CBPB1_CANLF
ID CBPB1_CANLF Reviewed; 416 AA.
AC P55261;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Carboxypeptidase B;
DE EC=3.4.17.2 {ECO:0000250|UniProtKB:P00732};
DE AltName: Full=47 kDa zymogen granule membrane-associated protein {ECO:0000303|PubMed:7765250};
DE AltName: Full=ZAP47 {ECO:0000303|PubMed:7765250};
DE Flags: Precursor;
GN Name=CPB1; Synonyms=CPB;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RA Fukuoka S.;
RT "Characterization and expression of cDNA encoding a dog zymogen granule
RT membrane associated protein, ZAP47.";
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 29-45, AND SUBCELLULAR LOCATION.
RX PubMed=7765250; DOI=10.1271/bbb.58.1282;
RA Fukuoka S.;
RT "Analysis of ZAPs, zymogen granule membrane associated proteins, in the
RT regulated exocytosis of the pancreas.";
RL Biosci. Biotechnol. Biochem. 58:1282-1285(1994).
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:0000305|PubMed:7765250}. Zymogen
CC granule lumen {ECO:0000305|PubMed:7765250}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR EMBL; D78348; BAA11366.1; -; mRNA.
DR PIR; PC2196; PC2196.
DR STRING; 9612.ENSCAFP00000012089; -.
DR MEROPS; M14.003; -.
DR PaxDb; P55261; -.
DR eggNOG; KOG2650; Eukaryota.
DR InParanoid; P55261; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; IBA:GO_Central.
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..15
FT /evidence="ECO:0000250|UniProtKB:P15086"
FT PROPEP 16..109
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000004369"
FT CHAIN 110..416
FT /note="Carboxypeptidase B"
FT /id="PRO_0000004370"
FT ACT_SITE 377
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00732"
FT BINDING 175..178
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15086"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15086"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 250..251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15086"
FT BINDING 304..305
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT DISULFID 244..267
FT /evidence="ECO:0000250|UniProtKB:P00732"
FT DISULFID 258..272
FT /evidence="ECO:0000250|UniProtKB:P00732"
SQ SEQUENCE 416 AA; 47597 MW; DFE1992CD52F8AB4 CRC64;
MAFLILVTLA LASAHYSGEH FEGEKVFRVN VEDENHINLL HTLASTTQID FWKPDSVTQI
KPHSTADFRV KAEDILTVED FLKQNELHYE VLINNLRLVL EGQFGRQVPA TGHSYEKYNR
WETIEAWTQQ VTSENPDLIS RRSIGTTFEG RTIYLLKVGK AGQNKPAIFM DCGFHAREWI
SPAFWQWFVR EXIRTYGQEI HMTELLDKLD FYVLPVGNID GYVYTWTKNR MWRKTRSTQV
GTNCVGTDPT RNFDAGWCKI GASRNPCDET YCGPAAESEK ETKALANFIR SNLSSIKAYL
TIHSYSQMML YPYSYDYKLT ENNAELNALA KATVKELATL HGTKYTYGPG ATTIYPAAGG
SDDWAYDQGI KYSFTFELRD KGRYGFALPE SQISPTCEET LLAIKHLARY VLQHLY
