ID   CBPA3_RAT               Reviewed;         412 AA.
AC   P21961; P97597;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Mast cell carboxypeptidase A;
DE            EC=3.4.17.1;
DE   AltName: Full=Carboxypeptidase A3;
DE   AltName: Full=R-CPA;
DE   AltName: Full=RMC-CP;
DE   Flags: Precursor; Fragment;
GN   Name=Cpa3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RX   PubMed=8996238; DOI=10.1084/jem.185.1.13;
RA   Lutzelschwab C., Pejler G., Aveskogh M., Hellman L.;
RT   "Secretory granule proteases in rat mast cells. Cloning of 10 different
RT   serine proteases and a carboxypeptidase A from various rat mast cell
RT   populations.";
RL   J. Exp. Med. 185:13-29(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 104-412.
RX   PubMed=1988052; DOI=10.1021/bi00217a009;
RA   Cole K.R., Kumar S., le Trong H., Woodbury R.G., Walsh K.A., Neurath H.;
RT   "Rat mast cell carboxypeptidase: amino acid sequence and evidence of enzyme
RT   activity within mast cell granules.";
RL   Biochemistry 30:648-655(1991).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of a C-terminal amino acid, but little or no action
CC         with -Asp, -Glu, -Arg, -Lys or -Pro.; EC=3.4.17.1;
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: Cytoplasmic vesicle, secretory vesicle.
CC       Note=Secretory granules.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U67914; AAB48267.1; -; mRNA.
DR   PIR; A38395; A38395.
DR   RefSeq; NP_062173.1; NM_019300.1.
DR   AlphaFoldDB; P21961; -.
DR   SMR; P21961; -.
DR   STRING; 10116.ENSRNOP00000014970; -.
DR   BindingDB; P21961; -.
DR   ChEMBL; CHEMBL4523202; -.
DR   MEROPS; M14.010; -.
DR   PhosphoSitePlus; P21961; -.
DR   PaxDb; P21961; -.
DR   PRIDE; P21961; -.
DR   GeneID; 54242; -.
DR   KEGG; rno:54242; -.
DR   UCSC; RGD:2390; rat.
DR   CTD; 1359; -.
DR   RGD; 2390; Cpa3.
DR   eggNOG; KOG2650; Eukaryota.
DR   InParanoid; P21961; -.
DR   OrthoDB; 524270at2759; -.
DR   PhylomeDB; P21961; -.
DR   Reactome; R-RNO-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; ISO:RGD.
DR   GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   GO; GO:0002002; P:regulation of angiotensin levels in blood; ISO:RGD.
DR   Gene3D; 3.30.70.340; -; 1.
DR   InterPro; IPR036990; M14A-like_propep.
DR   InterPro; IPR003146; M14A_act_pep.
DR   InterPro; IPR000834; Peptidase_M14.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   Pfam; PF02244; Propep_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE   1: Evidence at protein level;
KW   Carboxypeptidase; Cytoplasmic vesicle; Direct protein sequencing;
KW   Disulfide bond; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Signal; Zinc; Zymogen.
FT   SIGNAL          <1..10
FT                   /evidence="ECO:0000250"
FT   PROPEP          11..104
FT                   /note="Activation peptide"
FT                   /id="PRO_0000004399"
FT   CHAIN           105..412
FT                   /note="Mast cell carboxypeptidase A"
FT                   /id="PRO_0000004400"
FT   ACT_SITE        373
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         299
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   DISULFID        168..181
FT                   /evidence="ECO:0000250"
FT   DISULFID        240..263
FT                   /evidence="ECO:0000250"
FT   CONFLICT        196
FT                   /note="K -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        237
FT                   /note="N -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   412 AA;  47944 MW;  DAB59555FC49137D CRC64;
     LMGVIYSTLA IAPVQFDREK VFRVKLQDEK QASILKNLTQ TIELDFWYPD AIHDIAVNMT
     VDFRVTEKES QTIQSTLEQH KMDYEILIND LQEEIDKQFD VKEEIAGRHS YAKYNDWNKI
     VSWTEKMVEK HPEMVSRIKI GSTVEDNPLY VLKIGRKDGE RKAIFMDCGI HAREWVSPAF
     CQWFVYQAAK SYGKNKIMTK LLDRMNFYVL PVFNVDGYIW SWTKDRMWRK NRSKNPNSTC
     IGTDLNRNFD VSWDSSPNTD NPCLSVYRGP APESEKETKA VTNFIRSHLN SIKAYITFHS
     YSQMLLFPYG YTIKLPPNHQ DLLKVARIAT DVLSSRYETR YIYGPIASTI YKTSGSSLDW
     AYDLGIKHTF AFELRDKGKS GFLLPESRIK PTCKETMLSV KFIAKYILKH TS