Gene_Locus Report

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Gene_locus Report for: ratno-acot2

Rattus norvegicus (Rat) (EC 3.1.2.2) ACOT2 mitochondrial Acyl-CoA thioesterase 1 very-long-chain Acyl-CoA thioesterase (MTE-I)

Relationship
Family|Acyl-CoA_Thioesterase
Block| X
Position in NCBI Life Tree|Rattus norvegicus
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Metazoa: N E > Eumetazoa: N E > Bilateria: N E > Deuterostomia: N E > Chordata: N E > Craniata: N E > Vertebrata: N E > Gnathostomata: N E > Teleostomi: N E > Euteleostomi: N E > Sarcopterygii: N E > Dipnotetrapodomorpha: N E > Tetrapoda: N E > Amniota: N E > Mammalia: N E > Theria: N E > Eutheria: N E > Boreoeutheria: N E > Euarchontoglires: N E > Glires: N E > Rodentia: N E > Myomorpha: N E > Muroidea: N E > Muridae: N E > Murinae: N E > Rattus: N E > Rattus norvegicus: N E


Molecular evidence
Database
No mutation
No structure
No kinetic





No Substrate
No inhibitor
3 Genbank : Y09333, AB010429, BC072540
2 UniProt : O55171, Q6IMX8
2 UniProt : O55171, Q6IMX8
2 Interpro : O55171, Q6IMX8
2 Prodom : O55171, Q6IMX8
2 Pfam : O55171, Q6IMX8
2 PIRSF : O55171, Q6IMX8
2 SUPERFAM : O55171, Q6IMX8
Sequence
Graphical view for this peptide sequence: ratno-acot2
Colored MSA for Acyl-CoA_Thioesterase (raw)
MVASSFAVLRASRLCQWGWKSWTQLSGPPPLSTGGRTTFARTNATLSLEP
GSRSCWDEPLSITVRGLAPEQPVTLRAALRDEKGALFRAHARYRADAGGE
LDLARAPALGGSFTGLEPMGLIWAMEPERPLWRLVKRDVQKPYVVELEVL
DGHEPDGGQRLAQAVHERHFMAPGVRRVPVRDGRVRATLFLPPEPGPFPE
IIDLFGVGGGLLEYRASLLAGKGFAVMALAYYNYDDLPKTMETMRIEYFE
EAVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVA
AVGNTVCYKDETIPPVSLLRDKVKMTKDGLLDVVEALQSPLVDKKSFIPV
ERSDTTFLFLVGQDDHNWKSEFYAREASKRLQAHGKEKPQIICYPEAGHY
IEPPYFPLCSAGMHLLVGANITFGGEPKPHSVAQLDAWQQLQTFFHKQLS
GKS
Legend This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA

MVASSFAVLRASRLCQWGWKSWTQLSGPPPLSTGGRTTFARTNATLSLEP
GSRSCWDEPLSITVRGLAPEQPVTLRAALRDEKGALFRAHARYRADAGGE
LDLARAPALGGSFTGLEPMGLIWAMEPERPLWRLVKRDVQKPYVVELEVL
DGHEPDGGQRLAQAVHERHFMAPGVRRVPVRDGRVRATLFLPPEPGPFPE
IIDLFGVGGGLLEYRASLLAGKGFAVMALAYYNYDDLPKTMETMRIEYFE
EAVNYLRGHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVA
AVGNTVCYKDETIPPVSLLRDKVKMTKDGLLDVVEALQSPLVDKKSFIPV
ERSDTTFLFLVGQDDHNWKSEFYAREASKRLQAHGKEKPQIICYPEAGHY
IEPPYFPLCSAGMHLLVGANITFGGEPKPHSVAQLDAWQQLQTFFHKQLS
GKS


References
    Title: Molecular cloning and characterization of a mitochondrial peroxisome proliferator-induced acyl-CoA thioesterase from rat liver.
    Svensson LT, Engberg ST, Aoyama T, Usuda N, Alexson SEH, Hashimoto T
    Ref: Biochemical Journal, 329:601, 1998 : PubMed

            

    Title: cDNA cloning and genomic organization of peroxisome proliferator- inducible long-chain acyl-CoA hydrolase from rat liver cytosol.
    Yamada J, Suga K, Furihata T, Kitahara M, Watanabe T, Hosokawa M, Satoh T, Suga T
    Ref: Biochemical & Biophysical Research Communications, 248:608, 1998 : PubMed

            

    Title: Very long chain and long chain acyl-CoA thioesterases in rat liver mitochondria. Identification, purification, characterization, and induction by peroxisome proliferators.
    Svensson LT, Alexson SE, Hiltunen JK
    Ref: Journal of Biological Chemistry, 270:12177, 1995 : PubMed

            


Other Papers


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Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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