ID   PCP_BOVIN               Reviewed;         499 AA.
AC   Q2TA14;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Lysosomal Pro-X carboxypeptidase;
DE            EC=3.4.16.2;
DE   AltName: Full=Proline carboxypeptidase;
DE   AltName: Full=Prolylcarboxypeptidase;
DE            Short=PRCP;
DE   Flags: Precursor;
GN   Name=PRCP;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cleaves C-terminal amino acids linked to proline in peptides
CC       such as angiotensin II, III and des-Arg9-bradykinin. This cleavage
CC       occurs at acidic pH, but enzymatic activity is retained with some
CC       substrates at neutral pH (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of a -Pro-|-Xaa bond to release a C-terminal amino
CC         acid.; EC=3.4.16.2;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S28 family. {ECO:0000305}.
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DR   EMBL; BC111171; AAI11172.1; -; mRNA.
DR   RefSeq; NP_001033253.1; NM_001038164.2.
DR   AlphaFoldDB; Q2TA14; -.
DR   SMR; Q2TA14; -.
DR   STRING; 9913.ENSBTAP00000045060; -.
DR   ESTHER; bovin-q2ta14; Prolylcarboxypeptidase.
DR   MEROPS; S28.001; -.
DR   PaxDb; Q2TA14; -.
DR   PRIDE; Q2TA14; -.
DR   GeneID; 534927; -.
DR   KEGG; bta:534927; -.
DR   CTD; 5547; -.
DR   eggNOG; KOG2183; Eukaryota.
DR   InParanoid; Q2TA14; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IBA:GO_Central.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0060055; P:angiogenesis involved in wound healing; IBA:GO_Central.
DR   GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0043535; P:regulation of blood vessel endothelial cell migration; IMP:MGI.
DR   Gene3D; 1.20.120.980; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR008758; Peptidase_S28.
DR   InterPro; IPR042269; Ser_carbopepase_S28_SKS.
DR   Pfam; PF05577; Peptidase_S28; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Lysosome;
KW   Protease; Reference proteome; Signal; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..47
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000282871"
FT   CHAIN           48..499
FT                   /note="Lysosomal Pro-X carboxypeptidase"
FT                   /id="PRO_0000282872"
FT   REGION          196..337
FT                   /note="SKS domain"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        181
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        433
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        458
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        339
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        348
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        418
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        217..375
FT                   /evidence="ECO:0000250"
FT   DISULFID        235..313
FT                   /evidence="ECO:0000250"
FT   DISULFID        266..346
FT                   /evidence="ECO:0000250"
FT   DISULFID        367..397
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   499 AA;  56671 MW;  7C080F0774EB7B68 CRC64;
     MGRCSLLLLL LLIAFLTPGA ANPVSPSLRA PSSLPWSTSF RSRPTITLKY SIRYIQQKVD
     HFGFNIDRTF KQRYLIADNY WKEDGGSILF YTGNEGDIIW FCNNTGFMWD IAEEMKAMLV
     FAEHRYYGES LPFGADSFSD SRHLNFLTTE QALADFAKLI RYLKRTIPGA RNQHVIALGG
     SYGGMLAAWF RMKYPHLVVG ALASSAPIWQ FNDLVPCDIF MKIVTTDFSQ SGPNCSESIR
     RSWDAINRLA KKGTGLRWLS EALHLCTPLT KSQDVQRLKD WISETWVNVA MVDYPYESNF
     LQPLPAWPVK VVCQYFKYSN VPDTVMVQNI FQALNVYYNY SGQAKCLNVS ETATSSLGVL
     GWSYQACTEM VMPTCSDGVD DMFEPHSWNM KEYSDDCFKQ WGVRPRPSWI PTMYGGKNIS
     SHTNIIFSNG ELDPWSGGGV TKDITDTLLA IVIPNGAHHL DLRASNALDP VSVQLTRSLE
     VKYMKQWISD FYVRLRKMN