Gene_Locus Report

Biblio print

Add to basket

Go to basket

Tree Display

AceDB Schema

XML Display

Feedback

Gene_locus Report for: human-PRCP

Homo sapiens (Human) Lysosomal Pro-X carboxypeptidase C prolylcarboxypeptidase , Angiotensinase C, Proline carboxypeptidase (EC3.4.16.2)

Comment
Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH. PRCP was originally discovered as an angiotensinase and has since been implicated in vasodilatory, proinflammatory, and metabolic pathways. For example, angiotensin II, III and prekallikrein are all inactivated by PRCP, implicating a role for the enzyme in hypertension, tissue proliferation and smooth muscle growth. PRCP is also reported to inactivate -melanocyte-stimulating hormone, a neuropeptide that plays a role in regulating appetite Belongs to peptidase family s28


Relationship
Family|Prolylcarboxypeptidase
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
1 structure:
3N2Z: The Structure of Human Prolylcarboxypeptidase at 2.80 Angstroms Resolution
No kinetic





No Substrate
1 inhbitor:
CHEMBL3086040
>3 Genbank links 4 more: L13977, AP001646, CH471076
>3 UniProt links 9 more: P42785, B7Z7Q6, B3KR26
1 Ncbi-nid : 431320
1 Ncbi-pid : 431321
1 Structure : 3N2Z
>3 UniProt links 9 more: P42785, B7Z7Q6, B3KR26
>3 Interpro links 9 more: P42785, B7Z7Q6, B3KR26
>3 Prodom links 9 more: P42785, B7Z7Q6, B3KR26
>3 Pfam links 9 more: P42785, B7Z7Q6, B3KR26
>3 PIRSF links 9 more: P42785, B7Z7Q6, B3KR26
>3 SUPERFAM links 9 more: P42785, B7Z7Q6, B3KR26
1 EntrezGene : 5547
1 SNP : 5547
1 UniGene : 523936
1 HUGO HGNC : 9344
1 IUPHAR : 1584
1 OMIM : 176785
1 Ensembl : ENSG00000137509
Sequence
Graphical view for this peptide sequence: human-PRCP
Colored MSA for Prolylcarboxypeptidase (raw)
MGRRALLLLLLSFLAPWATIALRPALRALGSLHLPTNPTSLPAVAKNYSV
LYFQQKVDHFGFNTVKTFNQRYLVADKYWKKNGGSILFYTGNEGDIIWFC
NNTGFMWDVAEELKAMLVFAEHRYYGESLPFGDNSFKDSRHLNFLTSEQA
LADFAELIKHLKRTIPGAENQPVIAIGGSYGGMLAAWFRMKYPHMVVGAL
AASAPIWQFEDLVPCGVFMKIVTTDFRKSGPHCSESIHRSWDAINRLSNT
GSGLQWLTGALHLCSPLTSQDIQHLKDWISETWVNLAMVDYPYASNFLQP
LPAWPIKVVCQYLKNPNVSDSLLLQNIFQALNVYYNYSGQVKCLNISETA
TSSLGTLGWSYQACTEVVMPFCTNGVDDMFEPHSWNLKELSDDCFQQWGV
RPRPSWITTMYGGKNISSHTNIVFSNGELDPWSGGGVTKDITDTLVAVTI
SEGAHHLDLRTKNALDPMSVLLARSLEVRHMKNWIRDFYDSAGKQH
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

MGRRALLLLLLSFLAPWATIALRPALRALGSLHLPTNPTSLPAVAKNYSV
LYFQQKVDHFGFNTVKTFNQRYLVADKYWKKNGGSILFYTGNEGDIIWFC
NNTGFMWDVAEELKAMLVFAEHRYYGESLPFGDNSFKDSRHLNFLTSEQA
LADFAELIKHLKRTIPGAENQPVIAIGGSYGGMLAAWFRMKYPHMVVGAL
AASAPIWQFEDLVPCGVFMKIVTTDFRKSGPHCSESIHRSWDAINRLSNT
GSGLQWLTGALHLCSPLTSQDIQHLKDWISETWVNLAMVDYPYASNFLQP
LPAWPIKVVCQYLKNPNVSDSLLLQNIFQALNVYYNYSGQVKCLNISETA
TSSLGTLGWSYQACTEVVMPFCTNGVDDMFEPHSWNLKELSDDCFQQWGV
RPRPSWITTMYGGKNISSHTNIVFSNGELDPWSGGGVTKDITDTLVAVTI
SEGAHHLDLRTKNALDPMSVLLARSLEVRHMKNWIRDFYDSAGKQH


References
4 more
    Title: Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase families
    Tan F, Morris PW, Skidgel RA, Erdos EG
    Ref: Journal of Biological Chemistry, 268:16631, 1993 : PubMed

            

    Title: Purification and properties of prolylcarboxypeptidase (angiotensinase C) from human kidney
    Odya CE, Marinkovic DV, Hammon KJ, Stewart TA and
    Ref: Journal of Biological Chemistry, 253:5927, 1978 : PubMed

            

    Title: New enzymatic route for the inactivation of angiotensin
    Yang HY, Erdos EG, Chiang TS
    Ref: Nature, 218:1224, 1968 : 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
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer