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{{about|the gene|the postnominal|Royal College of Physicians}}
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{{Infobox_gene}}
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'''Lysosomal Pro-X carboxypeptidase''' is an [[enzyme]] that in humans is encoded by the ''PRCP'' [[gene]].<ref name="pmid8344943">{{cite journal | vauthors = Tan F, Morris PW, Skidgel RA, Erdos EG | title = Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase families | journal = J Biol Chem | volume = 268 | issue = 22 | pages = 16631–8 |date=Sep 1993 | pmid = 8344943 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PRCP prolylcarboxypeptidase (angiotensinase C)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5547| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Prolylcarboxypeptidase (angiotensinase C)
| HGNCid = 9344
| Symbol = PRCP
| AltSymbols =; PCP; HUMPCP; MGC2202
| OMIM = 176785
| ECnumber = 
| Homologene = 55867
| MGIid = 1919711
| GeneAtlas_image1 = PBB_GE_PRCP_201494_at_tn.png
| Function = {{GNF_GO|id=GO:0004188 |text = serine-type Pro-X carboxypeptidase activity}} {{GNF_GO|id=GO:0008236 |text = serine-type peptidase activity}}
| Component = {{GNF_GO|id=GO:0005764 |text = lysosome}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5547
    | Hs_Ensembl = ENSG00000137509
    | Hs_RefseqProtein = NP_005031
    | Hs_RefseqmRNA = NM_005040
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 82213058
    | Hs_GenLoc_end = 82289205
    | Hs_Uniprot = P42785
    | Mm_EntrezGene = 72461
    | Mm_Ensembl = ENSMUSG00000061119
    | Mm_RefseqmRNA = XM_988670
    | Mm_RefseqProtein = XP_993764
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 92750489
    | Mm_GenLoc_end = 92809191
    | Mm_Uniprot = Q3TLW3
  }}
}}
'''Prolylcarboxypeptidase (angiotensinase C)''', also known as '''PRCP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRCP prolylcarboxypeptidase (angiotensinase C)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5547| accessdate = }}</ref>


