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Gene_locus Report for: human-SCPEP1

Homo sapiens (Human) serine Retinoid-inducible serine carboxypeptidase RISC SCP1 (EC 3.4.16.-)

Comment
Homo sapiens (Human) dc39 Trembl Q9H2J9 mstp034 Q9H3F0 Serine carboxypeptidase 1 old human-HSCP1. Kollmann et al. (2009) showed that the 55-kD mouse Scpep1 precursor protein was processed into a 35-kD N-terminal fragment and an 18-kD C-terminal fragment. Processing was mediated by a lysosomal serine proteinase and took place in the endosomal-lysosomal compartment. All 5 putative N-glycosylation sites of Scpep1 were N-glycosylated in mouse embryonic fibroblasts. Lee et al. (2009) showed that Scpep1 expression promoted growth and migration of mouse or rat smooth muscle cells (SMCs). Mutation analysis revealed that the stimulatory effects of Scpep1 on SMC growth and migration required the Scpep1 catalytic triad, but not cleavage of Scpep1. Immunohistochemical analysis of injured mouse and rat carotid arteries demonstrated increased Scpep1 expression in vessel walls where modulated SMCs were proliferative and migratory. By analyzing cultured mouse aortic vascular SMCs (AVSMCs), Pan et al. (2014) showed that Scpep1 had carboxypeptidase activity towards ET1 (EDN1), complementing the serine carboxypeptidase activity of CathA (CTSA). Analysis with purified recombinant protein confirmed that Scpep1 cleaved the C-terminal trp residue from ET1. also named MSTP034 AF113214


Relationship
Family|Carboxypeptidase_S10
Block| X
Position in NCBI Life Tree|Homo sapiens
(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 > Primates: N E > Haplorrhini: N E > Simiiformes: N E > Catarrhini: N E > Hominoidea: N E > Hominidae: N E > Homininae: N E > Homo: N E > Homo sapiens: N E


Molecular evidence
Database
No mutation
No structure
No kinetic





No Substrate
1 inhbitor:
Rocaglate-Derived-beta-Lactone-5
>3 Genbank links 3 more: NM_021626, AF282618, AF113214
3 UniProt : Q9H2J9, Q9HB40, B4DP22
2 Ncbi-nid : 11055991, 11640575
2 Ncbi-pid : 11055992, 11640576
3 UniProt : Q9HB40, Q9H2J9, B4DP22
3 Interpro : Q9HB40, Q9H2J9, B4DP22
3 Pfam : Q9HB40, Q9H2J9, B4DP22
3 PIRSF : Q9HB40, Q9H2J9, B4DP22
3 SUPERFAM : Q9HB40, Q9H2J9, B4DP22
1 EntrezGene : 59342
1 SNP : 59342
1 HUGO HGNC : 29507
1 IUPHAR : 1585
1 OMIM : 619723
1 Ensembl : ENSG00000121064
Sequence
Graphical view for this peptide sequence: human-SCPEP1
Colored MSA for Carboxypeptidase_S10 (raw)
MELALRRSPVPRWLLLLPLLLGLNAGAVIDWPTEEGKEVWDYVTVRKDAY
MFWWLYYATNSCKNFSELPLVMWLQGGPGGSSTGFGNFEEIGPLDSDLKP
RKTTWLQAASLLFVDNPVGTGFSYVNGSGAYAKDLAMVASDMMVLLKTFF
SCHKEFQTVPFYIFSESYGGKMAAGIGLELYKAIQRGTIKCNFAGVALGD
SWISPVDSVLSWGPYLYSMSLLEDKGLAEVSKVAEQVLNAVNKGLYREAT
ELWGKAEMIIEQNTDGVNFYNILTKSTPTSTMESSLEFTQSHLVCLCQRH
VRHLQRDALSQLMNGPIRKKLKIIPEDQSWGGQATNVFVNMEEDFMKPVI
SIVDELLEAGINVTVYNGQLDLIVDTMGQEAWVRKLKWPELPKFSQLKWK
ALYSDPKSLETSAFVKSYKNLAFYWILKAGHMVPSDQGDMALKMMRLVTQ
QE
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

MELALRRSPVPRWLLLLPLLLGLNAGAVIDWPTEEGKEVWDYVTVRKDAY
MFWWLYYATNSCKNFSELPLVMWLQGGPGGSSTGFGNFEEIGPLDSDLKP
RKTTWLQAASLLFVDNPVGTGFSYVNGSGAYAKDLAMVASDMMVLLKTFF
SCHKEFQTVPFYIFSESYGGKMAAGIGLELYKAIQRGTIKCNFAGVALGD
SWISPVDSVLSWGPYLYSMSLLEDKGLAEVSKVAEQVLNAVNKGLYREAT
ELWGKAEMIIEQNTDGVNFYNILTKSTPTSTMESSLEFTQSHLVCLCQRH
VRHLQRDALSQLMNGPIRKKLKIIPEDQSWGGQATNVFVNMEEDFMKPVI
SIVDELLEAGINVTVYNGQLDLIVDTMGQEAWVRKLKWPELPKFSQLKWK
ALYSDPKSLETSAFVKSYKNLAFYWILKAGHMVPSDQGDMALKMMRLVTQ
QE


References
5 more
    Title: Remodeling natural products: chemistry and serine hydrolase activity of a rocaglate-derived beta-lactone
    Lajkiewicz NJ, Cognetta AB, 3rd, Niphakis MJ, Cravatt BF, Porco JA, Jr.
    Ref: Journal of the American Chemical Society, 136:2659, 2014 : PubMed

            

    Title: Signal peptide prediction based on analysis of experimentally verified cleavage sites
    Zhang Z, Henzel WJ
    Ref: Protein Science, 13:2819, 2004 : PubMed

            

    Title: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    Zhang H, Li XJ, Martin DB, Aebersold R
    Ref: Nat Biotechnol, 21:660, 2003 : 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.
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