CBPA2_MOUSE
ID CBPA2_MOUSE Reviewed; 417 AA.
AC Q504N0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Carboxypeptidase A2;
DE EC=3.4.17.15;
DE Flags: Precursor;
GN Name=Cpa2;
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 [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Similar to that of carboxypeptidase A (EC 3.4.17.1), but with
CC a preference for bulkier C-terminal residues.; EC=3.4.17.15;
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: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; BC094929; AAH94929.1; -; mRNA.
DR CCDS; CCDS19974.1; -.
DR RefSeq; NP_001019869.1; NM_001024698.3.
DR AlphaFoldDB; Q504N0; -.
DR SMR; Q504N0; -.
DR STRING; 10090.ENSMUSP00000093771; -.
DR MEROPS; M14.002; -.
DR iPTMnet; Q504N0; -.
DR PhosphoSitePlus; Q504N0; -.
DR MaxQB; Q504N0; -.
DR PaxDb; Q504N0; -.
DR PRIDE; Q504N0; -.
DR ProteomicsDB; 265282; -.
DR Antibodypedia; 17945; 540 antibodies from 32 providers.
DR DNASU; 232680; -.
DR Ensembl; ENSMUST00000096066; ENSMUSP00000093771; ENSMUSG00000071553.
DR GeneID; 232680; -.
DR KEGG; mmu:232680; -.
DR UCSC; uc009bfn.1; mouse.
DR CTD; 1358; -.
DR MGI; MGI:3617840; Cpa2.
DR VEuPathDB; HostDB:ENSMUSG00000071553; -.
DR eggNOG; KOG2650; Eukaryota.
DR GeneTree; ENSGT00940000160121; -.
DR HOGENOM; CLU_019326_0_0_1; -.
DR InParanoid; Q504N0; -.
DR OMA; DTIYSWM; -.
DR OrthoDB; 524270at2759; -.
DR PhylomeDB; Q504N0; -.
DR TreeFam; TF317197; -.
DR BioGRID-ORCS; 232680; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Cpa2; mouse.
DR PRO; PR:Q504N0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q504N0; protein.
DR Bgee; ENSMUSG00000071553; Expressed in pyloric antrum and 122 other tissues.
DR Genevisible; Q504N0; MM.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004180; F:carboxypeptidase activity; ISO:MGI.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd03870; M14_CPA; 1.
DR Gene3D; 3.30.70.340; -; 1.
DR InterPro; IPR034248; CPA_M14_CPD.
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; Disulfide bond; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc;
KW Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..112
FT /note="Activation peptide"
FT /id="PRO_0000280809"
FT CHAIN 113..417
FT /note="Carboxypeptidase A2"
FT /id="PRO_0000280810"
FT ACT_SITE 378
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00732"
FT BINDING 177..180
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 252..253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 305..306
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT DISULFID 246..269
FT /evidence="ECO:0000250|UniProtKB:Q96IY4"
FT DISULFID 318..352
FT /evidence="ECO:0000250|UniProtKB:P48052"
SQ SEQUENCE 417 AA; 47057 MW; A051FF523B9E1579 CRC64;
MRLTPLLVAL FGYIYCQETF VGDQVLEVIP NDEEQIKTLL QLEAEEHLEL DFWKSPSVPR
QTVHVRVPFA SIQDVKVFLE SQGITYSIMI EDVQVLLDQE REEMLFNQQR ERGTNFNFGA
YHTLEEIYQE MDNLVAENPG LVSKVNIGSS FENRPMNVLK FSTGGDKPAI WLDAGIHARE
WVTQATALWT ANKIASDYGT DPAITSLLNT LDVFLLPVTN PDGYVFSQTS NRMWRKTRSK
RSGSFCVGVD PNRNWDANFG GPGASSNPCS DSYHGPSPNS EVEVKSIVDF IKSHGKVKAF
ITLHSYSQLL MFPYGYKCAK PDDFNELDEV AQRAAQSLKR LHGTSYKVGP ICSVIYQASG
GSIDWAYDLG IKYSFAFELR DTGYYGFLLP AKQILPTAEE TWLGLKTIME HVRDHPY
