CBPB1_PIG
ID CBPB1_PIG Reviewed; 416 AA.
AC P09955; Q9XSP3;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 5.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Carboxypeptidase B;
DE EC=3.4.17.2 {ECO:0000250|UniProtKB:P00732};
DE Flags: Precursor;
GN Name=CPB1; Synonyms=CPB;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=10391940; DOI=10.1074/jbc.274.28.19925;
RA Ventura S., Villegas V., Sterner J., Larson J., Vendrell J.,
RA Hershberger C., Aviles F.X.;
RT "Mapping the pro-region of carboxypeptidase B by protein engineering.
RT Cloning, overexpression, and mutagenesis of the porcine proenzyme.";
RL J. Biol. Chem. 274:19925-19933(1999).
RN [2]
RP PROTEIN SEQUENCE OF 16-118.
RX PubMed=2018774; DOI=10.1021/bi00230a038;
RA Burgos F.J., Salva M., Villegas V., Soriano F., Mendez E., Aviles F.X.;
RT "Analysis of the activation process of porcine procarboxypeptidase B and
RT determination of the sequence of its activation segment.";
RL Biochemistry 30:4082-4089(1991).
RN [3]
RP PRELIMINARY PROTEIN SEQUENCE OF 16-53.
RX PubMed=4026847; DOI=10.1016/0006-291x(85)90387-0;
RA Aviles F.X., Vendrell J., Burgos F.J., Soriano F., Mendez E.;
RT "Sequential homologies between procarboxypeptidases A and B from porcine
RT pancreas.";
RL Biochem. Biophys. Res. Commun. 130:97-103(1985).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 41-416, AND DISULFIDE BONDS.
RX PubMed=1989878; DOI=10.1002/j.1460-2075.1991.tb07914.x;
RA Coll M., Guasch A., Aviles F.X., Huber R.;
RT "Three-dimensional structure of porcine procarboxypeptidase B: a structural
RT basis of its inactivity.";
RL EMBO J. 10:1-9(1991).
RN [5]
RP STRUCTURE BY NMR OF ACTIVATION PEPTIDE, AND PROTEIN SEQUENCE OF 16-96.
RX PubMed=2223783; DOI=10.1021/bi00484a600;
RA Vendrell J., Wider G., Aviles F.X., Wuethrich K.;
RT "Sequence-specific 1H NMR assignments and determination of the secondary
RT structure for the activation domain isolated from pancreatic
RT procarboxypeptidase B.";
RL Biochemistry 29:7515-7522(1990).
RN [6]
RP STRUCTURE BY NMR OF ACTIVATION PEPTIDE.
RX PubMed=1989879; DOI=10.1002/j.1460-2075.1991.tb07915.x;
RA Vendrell J., Billeter M., Wider G., Aviles F.X., Wuethrich K.;
RT "The NMR structure of the activation domain isolated from porcine
RT procarboxypeptidase B.";
RL EMBO J. 10:11-15(1991).
RN [7]
RP STRUCTURE BY NMR OF ACTIVATION PEPTIDE.
RX PubMed=1422143; DOI=10.1007/bf02192796;
RA Billeter M., Vendrell J., Wider G., Aviles F.X., Coll M., Guasch A.,
RA Huber R., Wuethrich K.;
RT "Comparison of the NMR solution structure with the X-ray crystal structure
RT of the activation domain from procarboxypeptidase B.";
RL J. Biomol. NMR 2:1-10(1992).
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 -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/COB/";
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DR EMBL; AJ133775; CAB46991.1; -; mRNA.
DR PIR; A38354; A38354.
DR RefSeq; NP_999334.1; NM_214169.1.
DR PDB; 1NSA; X-ray; 2.30 A; A=22-416.
DR PDB; 1PBA; NMR; -; A=16-96.
DR PDB; 1Z5R; X-ray; 1.40 A; A/B/C=111-416.
DR PDB; 1ZG7; X-ray; 1.75 A; A/B/C=111-416.
DR PDB; 1ZG8; X-ray; 2.00 A; A/B/C=111-416.
DR PDB; 1ZG9; X-ray; 2.00 A; A/B/C=111-416.
DR PDB; 2JEW; X-ray; 1.40 A; A=111-416.
