CBPA2_RAT
ID CBPA2_RAT Reviewed; 417 AA.
AC P19222; Q6LD54;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Carboxypeptidase A2;
DE EC=3.4.17.15;
DE Flags: Precursor;
GN Name=Cpa2;
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 [GENOMIC DNA].
RC TISSUE=Pancreas;
RX PubMed=3182871; DOI=10.1016/s0021-9258(19)77910-1;
RA Gardell S.J., Craik C.S., Clauser E., Goldsmith E.J., Stewart C.-B.,
RA Graf M., Rutter W.J.;
RT "A novel rat carboxypeptidase, CPA2: characterization, molecular cloning,
RT and evolutionary implications on substrate specificity in the
RT carboxypeptidase gene family.";
RL J. Biol. Chem. 263:17828-17836(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 131-143.
RX PubMed=7657630; DOI=10.1074/jbc.270.35.20543;
RA Normant E., Gros C., Schwartz J.C.;
RT "Carboxypeptidase A isoforms produced by distinct genes or alternative
RT splicing in brain and other extrapancreatic tissues.";
RL J. Biol. Chem. 270:20543-20549(1995).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ZINC IONS, AND
RP DISULFIDE BOND.
RX PubMed=1761558; DOI=10.1016/s0021-9258(18)54272-1;
RA Faming Z., Kobe B., Stewart C.-B., Rutter W.J., Goldsmith E.J.;
RT "Structural evolution of an enzyme specificity. The structure of rat
RT carboxypeptidase A2 at 1.9-A resolution.";
RL J. Biol. Chem. 266:24606-24612(1991).
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:0000269|PubMed:1761558};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:1761558};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; M23721; AAA40956.1; -; Genomic_DNA.
DR EMBL; M23714; AAA40956.1; JOINED; Genomic_DNA.
DR EMBL; M23715; AAA40956.1; JOINED; Genomic_DNA.
DR EMBL; M23716; AAA40956.1; JOINED; Genomic_DNA.
DR EMBL; M23717; AAA40956.1; JOINED; Genomic_DNA.
DR EMBL; M23718; AAA40956.1; JOINED; Genomic_DNA.
DR EMBL; M23719; AAA40956.1; JOINED; Genomic_DNA.
DR EMBL; M23720; AAA40956.1; JOINED; Genomic_DNA.
DR EMBL; S79837; AAP32037.1; -; mRNA.
DR PIR; A32128; A32128.
DR AlphaFoldDB; P19222; -.
DR SMR; P19222; -.
DR STRING; 10116.ENSRNOP00000038495; -.
DR MEROPS; M14.002; -.
DR jPOST; P19222; -.
DR PaxDb; P19222; -.
DR UCSC; RGD:1305563; rat.
DR RGD; 1305563; Cpa2.
DR eggNOG; KOG2650; Eukaryota.
DR InParanoid; P19222; -.
DR PhylomeDB; P19222; -.
DR SABIO-RK; P19222; -.
DR PRO; PR:P19222; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004180; F:carboxypeptidase activity; ISO:RGD.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; ISO:RGD.
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_0000004355"
FT CHAIN 113..417
FT /note="Carboxypeptidase A2"
FT /id="PRO_0000004356"
FT ACT_SITE 378
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:1761558"
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:0000269|PubMed:1761558"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:1761558"
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:0000269|PubMed:1761558"
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:P00732"
FT DISULFID 318..352
FT /evidence="ECO:0000250|UniProtKB:P00732"
SQ SEQUENCE 417 AA; 46912 MW; BEDCC41A830F2D45 CRC64;
MRLTLLLAAL LGYIYCQETF VGDQVLEIIP SHEEQIRTLL QLEAEEHLEL DFWKSPTIPG
ETVHVRVPFA SIQAVKVFLE SQGIDYSIMI EDVQVLLDQE REEMLFNQQR ERGGNFNFEA
YHTLEEIYQE MDNLVAENPG LVSKVNLGSS FENRPMNVLK FSTGGDKPAI WLDAGIHARE
WVTQATALWT ANKIASDYGT DPAITSLLNT LDIFLLPVTN PDGYVFSQTT NRMWRKTRSK
RSGSGCVGVD PNRNWDANFG GPGASSSPCS DSYHGPKPNS EVEVKSIVDF IKSHGKVKAF
ITLHSYSQLL MFPYGYKCTK PDDFNELDEV AQKAAQALKR LHGTSYKVGP ICSVIYQASG
GSIDWAYDLG IKYSFAFELR DTAFYGFLLP AKQILPTAEE TWLGLKTIME HVRDHPY
