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P42785

- PCP_HUMAN

UniProt

P42785 - PCP_HUMAN

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Protein
Lysosomal Pro-X carboxypeptidase
Gene
PRCP, PCP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

Cleavage of a -Pro-|-Xaa bond to release a C-terminal amino acid.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei179 – 1791Charge relay system1 Publication
Active sitei430 – 4301Charge relay system1 Publication
Active sitei455 – 4551Charge relay system1 Publication

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. serine-type carboxypeptidase activity Source: Reactome

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. blood coagulation, intrinsic pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Enzyme and pathway databases

ReactomeiREACT_326. Intrinsic Pathway.

Protein family/group databases

MEROPSiS28.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysosomal Pro-X carboxypeptidase (EC:3.4.16.2)
Alternative name(s):
Angiotensinase C
Lysosomal carboxypeptidase C
Proline carboxypeptidase
Prolylcarboxypeptidase
Short name:
PRCP
Gene namesi
Name:PRCP
Synonyms:PCP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:9344. PRCP.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. lysosome Source: UniProtKB-SubCell
  3. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33705.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121 Reviewed prediction
Add
BLAST
Propeptidei22 – 4524
PRO_0000027308Add
BLAST
Chaini46 – 496451Lysosomal Pro-X carboxypeptidase
PRO_0000027309Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi47 – 471N-linked (GlcNAc...) Reviewed prediction
Glycosylationi101 – 1011N-linked (GlcNAc...)1 Publication
Disulfide bondi215 ↔ 3721 Publication
Disulfide bondi233 ↔ 3101 Publication
Disulfide bondi264 ↔ 3431 Publication
Glycosylationi317 – 3171N-linked (GlcNAc...)2 Publications
Glycosylationi336 – 3361N-linked (GlcNAc...)1 Publication
Glycosylationi345 – 3451N-linked (GlcNAc...)1 Publication
Disulfide bondi364 ↔ 3941 Publication
Glycosylationi415 – 4151N-linked (GlcNAc...)2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP42785.
PaxDbiP42785.
PRIDEiP42785.

PTM databases

PhosphoSiteiP42785.

Expressioni

Tissue specificityi

Highest levels in placenta, lung and liver. Also present in heart, brain, pancreas and kidney.

Gene expression databases

ArrayExpressiP42785.
BgeeiP42785.
CleanExiHS_PRCP.
GenevestigatoriP42785.

Organism-specific databases

HPAiHPA017065.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GPR37L1O608832EBI-2803892,EBI-2927498

Protein-protein interaction databases

BioGridi111538. 12 interactions.
IntActiP42785. 4 interactions.
MINTiMINT-3015634.
STRINGi9606.ENSP00000377055.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi49 – 579
Beta strandi67 – 759
Turni81 – 833
Beta strandi85 – 906
Helixi96 – 1027
Helixi104 – 11310
Beta strandi115 – 1206
Helixi132 – 1365
Turni139 – 1413
Helixi147 – 16418
Helixi168 – 1703
Beta strandi173 – 1786
Helixi180 – 19112
Turni193 – 1953
Beta strandi197 – 2026
Helixi217 – 22711
Helixi233 – 24715
Helixi251 – 26010
Beta strandi263 – 2653
Helixi272 – 28817
Beta strandi295 – 3017
Helixi305 – 3128
Helixi320 – 33617
Beta strandi342 – 3443
Helixi354 – 36512
Beta strandi375 – 3806
Helixi387 – 39812
Helixi406 – 4116
Beta strandi422 – 4298
Helixi431 – 4355
Beta strandi441 – 45010
Helixi457 – 4593
Helixi468 – 48922

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N2ZX-ray2.79B46-491[»]
ProteinModelPortaliP42785.
SMRiP42785. Positions 46-491.

