ID   CPVL_PONAB              Reviewed;         476 AA.
AC   Q5RFE4;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Probable serine carboxypeptidase CPVL;
DE            EC=3.4.16.-;
DE   Flags: Precursor;
GN   Name=CPVL;
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=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the digestion of phagocytosed particles in
CC       the lysosome, participation in an inflammatory protease cascade, and
CC       trimming of peptides for antigen presentation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; CR857214; CAH89513.1; -; mRNA.
DR   RefSeq; NP_001124656.1; NM_001131184.1.
DR   AlphaFoldDB; Q5RFE4; -.
DR   SMR; Q5RFE4; -.
DR   STRING; 9601.ENSPPYP00000019824; -.
DR   ESTHER; ponab-cpvl; Carboxypeptidase_S10.
DR   MEROPS; S10.003; -.
DR   GeneID; 100171497; -.
DR   KEGG; pon:100171497; -.
DR   CTD; 54504; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   InParanoid; Q5RFE4; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802; PTHR11802; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Signal; Zymogen.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..?
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000004282"
FT   CHAIN           ?..476
FT                   /note="Probable serine carboxypeptidase CPVL"
FT                   /id="PRO_0000004283"
FT   ACT_SITE        204
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        388
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        448
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        307
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        346
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   476 AA;  54254 MW;  F05307D75BE88C63 CRC64;
     MVGTMWKVIV SLVLLMPGSC DGLFRSLYRS VSMPPKGDSG QPLFLTPYIE AGKIQKGREL
     SLVSPFLGLN MRSYAGFLTV NKTYNSNLFF WFFPAQIQPE DAPVVLWLQG GPGFSSMFGL
     FVEHGPYVVT SNMTLRDRDF PWTTTLSMLY IDNPVGTGFS FTDDTHGYAV NEDDVAQDLY
     SALIQFFQIF PEYKNNDFYV TGESYAGKYV PAIAHLIHSL NPVREVKINL KGIAIGDGYS
     DPESIIGGYA EFLYQIGLLD EKQKKYFQKQ CHECIEHIRK QNWFQAFEIL DKLLDGDLTS
     DPSYFQNVTG CSNYCNFLRC TEPEDQLYYA KFLSLPEVRQ AIHVGNRTFN DGTTVEKYLR
     EDTVQSVKPW LTEIMNNYKV LIYNGQLDII VAAALTEHSL MGMDWKGSQE YKKAEKKVWK
     IFKSDSEVAG YVRQVGDFHQ VIIRGGGHIL PYIQPLRAFD MINRFIYGKG WDPYVG