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{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = The protein encoded by this gene is a lysosomal prolylcarboxypeptidase, which cleaves C-terminal amino acids linked to proline in peptides such as angiotension II, III and des-Arg9-bradykinin. The cleavage occurs at acidic pH, but the enzyme activity is retained with some substrates at neutral pH. This enzyme has been shown to be an activator of the cell matrix-associated prekallikrein. The importance of angiotension II, one of the substrates of this enzyme, in regulating blood pressure and electrolyte balance suggests that this gene may be related to essential hypertension. Alternatively spliced transcript variants encoding distinct isoforms have been observed.<ref name="entrez">{{cite web | title = Entrez Gene: PRCP prolylcarboxypeptidase (angiotensinase C)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5547| accessdate = }}</ref>
| summary_text = The protein encoded by this gene is a lysosomal prolylcarboxypeptidase, which cleaves C-terminal amino acids linked to proline in peptides such as angiotension II, III and des-Arg9-bradykinin. The cleavage occurs at acidic pH, but the enzyme activity is retained with some substrates at neutral pH. This enzyme has been shown to be an activator of the cell matrix-associated prekallikrein. The importance of angiotension II, one of the substrates of this enzyme, in regulating blood pressure and electrolyte balance suggests that this gene may be related to essential hypertension. Alternatively spliced transcript variants encoding distinct isoforms have been observed.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Odya CE, Marinkovic DV, Hammon KJ, ''et al.'' |title=Purification and properties of prolylcarboxypeptidase (angiotensinase C) from human kidney. |journal=J. Biol. Chem. |volume=253 |issue= 17 |pages= 5927-31 |year= 1978 |pmid= 28321 |doi=  }}
*{{cite journal   |vauthors=Odya CE, Marinkovic DV, Hammon KJ, etal |title=Purification and properties of prolylcarboxypeptidase (angiotensinase C) from human kidney |journal=J. Biol. Chem. |volume=253 |issue= 17 |pages= 5927–31 |year= 1978 |pmid= 28321 |doi=  }}
*{{cite journal  | author=Yang HY, Erdös EG, Chiang TS |title=New enzymatic route for the inactivation of angiotensin. |journal=Nature |volume=218 |issue= 5148 |pages= 1224-6 |year= 1968 |pmid= 4297812 |doi=  }}
*{{cite journal  | vauthors=Yang HY, Erdös EG, Chiang TS |title=New enzymatic route for the inactivation of angiotensin |journal=Nature |volume=218 |issue= 5148 |pages= 1224–6 |year= 1968 |pmid= 4297812 |doi=10.1038/2181224a0 }}
*{{cite journal | author=Jackman HL, Tan F, Schraufnagel D, ''et al.'' |title=Plasma membrane-bound and lysosomal peptidases in human alveolar macrophages. |journal=Am. J. Respir. Cell Mol. Biol. |volume=13 |issue= 2 |pages= 196-204 |year= 1995 |pmid= 7626287 |doi=  }}
*{{cite journal   |vauthors=Jackman HL, Tan F, Schraufnagel D, etal |title=Plasma membrane-bound and lysosomal peptidases in human alveolar macrophages |journal=Am. J. Respir. Cell Mol. Biol. |volume=13 |issue= 2 |pages= 196–204 |year= 1995 |pmid= 7626287 |doi=  10.1165/ajrcmb.13.2.7626287}}
*{{cite journal  | author=Tan F, Morris PW, Skidgel RA, Erdös EG |title=Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase families. |journal=J. Biol. Chem. |volume=268 |issue= 22 |pages= 16631-8 |year= 1993 |pmid= 8344943 |doi=  }}
*{{cite journal   |vauthors=Watson B, Nowak NJ, Myracle AD, etal |title=The human angiotensinase C gene (HUMPCP) maps to 11q14 within 700 kb of D11S901: a candidate gene for essential hypertension |journal=Genomics |volume=44 |issue= 3 |pages= 365–7 |year= 1997 |pmid= 9325062 |doi= 10.1006/geno.1997.4883 }}
*{{cite journal | author=Watson B, Nowak NJ, Myracle AD, ''et al.'' |title=The human angiotensinase C gene (HUMPCP) maps to 11q14 within 700 kb of D11S901: a candidate gene for essential hypertension. |journal=Genomics |volume=44 |issue= 3 |pages= 365-7 |year= 1997 |pmid= 9325062 |doi= 10.1006/geno.1997.4883 }}
*{{cite journal  | vauthors=Shariat-Madar Z, Mahdi F, Schmaier AH |title=Identification and characterization of prolylcarboxypeptidase as an endothelial cell prekallikrein activator |journal=J. Biol. Chem. |volume=277 |issue= 20 |pages= 17962–9 |year= 2002 |pmid= 11830581 |doi= 10.1074/jbc.M106101200 }}
*{{cite journal  | author=Shariat-Madar Z, Mahdi F, Schmaier AH |title=Identification and characterization of prolylcarboxypeptidase as an endothelial cell prekallikrein activator. |journal=J. Biol. Chem. |volume=277 |issue= 20 |pages= 17962-9 |year= 2002 |pmid= 11830581 |doi= 10.1074/jbc.M106101200 }}
*{{cite journal   |vauthors=Moreira CR, Schmaier AH, Mahdi F, etal |title=Identification of prolylcarboxypeptidase as the cell matrix-associated prekallikrein activator |journal=FEBS Lett. |volume=523 |issue= 1–3 |pages= 167–70 |year= 2002 |pmid= 12123826 |doi=10.1016/S0014-5793(02)02980-0 }}
*{{cite journal | author=Moreira CR, Schmaier AH, Mahdi F, ''et al.'' |title=Identification of prolylcarboxypeptidase as the cell matrix-associated prekallikrein activator. |journal=FEBS Lett. |volume=523 |issue= 1-3 |pages= 167-70 |year= 2002 |pmid= 12123826 |doi=  }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | vauthors=Shariat-Madar Z, Mahdi F, Schmaier AH |title=Recombinant prolylcarboxypeptidase activates plasma prekallikrein |journal=Blood |volume=103 |issue= 12 |pages= 4554–61 |year= 2004 |pmid= 14996700 |doi= 10.1182/blood-2003-07-2510 |url=https://deepblue.lib.umich.edu/bitstream/2027.42/106127/1/jth03969.pdf }}
*{{cite journal  | author=Shariat-Madar Z, Mahdi F, Schmaier AH |title=Recombinant prolylcarboxypeptidase activates plasma prekallikrein. |journal=Blood |volume=103 |issue= 12 |pages= 4554-61 |year= 2004 |pmid= 14996700 |doi= 10.1182/blood-2003-07-2510 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal   |vauthors=Wang L, Feng Y, Zhang Y, etal |title=Prolylcarboxypeptidase gene, chronic hypertension, and risk of preeclampsia |journal=Am. J. Obstet. Gynecol. |volume=195 |issue= 1 |pages= 162–71 |year= 2006 |pmid= 16681991 |doi= 10.1016/j.ajog.2006.01.079 }}
*{{cite journal | author=Wang L, Feng Y, Zhang Y, ''et al.'' |title=Prolylcarboxypeptidase gene, chronic hypertension, and risk of preeclampsia. |journal=Am. J. Obstet. Gynecol. |volume=195 |issue= 1 |pages= 162-71 |year= 2006 |pmid= 16681991 |doi= 10.1016/j.ajog.2006.01.079 }}
}}
}}
{{refend}}
{{refend}}


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{{gene-11-stub}}

Latest revision as of 12:45, 4 November 2018

This article is about the gene. For the postnominal, see Royal College of Physicians.
VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Lysosomal Pro-X carboxypeptidase is an enzyme that in humans is encoded by the PRCP gene.[1][2]

The protein encoded by this gene is a lysosomal prolylcarboxypeptidase, which cleaves C-terminal amino acids linked to proline in peptides such as angiotension II, III and des-Arg9-bradykinin. The cleavage occurs at acidic pH, but the enzyme activity is retained with some substrates at neutral pH. This enzyme has been shown to be an activator of the cell matrix-associated prekallikrein. The importance of angiotension II, one of the substrates of this enzyme, in regulating blood pressure and electrolyte balance suggests that this gene may be related to essential hypertension. Alternatively spliced transcript variants encoding distinct isoforms have been observed.[2]

References

  1. ↑ Tan F, Morris PW, Skidgel RA, Erdos EG (Sep 1993). "Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase families". J Biol Chem. 268 (22): 16631–8. PMID 8344943.
  2. ↑ 2.0 2.1 "Entrez Gene: PRCP prolylcarboxypeptidase (angiotensinase C)".

Further reading



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