Miscellaneous databases

EvolutionaryTraceiP42785.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni194 – 334141SKS domain
Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S28 family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG290141.
HOGENOMiHOG000238311.
HOVERGENiHBG005526.
KOiK01285.
OMAiRSWKAIN.
OrthoDBiEOG78WKRN.
PhylomeDBiP42785.
TreeFamiTF314414.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR008758. Peptidase_S28.
[Graphical view]
PANTHERiPTHR11010. PTHR11010. 1 hit.
PfamiPF05577. Peptidase_S28. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P42785-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MGRRALLLLL LSFLAPWATI ALRPALRALG SLHLPTNPTS LPAVAKNYSV    50
LYFQQKVDHF GFNTVKTFNQ RYLVADKYWK KNGGSILFYT GNEGDIIWFC 100
NNTGFMWDVA EELKAMLVFA EHRYYGESLP FGDNSFKDSR HLNFLTSEQA 150
LADFAELIKH LKRTIPGAEN QPVIAIGGSY GGMLAAWFRM KYPHMVVGAL 200
AASAPIWQFE DLVPCGVFMK IVTTDFRKSG PHCSESIHRS WDAINRLSNT 250
GSGLQWLTGA LHLCSPLTSQ DIQHLKDWIS ETWVNLAMVD YPYASNFLQP 300
LPAWPIKVVC QYLKNPNVSD SLLLQNIFQA LNVYYNYSGQ VKCLNISETA 350
TSSLGTLGWS YQACTEVVMP FCTNGVDDMF EPHSWNLKEL SDDCFQQWGV 400
RPRPSWITTM YGGKNISSHT NIVFSNGELD PWSGGGVTKD ITDTLVAVTI 450
SEGAHHLDLR TKNALDPMSV LLARSLEVRH MKNWIRDFYD SAGKQH 496
Length:496
Mass (Da):55,800
Last modified:November 1, 1995 - v1
Checksum:iFC5DD570D3D3AB4F
GO
Isoform 2 (identifier: P42785-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     56-56: K → KALAAGQLHICIIQLNHYKTPL

Note: No experimental confirmation available.

Show »
Length:517
Mass (Da):58,100
Checksum:iA2490258A57E6F23
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti112 – 1121E → D.1 Publication
Corresponds to variant rs2298668 [ dbSNP | Ensembl ].
VAR_020464
Natural varianti444 – 4441T → S.
Corresponds to variant rs2228312 [ dbSNP | Ensembl ].
VAR_029329

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei56 – 561K → KALAAGQLHICIIQLNHYKT PL in isoform 2.
VSP_045799

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041G → E in BAG52417. 1 Publication
Sequence conflicti248 – 2481S → L in BAG52417. 1 Publication
Sequence conflicti304 – 3041W → R in BAG52417. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L13977 mRNA. Translation: AAA99891.1.
AK091786 mRNA. Translation: BAG52417.1.
AK312919 mRNA. Translation: BAG35764.1.
AB451270 mRNA. Translation: BAG70084.1.
AB451397 mRNA. Translation: BAG70211.1.
AP000893 Genomic DNA. No translation available.
AP001646 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW75074.1.
CH471076 Genomic DNA. Translation: EAW75075.1.
BC001500 mRNA. Translation: AAH01500.1.
CCDSiCCDS41695.1. [P42785-2]
CCDS8262.1. [P42785-1]
PIRiA47352.
RefSeqiNP_005031.1. NM_005040.2. [P42785-1]
NP_955450.2. NM_199418.2. [P42785-2]
UniGeneiHs.523936.

Genome annotation databases

EnsembliENST00000313010; ENSP00000317362; ENSG00000137509. [P42785-1]
ENST00000393399; ENSP00000377055; ENSG00000137509. [P42785-2]
GeneIDi5547.
KEGGihsa:5547.
UCSCiuc001ozr.3. human.
uc001ozs.3. human. [P42785-1]

