ID   CBPB_ASTAS              Reviewed;         303 AA.
AC   P04069;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1986, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Carboxypeptidase B;
DE            EC=3.4.17.2;
OS   Astacus astacus (Noble crayfish) (Astacus fluviatilis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC   Astacoidea; Astacidae; Astacus.
OX   NCBI_TaxID=6715;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Titani K., Ericsson L.H., Kumar S., Jakob F., Neurath H., Zwilling R.;
RT   "Amino acid sequence of crayfish (Astacus fluviatilis) carboxypeptidase
RT   B.";
RL   Biochemistry 23:1245-1250(1984).
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; A05141; CPCYB.
DR   AlphaFoldDB; P04069; -.
DR   SMR; P04069; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR000834; Peptidase_M14.
DR   Pfam; PF00246; Peptidase_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; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Zinc.
FT   CHAIN           1..303
FT                   /note="Carboxypeptidase B"
FT                   /id="PRO_0000212783"
FT   ACT_SITE        264
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00732"
FT   BINDING         63..66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         136..137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         189
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         190..191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
SQ   SEQUENCE   303 AA;  33918 MW;  3DF8379B16ECB4F7 CRC64;
     MDWTSYHDYD EINAWLDSLA TDYPELASVE DVGLSYEGRT MKLLKLGKGG ADKPIIFIDG
     GIHAREWIAP STVTYIVNEF VSNSATYDDI LSNVNFYVMP TINPDGYAYT FTDDRLWRKT
     RSETGSVLGC KGADPNRNWS FHWDEVGASD SPCSDIYAGP EPFSEVEMRN VRDQILEYAA
     NIKVYLTFHS YSQLWMYPWG FTSDLPDDWQ DLDTLATNAV DALTAVHGTR YEIGSSTNTI
     YAAAGGSDDW AKGEGGVKYA YTIELRDTGN YGFLLPENQI IPTGEETFEG VKVVANFVKD
     TYS