ID   PCP_PONAB               Reviewed;         496 AA.
AC   Q5RBU7;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR858536; CAH90763.1; -; mRNA.
DR   RefSeq; NP_001125428.1; NM_001131956.1.
DR   AlphaFoldDB; Q5RBU7; -.
DR   SMR; Q5RBU7; -.
DR   STRING; 9601.ENSPPYP00000004261; -.
DR   ESTHER; ponpy-q5rbu7; Prolylcarboxypeptidase.
DR   MEROPS; S28.001; -.
DR   GeneID; 100172335; -.
DR   KEGG; pon:100172335; -.
DR   CTD; 5547; -.
DR   eggNOG; KOG2183; Eukaryota.
DR   InParanoid; Q5RBU7; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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..45
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000027312"
FT   CHAIN           46..496
FT                   /note="Lysosomal Pro-X carboxypeptidase"
FT                   /id="PRO_0000027313"
FT   REGION          194..334
FT                   /note="SKS domain"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        179
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        430
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        455
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        317
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        345
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        415
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        215..372
FT                   /evidence="ECO:0000250"
FT   DISULFID        233..310
FT                   /evidence="ECO:0000250"
FT   DISULFID        264..343
FT                   /evidence="ECO:0000250"
FT   DISULFID        364..394
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   496 AA;  55833 MW;  1915DB525566D58E CRC64;
     MGRRALLLLL LSFLAPWTTI ALRPALRALG SLHLPTNPTS LPAVAKNYSV LYFQQKVDHF
     GFNTVKTFNQ RYLVADKYWK KNGGSILFYT GNEGDIIWFC NNTGFMWDVA EELKAMLVFA
     EHRYYGESLP FGDNTFKDSR HLNFLTSEQA LADFAELIKH LKRTIPGAEN QPVIAIGGSY
     GGMLAAWFRM KYPHMVVGAL AASAPIWQFE DLVPCGVFMK IVTTDFRKSG PHCSESIRRS
     WDAINRLSNT GSGLQWLTGA LHLCSPLTSQ DIQHLKDWIS ETWVNLAMVD YPYASNFLQP
     LPAWPIKVVC QYLKNPNVSD SLLLQNIFQA LNVYYNYSGQ VKCLNISETA TSSLGTLGWS
     YQACTEVVMP FCTNGVDDMF EPHSWNLKEL SDDCFQQWGV RPRPSWITTM YGGKNISSHT
     NIVFSNGELD PWSGGGVTKD ITDTLVAVTI SEGAHHLDLR TKNALDPTSV LLARSLEVRH
     MKNWIRDFYD SAGKQH