DR PDB; 2PIY; X-ray; 1.43 A; A/B/C=111-416.
DR PDB; 2PIZ; X-ray; 1.60 A; A/B/C=111-416.
DR PDB; 2PJ0; X-ray; 1.65 A; A/B/C=111-416.
DR PDB; 2PJ1; X-ray; 1.64 A; A/B/C=111-416.
DR PDB; 2PJ2; X-ray; 1.95 A; A/B/C=111-416.
DR PDB; 2PJ3; X-ray; 1.64 A; A/B/C=111-416.
DR PDB; 2PJ4; X-ray; 2.00 A; A/B=111-416.
DR PDB; 2PJ5; X-ray; 1.65 A; A/B/C=111-416.
DR PDB; 2PJ6; X-ray; 1.60 A; A=111-416.
DR PDB; 2PJ7; X-ray; 1.77 A; A/B/C=111-416.
DR PDB; 2PJ8; X-ray; 1.70 A; A/B/C=111-416.
DR PDB; 2PJ9; X-ray; 1.56 A; A=111-416.
DR PDB; 2PJA; X-ray; 1.70 A; A/B/C=111-416.
DR PDB; 2PJB; X-ray; 1.70 A; A/B/C=111-416.
DR PDB; 2PJC; X-ray; 1.74 A; A/B/C=111-416.
DR PDB; 3GLJ; X-ray; 1.89 A; A=16-416.
DR PDB; 3WAB; X-ray; 2.15 A; A=111-416.
DR PDB; 3WC5; X-ray; 1.70 A; A=111-416.
DR PDB; 3WC6; X-ray; 1.65 A; A=111-416.
DR PDB; 3WC7; X-ray; 1.90 A; A=111-416.
DR PDB; 4UIA; X-ray; 2.18 A; A=111-416.
DR PDB; 4UIB; X-ray; 1.94 A; A=111-416.
DR PDB; 4Z65; X-ray; 1.25 A; A=113-416.
DR PDB; 5J1Q; X-ray; 1.74 A; A=113-416.
DR PDB; 5JC6; X-ray; 1.40 A; A=113-416.
DR PDB; 5LRG; X-ray; 2.02 A; A/B/C=111-416.
DR PDB; 5LRJ; X-ray; 2.20 A; A/B/C=111-416.
DR PDB; 5LRK; X-ray; 2.30 A; A/B/C=111-416.
DR PDB; 5LYD; X-ray; 2.02 A; A=111-416.
DR PDB; 5LYF; X-ray; 2.01 A; A=111-416.
DR PDB; 5LYI; X-ray; 1.64 A; A=111-416.
DR PDB; 5LYL; X-ray; 1.83 A; A=111-416.
DR PDB; 5ZEQ; X-ray; 1.90 A; A=113-416.
DR PDBsum; 1NSA; -.
DR PDBsum; 1PBA; -.
DR PDBsum; 1Z5R; -.
DR PDBsum; 1ZG7; -.
DR PDBsum; 1ZG8; -.
DR PDBsum; 1ZG9; -.
DR PDBsum; 2JEW; -.
DR PDBsum; 2PIY; -.
DR PDBsum; 2PIZ; -.
DR PDBsum; 2PJ0; -.
DR PDBsum; 2PJ1; -.
DR PDBsum; 2PJ2; -.
DR PDBsum; 2PJ3; -.
DR PDBsum; 2PJ4; -.
DR PDBsum; 2PJ5; -.
DR PDBsum; 2PJ6; -.
DR PDBsum; 2PJ7; -.
DR PDBsum; 2PJ8; -.
DR PDBsum; 2PJ9; -.
DR PDBsum; 2PJA; -.
DR PDBsum; 2PJB; -.
DR PDBsum; 2PJC; -.
DR PDBsum; 3GLJ; -.
DR PDBsum; 3WAB; -.
DR PDBsum; 3WC5; -.
DR PDBsum; 3WC6; -.
DR PDBsum; 3WC7; -.
DR PDBsum; 4UIA; -.
DR PDBsum; 4UIB; -.
DR PDBsum; 4Z65; -.
DR PDBsum; 5J1Q; -.
DR PDBsum; 5JC6; -.
DR PDBsum; 5LRG; -.
DR PDBsum; 5LRJ; -.
