CBPB1_RAT
ID CBPB1_RAT Reviewed; 415 AA.
AC P19223;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Carboxypeptidase B;
DE EC=3.4.17.2 {ECO:0000250|UniProtKB:P00732};
DE Flags: Precursor;
GN Name=Cpb1; Synonyms=Cpb;
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].
RX PubMed=3182872; DOI=10.1016/s0021-9258(19)77911-3;
RA Clauser E., Gardell S.J., Craik C.S., Macdonald R.J., Rutter W.J.;
RT "Structural characterization of the rat carboxypeptidase A1 and B genes.
RT Comparative analysis of the rat carboxypeptidase gene family.";
RL J. Biol. Chem. 263:17837-17845(1988).
RN [2]
RP PROTEIN SEQUENCE OF 109-130.
RC STRAIN=Wistar; TISSUE=Pancreas;
RX PubMed=1898371; DOI=10.1042/bj2780857;
RA Kodama H., Shimojo N., Suzuki K.T.;
RT "Distribution of manganese in rat pancreas and identification of its
RT primary binding protein as pro-carboxypeptidase B.";
RL Biochem. J. 278:857-862(1991).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential release of a C-terminal lysine or arginine amino
CC acid.; EC=3.4.17.2; Evidence={ECO:0000250|UniProtKB:P00732};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P15086};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P15086};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00732}. Zymogen
CC granule lumen {ECO:0000250|UniProtKB:P55261}.
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; M23959; AAA40872.1; -; Genomic_DNA.
DR EMBL; M23947; AAA40872.1; JOINED; Genomic_DNA.
DR EMBL; M23950; AAA40872.1; JOINED; Genomic_DNA.
DR EMBL; M23952; AAA40872.1; JOINED; Genomic_DNA.
DR EMBL; M23953; AAA40872.1; JOINED; Genomic_DNA.
DR EMBL; M23954; AAA40872.1; JOINED; Genomic_DNA.
DR PIR; A32129; A32129.
DR AlphaFoldDB; P19223; -.
DR SMR; P19223; -.
DR STRING; 10116.ENSRNOP00000048109; -.
DR MEROPS; M14.003; -.
DR PhosphoSitePlus; P19223; -.
DR PaxDb; P19223; -.
DR PRIDE; P19223; -.
DR UCSC; RGD:2391; rat.
DR RGD; 2391; Cpb1.
DR eggNOG; KOG2650; Eukaryota.
DR InParanoid; P19223; -.
DR PhylomeDB; P19223; -.
DR Reactome; R-RNO-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR PRO; PR:P19223; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004180; F:carboxypeptidase activity; IDA:RGD.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR CDD; cd03871; M14_CPB; 1.
DR Gene3D; 3.30.70.340; -; 1.
DR InterPro; IPR034253; CPB_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; Cytoplasmic vesicle; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..13
FT /evidence="ECO:0000250|UniProtKB:P15086"
FT PROPEP 14..108
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:1898371"
FT /id="PRO_0000004375"
FT CHAIN 109..415
FT /note="Carboxypeptidase B"
FT /id="PRO_0000004376"
FT ACT_SITE 376
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00732"
FT BINDING 174..177
FT /ligand="substrate"
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:P15086"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15086"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 249..250
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15086"
FT BINDING 303..304
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT DISULFID 171..184
FT /evidence="ECO:0000250|UniProtKB:P00732"
FT DISULFID 243..266
FT /evidence="ECO:0000250|UniProtKB:P00732"
FT DISULFID 257..271
FT /evidence="ECO:0000250|UniProtKB:P00732"
SQ SEQUENCE 415 AA; 47515 MW; 8EA06CCADE30B6F2 CRC64;
MLLLLALVSV ALAHASEEHF DGNRVYRVSV HGEDHVNLIQ ELANTKEIDF WKPDSATQVK
PLTTVDFHVK AEDVADVENF LEENEVHYEV LISNVRNALE SQFDSHTRAS GHSYTKYNKW
ETIEAWIQQV ATDNPDLVTQ SVIGTTFEGR NMYVLKIGKT RPNKPAIFID CGFHAREWIS
PAFCQWFVRE AVRTYNQEIH MKQLLDELDF YVLPVVNIDG YVYTWTKDRM WRKTRSTMAG
SSCLGVRPNR NFNAGWCEVG ASRSPCSETY CGPAPESEKE TKALADFIRN NLSTIKAYLT
IHSYSQMMLY PYSYDYKLPE NYEELNALVK GAAKELATLH GTKYTYGPGA TTIYPAAGGS
DDWSYDQGIK YSFTFELRDT GFFGFLLPES QIRQTCEETM LAVKYIANYV REHLY
