ID   CBPM_PONAB              Reviewed;         443 AA.
AC   Q5RFD6;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Carboxypeptidase M;
DE            Short=CPM;
DE            EC=3.4.17.12;
DE   Flags: Precursor;
GN   Name=CPM;
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: Specifically removes C-terminal basic residues (Arg or Lys)
CC       from peptides and proteins. It is believed to play important roles in
CC       the control of peptide hormone and growth factor activity at the cell
CC       surface, and in the membrane-localized degradation of extracellular
CC       proteins (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of C-terminal arginine or lysine residues from
CC         polypeptides.; EC=3.4.17.12;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P00730};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR   EMBL; CR857222; CAH89521.1; -; mRNA.
DR   RefSeq; NP_001124659.1; NM_001131187.1.
DR   AlphaFoldDB; Q5RFD6; -.
DR   SMR; Q5RFD6; -.
DR   STRING; 9601.ENSPPYP00000005417; -.
DR   GeneID; 100171502; -.
DR   KEGG; pon:100171502; -.
DR   CTD; 1368; -.
DR   eggNOG; KOG2649; Eukaryota.
DR   InParanoid; Q5RFD6; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03866; M14_CPM; 1.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR033842; CPM_N.
DR   InterPro; IPR000834; Peptidase_M14.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF49464; SSF49464; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Hydrolase; Lipoprotein; Membrane; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Signal; Zinc.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..423
FT                   /note="Carboxypeptidase M"
FT                   /id="PRO_0000004393"
FT   PROPEP          424..443
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000251912"
FT   ACT_SITE        281
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P14384"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   LIPID           423
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        363
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        384
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        138..285
FT                   /evidence="ECO:0000250|UniProtKB:P14384"
FT   DISULFID        242..284
FT                   /evidence="ECO:0000250|UniProtKB:P14384"
FT   DISULFID        341..410
FT                   /evidence="ECO:0000250|UniProtKB:P14384"
SQ   SEQUENCE   443 AA;  50500 MW;  1711C41E803C1FE2 CRC64;
     MDFPCLWLGL LLPLVAALDF NYHHQEGMEA FLKTVAQNYS SITHLHSIGK SVKGRNLWVL
     VVGRFPKEHR IGIPEFKYVA NMHGDETVGR ELLLHLIDYL VTSDGKDPEI TNLINSTRIH
     IMPSMNPDGF EAVKKPDCYY SIGRENYNQY DLNRNFPDAF EYNNVSRQPE TVAVMKWLKT
     ETFVLSANLH GGALVASYPF DNGVQATGAL YSRSLTPDDD VFQYLAHTYA SRNPNMKKGD
     ECKNKMNFPN GVTNGYSWYP LQGGMQDYNY IWAQCFEITL ELSCCKYPRE EKLPSFWNNN
     KASLIEYIKQ VHLGVKGQVF DQNGNPLPDV IVEVQDRKHI CPYRTNKYGE YYLLLLPGSY
     IINVTVSGHD PHLTKVIIPE KSQNFSALKK DILLPFQGQL DSIPVSNPSC PMIPLYRNLP
     DHSAATKPSL FLFLVSLLHI FFK