ID   CBPB_PROAT              Reviewed;          15 AA.
AC   P19628;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Carboxypeptidase B;
DE            EC=3.4.17.2;
DE   Flags: Precursor; Fragment;
OS   Protopterus aethiopicus (Marbled lungfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Dipnomorpha; Ceratodontiformes; Lepidosirenoidei; Protopteridae;
OC   Protopterus.
OX   NCBI_TaxID=7886;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Pancreas;
RX   PubMed=5079891; DOI=10.1021/bi00771a018;
RA   Reeck G.R., Neurath H.;
RT   "Isolation and characterization of pancreatic procarboxypeptidase B and
RT   carboxypeptidase B of the African lungfish.";
RL   Biochemistry 11:3947-3955(1972).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential release of a C-terminal lysine or arginine amino
CC         acid.; EC=3.4.17.2;
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.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR   PIR; A26212; A26212.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Carboxypeptidase; Direct protein sequencing; Hydrolase; Metalloprotease;
KW   Protease; Secreted; Zinc; Zymogen.
FT   PROPEP          1..>15
FT                   /note="Activation peptide"
FT                   /id="PRO_0000004383"
FT   NON_TER         15
SQ   SEQUENCE   15 AA;  1749 MW;  124C910D937BED65 CRC64;
     EPTPRSFNGD KVFRV