ID   CBPN_BOVIN              Reviewed;         462 AA.
AC   Q2KJ83;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Carboxypeptidase N catalytic chain;
DE            Short=CPN;
DE            EC=3.4.17.3;
DE   AltName: Full=Carboxypeptidase N polypeptide 1;
DE   AltName: Full=Carboxypeptidase N small subunit;
DE   Flags: Precursor;
GN   Name=CPN1;
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=Hereford; TISSUE=Fetal liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protects the body from potent vasoactive and inflammatory
CC       peptides containing C-terminal Arg or Lys (such as kinins or
CC       anaphylatoxins) which are released into the circulation. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of a C-terminal basic amino acid, preferentially
CC         lysine.; EC=3.4.17.3;
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   -!- SUBUNIT: Tetramer of two catalytic chains and two glycosylated inactive
CC       chains. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR   EMBL; BC105475; AAI05476.1; -; mRNA.
DR   RefSeq; NP_001069548.1; NM_001076080.2.
DR   AlphaFoldDB; Q2KJ83; -.
DR   SMR; Q2KJ83; -.
DR   STRING; 9913.ENSBTAP00000032859; -.
DR   PaxDb; Q2KJ83; -.
DR   PRIDE; Q2KJ83; -.
DR   GeneID; 536753; -.
DR   KEGG; bta:536753; -.
DR   CTD; 1369; -.
DR   eggNOG; KOG2649; Eukaryota.
DR   InParanoid; Q2KJ83; -.
DR   OrthoDB; 101221at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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:0006518; P:peptide metabolic process; IBA:GO_Central.
DR   GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR027063; CPN1.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11532:SF80; PTHR11532:SF80; 1.
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; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..462
FT                   /note="Carboxypeptidase N catalytic chain"
FT                   /id="PRO_0000280816"
FT   REGION          20..340
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   REGION          417..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..443
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        308
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P14384"
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         216
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   CARBOHYD        402
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        41..103
FT                   /evidence="ECO:0000250"
FT   DISULFID        271..311
FT                   /evidence="ECO:0000250|UniProtKB:P14384"
SQ   SEQUENCE   462 AA;  52669 MW;  CFBCC53B5E9B2171 CRC64;
     MSDLVSIFLH LLLFKLVAPV TFRHHRYDDL VRMLYKVHNE CPHITRVYSI GRSVKGRHLY
     VLEFSDYPGI HEPLEPEVKY VGNMHGNEVL GRELLLQLSE FLCEEFRNRN QRIVRLVEDT
     RIHIMPSMNP DGYEVAAAAQ ERDISGYLVG RNNANGVDLN RNFPDLNTYI YYNEKNGGPN
     HHFPLPDNWK SQVEPETQAV IQWIRSFNFV LSANLHGGAV VANYPYDKSL GHRVRGFRRT
     ANTPTPDDKL FQKLAKIYSY AHGWMHQGWN CGDYFPDGIT NGASWYSLSK GMQDFNYLHT
     NCFEITLELS CDKFPLQGEL QREWLGNREA LIQFLEQVHQ GIKGMVRDEN YNNLADAVIS
     VGGINHDVTS GAHGDYFRLL LPGTYTVTAT APGFDPETVS VTVGPAEPKL VNFQLKRSTP
     QAAPKRRIPN SGHRGRVLPK KVQPRAARKK ETMMKQPQRG PA