Polymorphism databases

DMDMi1172047.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L13977 mRNA. Translation: AAA99891.1 .
AK091786 mRNA. Translation: BAG52417.1 .
AK312919 mRNA. Translation: BAG35764.1 .
AB451270 mRNA. Translation: BAG70084.1 .
AB451397 mRNA. Translation: BAG70211.1 .
AP000893 Genomic DNA. No translation available.
AP001646 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW75074.1 .
CH471076 Genomic DNA. Translation: EAW75075.1 .
BC001500 mRNA. Translation: AAH01500.1 .
CCDSi CCDS41695.1. [P42785-2 ]
CCDS8262.1. [P42785-1 ]
PIRi A47352.
RefSeqi NP_005031.1. NM_005040.2. [P42785-1 ]
NP_955450.2. NM_199418.2. [P42785-2 ]
UniGenei Hs.523936.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3N2Z X-ray 2.79 B 46-491 [» ]
ProteinModelPortali P42785.
SMRi P42785. Positions 46-491.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111538. 12 interactions.
IntActi P42785. 4 interactions.
MINTi MINT-3015634.
STRINGi 9606.ENSP00000377055.

Chemistry

BindingDBi P42785.
ChEMBLi CHEMBL2335.

Protein family/group databases

MEROPSi S28.001.

PTM databases

PhosphoSitei P42785.

Polymorphism databases

DMDMi 1172047.

Proteomic databases

MaxQBi P42785.
PaxDbi P42785.
PRIDEi P42785.

Protocols and materials databases

DNASUi 5547.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000313010 ; ENSP00000317362 ; ENSG00000137509 . [P42785-1 ]
ENST00000393399 ; ENSP00000377055 ; ENSG00000137509 . [P42785-2 ]
GeneIDi 5547.
KEGGi hsa:5547.
UCSCi uc001ozr.3. human.
uc001ozs.3. human. [P42785-1 ]

Organism-specific databases

CTDi 5547.
GeneCardsi GC11M082535.
HGNCi HGNC:9344. PRCP.
HPAi HPA017065.
MIMi 176785. gene.
neXtProti NX_P42785.
PharmGKBi PA33705.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG290141.
HOGENOMi HOG000238311.
HOVERGENi HBG005526.
KOi K01285.
OMAi RSWKAIN.
OrthoDBi EOG78WKRN.
PhylomeDBi P42785.
TreeFami TF314414.

Enzyme and pathway databases

Reactomei REACT_326. Intrinsic Pathway.

Miscellaneous databases

ChiTaRSi PRCP. human.
EvolutionaryTracei P42785.
GeneWikii PRCP.
GenomeRNAii 5547.
NextBioi 21494.
PROi P42785.
SOURCEi Search...

Gene expression databases

ArrayExpressi P42785.
Bgeei P42785.
CleanExi HS_PRCP.
Genevestigatori P42785.

Family and domain databases

Gene3Di 3.40.50.1820. 2 hits.
InterProi IPR029058. AB_hydrolase.
IPR008758. Peptidase_S28.
[Graphical view ]
PANTHERi PTHR11010. PTHR11010. 1 hit.
Pfami PF05577. Peptidase_S28. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase families."
    Tan F., Morris P.W., Skidgel R.A., Erdoes E.G.
    J. Biol. Chem. 268:16631-16638(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    Tissue: Kidney.
  2. Erratum
    Tan F., Morris P.W., Skidgel R.A., Erdoes E.G.
    J. Biol. Chem. 268:26032-26032(1993)
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ASP-112.
    Tissue: Kidney and Lung.
  4. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  8. "Purification and properties of prolylcarboxypeptidase (angiotensinase C) from human kidney."
    Odya C.E., Marinkovic D.V., Hammon K.J., Stewart T.A., Erdos E.G.
    J. Biol. Chem. 253:5927-5931(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Tissue: Kidney.
  9. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-317 AND ASN-415.
    Tissue: Liver.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase."
    Soisson S.M., Patel S.B., Abeywickrema P.D., Byrne N.J., Diehl R.E., Hall D.L., Ford R.E., Reid J.C., Rickert K.W., Shipman J.M., Sharma S., Lumb K.J.
    BMC Struct. Biol. 10:16-16(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 46-491, SUBUNIT, DISULFIDE BONDS, ACTIVE SITE, GLYCOSYLATION AT ASN-101; ASN-317; ASN-336; ASN-345 AND ASN-415.

Entry informationi

Entry nameiPCP_HUMAN
AccessioniPrimary (citable) accession number: P42785
Secondary accession number(s): A8MU24
, B2R7B7, B3KRK5, B5BU34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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