurotactin show that cholinesterasic domains may have adhesive properties
    Darboux I, Barthalay Y, Piovant M, Hipeau-Jacquotte R
    Ref: EMBO Journal, 15:4835, 1996 : PubMed

            

    Title: Gliotactin, a novel transmembrane protein on peripheral glia, is required to form the blood-nerve barrier in Drosophila
    Auld VJ, Fetter RD, Broadie K, Goodman CS
    Ref: Cell, 81:757, 1995 : PubMed

            

    Title: Neuroligin 1: a splice site-specific ligand for beta-neurexins
    Ichtchenko K, Hata Y, Nguyen T, Ullrich B, Missler M, Moomaw C, Sudhof TC
    Ref: Cell, 81:435, 1995 : PubMed

            

    Title: Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid
    Krejci E, Duval N, Chatonnet A, Vincens P, Massoulie J
    Ref: Proceedings of the National Academy of Sciences of the United States of America, 88:6647, 1991 : PubMed

            

    Title: Drosophila neurotactin, a surface glycoprotein with homology to serine esterases, is dynamically expressed during embryogenesis
    Hortsch M, Patel NH, Bieber AJ, Traquina ZR, Goodman CS
    Ref: Development, 110 (4):1327, 1990 : PubMed

            

    Title: Glutactin, a novel Drosophila basement membrane-related glycoprotein with sequence similarity to serine esterases
    Olson PF, Fessler LI, Nelson RE, Sterne RE, Campbell AG, Fessler JH
    Ref: EMBO Journal, 9:1219, 1990 : PubMed

            

    Title: Characterization and gene cloning of neurotactin, a Drosophila transmembrane protein related to cholinesterases
    de la Escalera S, Bockamp EO, Moya F, Piovant M, Jimenez F
    Ref: EMBO Journal, 9:3593, 1990 : PubMed

            

    Title: Primary structure of human thyroglobulin deduced from the sequence of its 8448-base complementary DNA
    Malthiery Y, Lissitzky S
    Ref: European Journal of Biochemistry, 165:491, 1987 : PubMed

            

&gt; Structure scheme for Non-catalytic_C
&gt; Structures for Non-catalytic_C (18)
&gt; List of Gene_Locus for Non-catalytic_C (981)


Top
FamilyOtherNon-catalytic_CParent FamilyNon-catalytic_C
CommentAmong COesterase PF00135 a number of proteins seem to lack active site residues but have not yet been characterized. They are not related to the known families of non-catalytic COesterase (neuroligins, neurotactin, gliotactin, glutactin) They could be pseudo genes or sequencing errors
InterproIPR002018 (Carboxylesterase, type B)Pdoc
PFamPF00135 (COesterase)PrintsProsite
EC no EC numberTables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid
    Krejci E, Duval N, Chatonnet A, Vincens P, Massoulie J
    Ref: Proceedings of the National Academy of Sciences of the United States of America, 88:6647, 1991 : PubMed

            

no Image
no Structure
&gt; List of Gene_Locus for OtherNon-catalytic_C (179)