DR PDBsum; 5LRK; -.
DR PDBsum; 5LYD; -.
DR PDBsum; 5LYF; -.
DR PDBsum; 5LYI; -.
DR PDBsum; 5LYL; -.
DR PDBsum; 5ZEQ; -.
DR AlphaFoldDB; P09955; -.
DR BMRB; P09955; -.
DR SMR; P09955; -.
DR STRING; 9823.ENSSSCP00000012464; -.
DR BindingDB; P09955; -.
DR ChEMBL; CHEMBL4065; -.
DR MEROPS; M14.003; -.
DR PaxDb; P09955; -.
DR PeptideAtlas; P09955; -.
DR GeneID; 397341; -.
DR KEGG; ssc:397341; -.
DR CTD; 1360; -.
DR eggNOG; KOG2650; Eukaryota.
DR InParanoid; P09955; -.
DR OMA; LYKAYGC; -.
DR BRENDA; 3.4.17.2; 6170.
DR EvolutionaryTrace; P09955; -.
DR PRO; PR:P09955; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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 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..15
FT /evidence="ECO:0000269|PubMed:2018774,
FT ECO:0000269|PubMed:2223783"
FT PROPEP 16..110
FT /note="Activation peptide"
FT /id="PRO_0000004373"
FT CHAIN 111..416
FT /note="Carboxypeptidase B"
FT /id="PRO_0000004374"
FT ACT_SITE 378
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00732"
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:1989878"
FT DISULFID 245..268
FT /evidence="ECO:0000269|PubMed:1989878"
FT DISULFID 259..273
FT /evidence="ECO:0000269|PubMed:1989878"
FT CONFLICT 40
FT /note="L -> E (in Ref. 2; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:1PBA"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:3GLJ"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:3GLJ"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:3GLJ"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:3GLJ"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:3GLJ"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:3GLJ"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:3GLJ"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:3GLJ"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:3GLJ"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:2PJ9"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:4Z65"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:4Z65"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:4Z65"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:4Z65"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:4Z65"
FT HELIX 180..196
FT /evidence="ECO:0007829|PDB:4Z65"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:4Z65"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:4Z65"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:4Z65"
FT HELIX 220..228
FT /evidence="ECO:0007829|PDB:4Z65"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:2PJ6"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:4Z65"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:4Z65"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:1Z5R"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:2JEW"
FT HELIX 281..292
FT /evidence="ECO:0007829|PDB:4Z65"
FT TURN 293..296
FT /evidence="ECO:0007829|PDB:4Z65"
FT STRAND 297..304
FT /evidence="ECO:0007829|PDB:4Z65"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:4Z65"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:4Z65"
FT HELIX 324..339
FT /evidence="ECO:0007829|PDB:4Z65"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:4Z65"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:4Z65"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:4Z65"
FT HELIX 362..368
FT /evidence="ECO:0007829|PDB:4Z65"
FT STRAND 372..378
FT /evidence="ECO:0007829|PDB:4Z65"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:4Z65"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:4Z65"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:4Z65"
FT HELIX 394..414
FT /evidence="ECO:0007829|PDB:4Z65"
SQ SEQUENCE 416 AA; 47381 MW; 5FA7FCED7B45AE6A CRC64;
MLAFLILVTV TLASAHHSGE HFEGEKVFRV NVEDENDISL LHELASTRQI DFWKPDSVTQ
IKPHSTVDFR VKAEDILAVE DFLEQNELQY EVLINNLRSV LEAQFDSRVR TTGHSYEKYN
NWETIEAWTK QVTSENPDLI SRTAIGTTFL GNNIYLLKVG KPGPNKPAIF MDCGFHAREW
ISHAFCQWFV REAVLTYGYE SHMTEFLNKL DFYVLPVLNI DGYIYTWTKN RMWRKTRSTN
AGTTCIGTDP NRNFDAGWCT TGASTDPCDE TYCGSAAESE KETKALADFI RNNLSSIKAY
LTIHSYSQMI LYPYSYDYKL PENNAELNNL AKAAVKELAT LYGTKYTYGP GATTIYPAAG
GSDDWAYDQG IKYSFTFELR DKGRYGFILP ESQIQATCEE TMLAIKYVTN YVLGHL
