CBPB1_BOVIN
ID CBPB1_BOVIN Reviewed; 417 AA.
AC P00732;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Carboxypeptidase B;
DE EC=3.4.17.2 {ECO:0000269|PubMed:5344132};
DE Flags: Precursor;
GN Name=CPB1; Synonyms=CPB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP PROTEIN SEQUENCE OF 111-416.
RX PubMed=1057162; DOI=10.1073/pnas.72.5.1666;
RA Titani K., Ericsson L.H., Walsh K.A., Neurath H.;
RT "Amino-acid sequence of bovine carboxypeptidase B.";
RL Proc. Natl. Acad. Sci. U.S.A. 72:1666-1670(1975).
RN [3]
RP PROTEIN SEQUENCE OF 141-203; 241-291; 373-375 AND 402-416.
RX PubMed=4833744; DOI=10.1016/s0021-9258(19)42538-6;
RA Schmidt J.J., Hirs C.H.W.;
RT "Primary structure of bovine carboxypeptidase B. Inferences from the
RT locations of the half-cystines and identification of the active site
RT arginine.";
RL J. Biol. Chem. 249:3756-3764(1974).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=957425; DOI=10.1016/0022-2836(76)90058-9;
RA Schmid M.F., Herriott J.R.;
RT "Structure of carboxypeptidase B at 2.8-A resolution.";
RL J. Mol. Biol. 103:175-190(1976).
RN [5]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SITE, AND PARTIAL PROTEIN
RP SEQUENCE.
RX PubMed=5344132; DOI=10.1016/s0021-9258(18)63653-1;
RA Plummer T.H. Jr.;
RT "Isolation and sequence of peptides at the active center of bovine
RT carboxypeptidase B.";
RL J. Biol. Chem. 244:5246-5253(1969).
RN [6]
RP ACTIVE SITE, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=4565668; DOI=10.1016/s0021-9258(20)81780-3;
RA Kimmel M.T., Plummer T.H. Jr.;
RT "Identification of a glutamic acid at the active center of bovine
RT carboxypeptidase B.";
RL J. Biol. Chem. 247:7864-7869(1972).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential release of a C-terminal lysine or arginine amino
CC acid.; EC=3.4.17.2; Evidence={ECO:0000269|PubMed:5344132};
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:0000269|PubMed:5344132}. Zymogen
CC granule lumen {ECO:0000250|UniProtKB:P55261}.
CC -!- MISCELLANEOUS: Chemical modification of Tyr-356 leads to loss of enzyme
CC activity (PubMed:5344132). Chemical modification of Glu-378 leads to
CC loss of enzyme activity (PubMed:4565668). {ECO:0000305|PubMed:4565668,
CC ECO:0000305|PubMed:5344132}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR PIR; A93797; CPBOB.
DR PDB; 1CPB; X-ray; 2.80 A; A=111-192, B=200-416.
DR PDBsum; 1CPB; -.
DR AlphaFoldDB; P00732; -.
DR SMR; P00732; -.
DR STRING; 9913.ENSBTAP00000000580; -.
DR MEROPS; M14.003; -.
DR PaxDb; P00732; -.
DR PRIDE; P00732; -.
DR Ensembl; ENSBTAT00000000580; ENSBTAP00000000580; ENSBTAG00000000456.
DR VEuPathDB; HostDB:ENSBTAG00000000456; -.
DR VGNC; VGNC:27645; CPB1.
DR eggNOG; KOG2650; Eukaryota.
DR GeneTree; ENSGT00940000157819; -.
DR HOGENOM; CLU_019326_0_0_1; -.
DR InParanoid; P00732; -.
DR OMA; GASRYPC; -.
DR TreeFam; TF317197; -.
DR EvolutionaryTrace; P00732; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000000456; Expressed in urinary bladder and 31 other tissues.
DR ExpressionAtlas; P00732; baseline and differential.
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 3D-structure; Carboxypeptidase; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc;
KW Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000250|UniProtKB:P15086"
FT PROPEP 17..110
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000280813"
FT CHAIN 111..417
FT /note="Carboxypeptidase B"
FT /id="PRO_0000212782"
FT ACT_SITE 378
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:4565668"
FT BINDING 176..179
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15086"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15086"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 251..252
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:0000250|UniProtKB:P15086"
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 173..186
FT /evidence="ECO:0000269|PubMed:1057162,
FT ECO:0000269|PubMed:957425"
FT DISULFID 245..268
FT /evidence="ECO:0000269|PubMed:1057162,
FT ECO:0000269|PubMed:957425"
FT DISULFID 259..273
FT /evidence="ECO:0000269|PubMed:1057162,
FT ECO:0000269|PubMed:957425"
FT CONFLICT 347
FT /note="T -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="S -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 47348 MW; 923DABC54214CB27 CRC64;
MLAFLILVTV TLASAHHSGE HFEGDKVFRV HVEDENHISL LHELASTRQM DFWKPDSVTQ
VKPHSTVDFR VKAEDTVAVE DFLGQNGLRY EVLISNLRSM LEAQFDSRVR TTGHSYEKYN
NWETIEAWTE QVASENPDLI SRSAIGTTFL GNTIYLLKVG KPGSNKPAVF MDCGFHAREW
ISPAFCQWFV REAVRTYGRE IHMTEFLDKL DFYVLPVVNI DGYIYTWTTN RMWRKTRSTR
AGSSCTGTDL NRNFDAGWCS IGASNNPCSE TYCGSAAESE KESKAVADFI RNHLSSIKAY
LTIHSYSQMM LYPYSYDYKL PKNNVELNTL AKGAVKKLAS LHGTTYTYGP GASTIYPASG
GSDDWAYDQG IKYSFTFELR DKGRYGFVLP ESQIQPTCEE TMLAIKYVTS YVLEHLY