Top
FamilyThyroglobulinParent FamilyNon-catalytic_C
CommentOnly the C-terminal part of thyroglobulin is a member of the alpha/beta hydrolase family, here starting with the first G in cholinesterase 2206 (aa numbering in human thyroglobulin). The N-terminal part of thyroglobulin is made of three domains, labeled I to III, that encompass 10 repeats of a ca. 65 amino acid residues known as the Tg type-1 repeat PF00086 PS00484 IPR011641 IPR000716 not included in ESTHER. Thyroglobulin is the glycoprotein precursor to the thyroid hormones T3 (triiodothyronine) and T4 (tetraiodothyronine). It has a molecular mass of 660 kD, with 2 identical subunits, yet its complete hydrolysis yields only 2 to 4 molecules of T3 and T4. The protein contains a 19-amino acid signal peptide followed by 2,748 residues. Van Ommen (1987) suggested that defects in the TG gene can cause either dominant or recessive disorders depending on the nature of the defect. When the gene is absent or at least when no thyroglobulin is synthesized, the disorder is likely to be recessive, whereas the presence of an abnormal subunit leads to a dominantly inherited disorder. The explanation for this is that in a dimeric protein such as thyroglobulin, 75% of the dimers in heterozygotes will contain 1 or more abnormal subunits. This should profoundly disturb thyroglobulin metabolism, since this protein fulfills a dual storage/catalytic role as a dimer, is present in bulk quantities (100 mg Tg/g thyroid mass), and needs to be exocytosed, iodinated, endocytosed, and degraded. EnsemblClone AF230666, EnsemblContig AC079020.2.132816.152274, AF235100_2 gene chromosome 8 clone PAC 98A24 map 8q24.3. there is a small gene with only a little bit of thyroglobuline just 3' of the real gene AC069434.7.189089.192039 ENST00000254617 ENSG00000132287. Three out of five iodination sites are in the cholinesterase homologous domain 2573 (In T4), 2587 (In T4),2766 (In T3)
InterproIPR016324 (Thyroglobulin), IPR002018 (Carboxylesterase, type B)Pdoc PDOC00112
PFamPF00135 (COesterase)PrintsProsite PS00122, PS00941
EC no EC numberTables FASTAPeptides in fastaNucleotides in fasta
Alignmentwith Multalin:Text only/graphic displaywith Clustalw:No colour/coloured with Mview
DendrogramGraphical display, obtained with the dnd file produced by Clustalw
    Title: Formation of thyroid hormone revealed by a cryo-EM structure of native bovine thyroglobulin
    Marechal N, Serrano BP, Zhang X, Weitz CJ
    Ref: Nat Commun, 13:2380, 2022 : PubMed

            

    Title: The structure of human thyroglobulin
    Coscia F, Taler-Vercic A, Chang VT, Sinn L, O'Reilly FJ, Izore T, Renko M, Berger I, Rappsilber J and Lowe J <1 more author(s)>
    Ref: Nature, :, 2020 : PubMed

            

    Title: The role of thyroglobulin in thyroid hormonogenesis
    Citterio CE, Targovnik HM, Arvan P
    Ref: Nat Rev Endocrinol, 15:323, 2019 : PubMed

            

    Title: Relationship between the dimerization of thyroglobulin and its ability to form triiodothyronine
    Citterio CE, Morishita Y, Dakka N, Veluswamy B, Arvan P
    Ref: Journal of Biological Chemistry, 293:4860, 2018 : PubMed

            

    Title: Thyroglobulin Represents a Novel Molecular Architecture of Vertebrates
    Holzer G, Morishita Y, Fini JB, Lorin T, Gillet B, Hughes S, Tohme M, Deleage G, Demeneix B and Laudet V <1 more author(s)>
    Ref: Journal of Biological Chemistry, 291:16553, 2016 : PubMed

            

    Title: Molecular analysis of congenital goitres with hypothyroidism caused by defective thyroglobulin synthesis. Identification of a novel c.7006C>T [p.R2317X] mutation and expression of minigenes containing nonsense mutations in exon 7
    Machiavelli GA, Caputo M, Rivolta CM, Olcese MC, Gruneiro-Papendieck L, Chiesa A, Gonzalez-Sarmiento R, Targovnik HM
    Ref: Clinical Endocrinology (Oxf), 72:112, 2010 : PubMed

            

    Title: Congenital hypothyroidism with goitre caused by new mutations in the thyroglobulin gene
    Caputo M, Rivolta CM, Esperante SA, Gruneiro-Papendieck L, Chiesa A, Pellizas CG, Gonzalez-Sarmiento R, Targovnik HM
    Ref: Clinical Endocrinology (Oxf), 67:351, 2007 : PubMed

            

