ID   CBPO_BOVIN              Reviewed;         375 AA.
AC   Q0II73;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Carboxypeptidase O {ECO:0000250|UniProtKB:Q8IVL8};
DE            Short=CPO {ECO:0000250|UniProtKB:Q8IVL8};
DE            EC=3.4.17.- {ECO:0000250|UniProtKB:Q8IVL8};
DE   Flags: Precursor;
GN   Name=CPO {ECO:0000250|UniProtKB:Q8IVL8};
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=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Carboxypeptidase which preferentially cleaves C-terminal
CC       acidic residues from peptides and proteins. Can also cleave C-terminal
CC       hydrophobic amino acids, with a preference for small residues over
CC       large residues. {ECO:0000250|UniProtKB:Q8IVL8}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P00730};
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q8IVL8}; Lipid-anchor, GPI-anchor
CC       {ECO:0000250|UniProtKB:Q8IVL8}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR   EMBL; BC122774; AAI22775.1; -; mRNA.
DR   RefSeq; NP_001068840.1; NM_001075372.2.
DR   AlphaFoldDB; Q0II73; -.
DR   SMR; Q0II73; -.
DR   STRING; 9913.ENSBTAP00000025539; -.
DR   MEROPS; M14.021; -.
DR   PaxDb; Q0II73; -.
DR   Ensembl; ENSBTAT00000025539; ENSBTAP00000025539; ENSBTAG00000019190.
DR   GeneID; 508767; -.
DR   KEGG; bta:508767; -.
DR   CTD; 130749; -.
DR   VEuPathDB; HostDB:ENSBTAG00000019190; -.
DR   VGNC; VGNC:27666; CPO.
DR   eggNOG; KOG2650; Eukaryota.
DR   GeneTree; ENSGT00940000161508; -.
DR   HOGENOM; CLU_019326_4_1_1; -.
DR   InParanoid; Q0II73; -.
DR   OMA; TKKIIWM; -.
DR   OrthoDB; 524270at2759; -.
DR   TreeFam; TF317197; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000019190; Expressed in ileum and 3 other tissues.
DR   GO; GO:0046658; C:anchored component of plasma membrane; IEA:Ensembl.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd06247; M14_CPO; 1.
DR   InterPro; IPR033850; Carboxypeptidase_O.
DR   InterPro; IPR000834; Peptidase_M14.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Cell membrane; Glycoprotein; GPI-anchor; Hydrolase;
KW   Lipoprotein; Membrane; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Signal; Zinc.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250|UniProtKB:Q8IVL8"
FT   CHAIN           21..354
FT                   /note="Carboxypeptidase O"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000282873"
FT   PROPEP          355..375
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000437880"
FT   ACT_SITE        311
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         112
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         237
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   LIPID           354
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   375 AA;  43175 MW;  D2F8A001F5E8510B CRC64;
     MKPLLGTFYL LGMLVPGWLG YDRSLTQQRQ EVVDKVVSPW SILETYSYNR YHPMGEIYQW
     MSEIREKYTE VVTQHFLGMT YESRPMYYLK ISQPSSNPKK IIWMDCGIHA REWIAPAFCQ
     WFVKEILQNY EDNSRIRRLL KNLDFYVLPV LNIDGYIYTW TTDRLWRKSR SSHNNGTCFG
     TDLNRNFDAS WCSIGASHNC ESLTFCGTGP MSEPETKAVS SFIESKKENI ACFLTMHSYG
     QLILVPYGYT KNKSNNHEEL IQVGQKAANA LKAKHGTNYR VGSSADILYA TSGSSRDWAR
     DIGIPFSYTF ELRDNGTYGF VLPETQIQAT CEETMEAVLS VLDDVYEKYW YTNSARKAKS
     TALVLGLLMS FMSLL