ID CBPA3_MOUSE Reviewed; 417 AA.
AC P15089;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 24-JAN-2024, entry version 174.
DE RecName: Full=Mast cell carboxypeptidase A;
DE Short=MC-CPA;
DE EC=3.4.17.1;
DE AltName: Full=Carboxypeptidase A3;
DE Flags: Precursor;
GN Name=Cpa3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2584208; DOI=10.1016/s0021-9258(19)47223-2;
RA Reynolds D.S., Stevens R.L., Gurley D.S., Lane W.S., Austen K.F.,
RA Serafin W.E.;
RT "Isolation and molecular cloning of mast cell carboxypeptidase A. A novel
RT member of the carboxypeptidase gene family.";
RL J. Biol. Chem. 264:20094-20099(1989).
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}.
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DR EMBL; J05118; AAA37369.1; -; mRNA.
DR CCDS; CCDS17262.1; -.
DR PIR; A34487; A34487.
DR RefSeq; NP_031779.1; NM_007753.2.
DR AlphaFoldDB; P15089; -.
DR SMR; P15089; -.
DR BioGRID; 198852; 1.
DR STRING; 10090.ENSMUSP00000001921; -.
DR MEROPS; M14.010; -.
DR PhosphoSitePlus; P15089; -.
DR PaxDb; 10090-ENSMUSP00000001921; -.
DR PeptideAtlas; P15089; -.
DR ProteomicsDB; 265680; -.
DR Antibodypedia; 1510; 218 antibodies from 26 providers.
DR DNASU; 12873; -.
DR Ensembl; ENSMUST00000001921.3; ENSMUSP00000001921.2; ENSMUSG00000001865.3.
DR GeneID; 12873; -.
DR KEGG; mmu:12873; -.
DR UCSC; uc008osp.2; mouse.
DR AGR; MGI:88479; -.
DR CTD; 1359; -.
DR MGI; MGI:88479; Cpa3.
DR VEuPathDB; HostDB:ENSMUSG00000001865; -.
DR eggNOG; KOG2650; Eukaryota.
DR GeneTree; ENSGT00940000161551; -.
DR HOGENOM; CLU_019326_0_0_1; -.
DR InParanoid; P15089; -.
DR OMA; YRIYNVQ; -.
DR OrthoDB; 3540647at2759; -.
DR PhylomeDB; P15089; -.
DR TreeFam; TF317197; -.
DR Reactome; R-MMU-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR BioGRID-ORCS; 12873; 0 hits in 78 CRISPR screens.
DR PRO; PR:P15089; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P15089; Protein.
DR Bgee; ENSMUSG00000001865; Expressed in dermis and 106 other cell types or tissues.
DR ExpressionAtlas; P15089; baseline and differential.
DR Genevisible; P15089; MM.
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:MGI.
DR GO; GO:0008233; F:peptidase activity; IDA:MGI.
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; IGI:MGI.
DR Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF65; MAST CELL CARBOXYPEPTIDASE A; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF02244; Propep_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
DR PROSITE; PS52035; PEPTIDASE_M14; 1.
PE 2: Evidence at transcript level;
KW Carboxypeptidase; Cytoplasmic vesicle; Disulfide bond; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Signal; Zinc;
KW Zymogen.
FT SIGNAL 1..15
FT PROPEP 16..109
FT /note="Activation peptide"
FT /id="PRO_0000004397"
FT CHAIN 110..417
FT /note="Mast cell carboxypeptidase A"
FT /id="PRO_0000004398"
FT DOMAIN 118..412
FT /note="Peptidase M14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT ACT_SITE 378
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379"
FT DISULFID 173..186
FT /evidence="ECO:0000250"
FT DISULFID 245..268
FT /evidence="ECO:0000250"
SQ SEQUENCE 417 AA; 48790 MW; A2B300A068D1BA6D CRC64;
MRFFLLMAVI YTTLAIAPVH FDREKVFRVK LQNEKHASVL KNLTQSIELD FWYPDAIHDI
AVNMTVDFRV SEKESQTIQS TLEQHKIHYE ILIHDLQEEI EKQFDVKDEI AGRHSYAKYN
DWDKIVSWTE KMLEKHPEMV SRIKIGSTVE DNPLYVLKIG KKDGERKAIF MDCGIHAREW
ISPAFCQWFV YQATKSYGKN KIMTKLLDRM NFYVLPVFNV DGYIWSWTQD RMWRKNRSRN
QNSTCIGTDL NRNFDVSWDS SPNTNKPCLN VYRGPAPESE KETKAVTNFI RSHLNSIKAY
ITFHSYSQML LIPYGYTFKL PPNHQDLLKV ARIATDALST RYETRYIYGP IASTIYKTSG
SSLDWVYDLG IKHTFAFELR DKGKSGFLLP ESRIKPTCKE TMLSVKFIAK YILKNTS
//