    Title: Haplotype analysis reveals founder effects of thyroglobulin gene mutations C1058R and C1977S in Japan
    Hishinuma A, Fukata S, Nishiyama S, Nishi Y, Oh-Ishi M, Murata Y, Ohyama Y, Matsuura N, Kasai K and Ieiri T <10 more author(s)>
    Ref: J Clinical Endocrinology Metab, 91:3100, 2006 : PubMed

            

    Title: Two distinct compound heterozygous constellations (R277X/IVS34-1G>C and R277X/R1511X) in the thyroglobulin (TG) gene in affected individuals of a Brazilian kindred with congenital goiter and defective TG synthesis
    Gutnisky VJ, Moya CM, Rivolta CM, Domene S, Varela V, Toniolo JV, Medeiros-Neto G, Targovnik HM
    Ref: J Clinical Endocrinology Metab, 89:646, 2004 : PubMed

            

    Title: Compound heterozygous mutations in the thyroglobulin gene (1143delC and 6725G-->A [R2223H]) resulting in fetal goitrous hypothyroidism
    Caron P, Moya CM, Malet D, Gutnisky VJ, Chabardes B, Rivolta CM, Targovnik HM
    Ref: J Clinical Endocrinology Metab, 88:3546, 2003 : PubMed

            

    Title: Congenital goiter with hypothyroidism caused by a 5' splice site mutation in the thyroglobulin gene
    Targovnik HM, Rivolta CM, Mendive FM, Moya CM, Vono J, Medeiros-Neto G
    Ref: Thyroid, 11:685, 2001 : PubMed

            

    Title: A missense mutation G2320R in the thyroglobulin gene causes non-goitrous congenital primary hypothyroidism in the WIC-rdw rat
    Kim PS, Ding M, Menon S, Jung CG, Cheng JM, Miyamoto T, Li B, Furudate S, Agui T
    Ref: Mol Endocrinol, 14:1944, 2000 : PubMed

            

    Title: A single amino acid change in the acetylcholinesterase-like domain of thyroglobulin causes congenital goiter with hypothyroidism in the cog/cog mouse: a model of human endoplasmic reticulum storage diseases
    Kim PS, Hossain SA, Park YN, Lee I, Yoo SE, Arvan P
    Ref: Proc Natl Acad Sci U S A, 95:9909, 1998 : PubMed

            

    Title: The revised 8307 base pair coding sequence of human thyroglobulin transiently expressed in eukaryotic cells
    van de Graaf SA, Pauws E, de Vijlder JJ, Ris-Stalpers CR
    Ref: European Journal of Endocrinology, 136:508, 1997 : PubMed

            

    Title: A 138-nucleotide deletion in the thyroglobulin ribonucleic acid messenger in a congenital goiter with defective thyroglobulin synthesis
    Targovnik HM, Vono J, Billerbeck AE, Cerrone GE, Varela V, Mendive F, Wajchenberg BL, Medeiros-Neto G
    Ref: J Clinical Endocrinology Metab, 80:3356, 1995 : PubMed

            

    Title: A nonsense mutation causes human hereditary congenital goiter with preferential production of a 171-nucleotide-deleted thyroglobulin ribonucleic acid messenger
    Targovnik HM, Medeiros-Neto G, Varela V, Cochaux P, Wajchenberg BL, Vassart G
    Ref: J Clinical Endocrinology Metab, 77:210, 1993 : PubMed

            

    Title: A 3' splice site mutation in the thyroglobulin gene responsible for congenital goiter with hypothyroidism
    Ieiri T, Cochaux P, Targovnik HM, Suzuki M, Shimoda S, Perret J, Vassart G
    Ref: J Clinical Investigation, 88:1901, 1991 : PubMed

            

    Title: Mutant gene-induced disorders of structure, function and thyroglobulin synthesis in congenital goitre (cog/cog) in mice
    Adkison LR, Taylor S, Beamer WG
    Ref: J Endocrinol, 126:51, 1990 : PubMed

