rabit-Q7M370

 
Oryctolagus cuniculus (Rabbit) esterase/n-deacetylase (EC 3.5.1.-), 50k hepatic

Comment
(from Uniprot) Displays cellular triglyceride lipase activity in liver, increases the levels of intracellular fatty acids derived from the hydrolysis of newly formed triglyceride stores and plays a role in very low-density lipoprotein assembly. Displays serine esterase activity in liver. Deacetylates a variety of arylacetamide substrates, including xenobiotic compounds and procarcinogens, converting them to the primary arylamide compounds and increasing their toxicity (By similarity)


Relationship
Block H
Oryctolagus cuniculus position in NCBI Life Tree :
N link to NCBI taxonomic web page and E link to ESTHER gene locus found in this strain.
> 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 > Lagomorpha: N E > Leporidae: N E > Oryctolagus: N E > Oryctolagus cuniculus: N E

Molecular evidence
Database
No mutation
No structure
No kinetic



1 UniProt : Q7M370
1 UniProtTrembl : Q7M370
1 Interpro : Q7M370
1 Prodom : Q7M370
1 Pfam : Q7M370
1 PIRSF : Q7M370
1 SUPERFAM : Q7M370
1 QuickSwissBlast : Q7M370
 
Sequence
Graphical view for this peptide sequence: rabit-Q7M370
Colored MSA for Arylacetamide_deacetylase (raw)
GVKTVLLLIVGVLGAYYVYTPLPDNIEEPWRLLWVNAHMKTLTNLALFAE
YLGSNIFMNTVKFLTSFQEVPPTSDENVTVTETTFNNVPVRVYVPKRKSK
TLRRGLFYIHGGGWCVGSAALSGYDLLSRRTADRLDVVVVSTNYRLAPEY
HFPIQFEDVYDALKWFLRQDVLEKYGVDPERVGVSGDSAGGNLAAAVAQQ
LIKDPDVKIKLKTQSLIYPALQTLDMDLPSYRENAQFPILSKSFMVRLWS
EYFTSDRSLEKAMLLNQHVPVESSHLFKFTNWSSLLPEKFKKGHVYNTPT
YGSSELARKYPGFLDVRAAPLLADDAQLRGFPLTYVITCQYDVLRDDGVM
YVTRLRNAGVQVTHNHIEDGFHGALSYNGFKTGYRVEKQYFEWLRENV
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

GVKTVLLLIVGVLGAYYVYTPLPDNIEEPWRLLWVNAHMKTLTNLALFAE
YLGSNIFMNTVKFLTSFQEVPPTSDENVTVTETTFNNVPVRVYVPKRKSK
TLRRGLFYIHGGGWCVGSAALSGYDLLSRRTADRLDVVVVSTNYRLAPEY
HFPIQFEDVYDALKWFLRQDVLEKYGVDPERVGVSGDSAGGNLAAAVAQQ
LIKDPDVKIKLKTQSLIYPALQTLDMDLPSYRENAQFPILSKSFMVRLWS
EYFTSDRSLEKAMLLNQHVPVESSHLFKFTNWSSLLPEKFKKGHVYNTPT
YGSSELARKYPGFLDVRAAPLLADDAQLRGFPLTYVITCQYDVLRDDGVM
YVTRLRNAGVQVTHNHIEDGFHGALSYNGFKTGYRVEKQYFEWLRENV

no DNA




References
    Title: Appropriate function of 11beta-hydroxysteroid dehydrogenase type 1 in the endoplasmic reticulum lumen is dependent on its N-terminal region sharing similar topological determinants with 50-kDa esterase
    Frick C, Atanasov AG, Arnold P, Ozols J, Odermatt A
    Ref: Journal of Biological Chemistry, 279:31131, 2004 : PubMed

            

    Title: Targeting proteins to the lumen of endoplasmic reticulum using N-terminal domains of 11beta-hydroxysteroid dehydrogenase and the 50-kDa esterase
    Mziaut H, Korza G, Hand AR, Gerard C, Ozols J
    Ref: Journal of Biological Chemistry, 274:14122, 1999 : PubMed

            

    Title: Determination of lumenal orientation of microsomal 50-kDa esterase/N-deacetylase
    Ozols J
    Ref: Biochemistry, 37:10336, 1998 : PubMed

            


Other Papers


Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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