            

    Title: Consensus sequences for early iodination and hormonogenesis in human thyroglobulin
    Lamas L, Anderson PC, Fox JW, Dunn JT
    Ref: Journal of Biological Chemistry, 264:13541, 1989 : PubMed

            

    Title: Low levels of thyroglobulin messenger ribonucleic acid in congenital goitrous hypothyroidism with defective thyroglobulin synthesis
    Targovnik H, Propato F, Varela V, Wajchenberg B, Knobel M, D'Abronzo HF, Medeiros-Neto G
    Ref: J Clinical Endocrinology Metab, 69:1137, 1989 : PubMed

            

    Title: Autosomal recessive inheritance of goiter in Dutch goats
    Kok K, van Dijk JE, Sterk A, Baas F, van Ommen GJ, de Vijlder JJ
    Ref: Journal of Heredity, 78:298, 1987 : PubMed

            

    Title: Primary structure of human thyroglobulin deduced from the sequence of its 8448-base complementary DNA
    Malthiery Y, Lissitzky S
    Ref: European Journal of Biochemistry, 165:491, 1987 : PubMed

            

    Title: Structural organization of the 5' region of the thyroglobulin gene. Evidence for intron loss and exonization during evolution
    Parma J, Christophe D, Pohl V, Vassart G
    Ref: Journal of Molecular Biology, 196:769, 1987 : PubMed

            

    Title: A nonsense mutation causes hereditary goitre in the Afrikander cattle and unmasks alternative splicing of thyroglobulin transcripts
    Ricketts MH, Simons MJ, Parma J, Mercken L, Dong Q, Vassart G
    Ref: Proc Natl Acad Sci U S A, 84:3181, 1987 : PubMed

            

    Title: The human thyroglobulin gene is over 300 kb long and contains introns of up to 64 kb
    Baas F, van Ommen GJ, Bikker H, Arnberg AC, de Vijlder JJ
    Ref: Nucleic Acids Research, 14:5171, 1986 : PubMed

            

    Title: Mapping of human thyroglobulin gene on the long arm of chromosome 8 by in situ hybridization
    Avvedimento VE, Di Lauro R, Monticelli A, Bernardi F, Patracchini P, Calzolari E, Martini G, Varrone S
    Ref: Hum Genet, 71:163, 1985 : PubMed

            

    Title: The thyroglobulin gene resides on chromosome 8 in man and on chromosome 7 in the rat
    Brocas H, Szpirer J, Lebo RV, Levan G, Szpirer C, Cheung MC, Vassart G
    Ref: Cytogenet Cell Genet, 39:150, 1985 : PubMed

            

    Title: Defective splicing of thyroglobulin gene transcripts in the congenital goitre of the Afrikander cattle
    Ricketts MH, Pohl V, de Martynoff G, Boyd CD, Bester AJ, Van Jaarsveld PP, Vassart G
    Ref: EMBO Journal, 4:731, 1985 : PubMed

            

    Title: Autosomal dominant inheritance of a thyroglobulin abnormality suggests cooperation of sub-units in hormone formation
    De Vijlder JJM, Baas F, Koch CAM, Kok K, Gons M
    Ref: Ann Endocrinol (Paris), 44:36, 1983 : PubMed

            

    Title: Defective thyroglobulin export as a cause of congenital goitre
    Lissitzky S, Torresani J, Burrow GN, Bouchilloux S, Chabaud O
    Ref: Clinical Endocrinology (Oxf), 4:363, 1975 : PubMed

            

    Title: A goitrous subject with structural abnormality of thyroglobulin
    Kusakabe T
    Ref: J Clinical Endocrinology Metab, 35:785, 1972 : PubMed

            

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&gt; Structures for Thyroglobulin (4)
&gt; List of Gene_Locus for Thyroglobulin (68)



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