ID   CTRB_BOVIN              Reviewed;         245 AA.
AC   P00767;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 133.
DE   RecName: Full=Chymotrypsinogen B;
DE            EC=3.4.21.1;
DE   Contains:
DE     RecName: Full=Chymotrypsin B chain A;
DE   Contains:
DE     RecName: Full=Chymotrypsin B chain B;
DE   Contains:
DE     RecName: Full=Chymotrypsin B chain C;
DE   Flags: Precursor;
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   PROTEIN SEQUENCE, DISULFIDE BONDS, AND ACTIVE SITE.
RX   PubMed=5649671; DOI=10.1038/218343a0;
RA   Smillie L.B., Furka A., Nagabhushan N., Stevenson K.J., Parkes C.O.;
RT   "Structure of chymotrypsinogen B compared with chymotrypsinogen A and
RT   trypsinogen.";
RL   Nature 218:343-346(1968).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-
CC         Xaa.; EC=3.4.21.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10078,
CC         ECO:0000255|PROSITE-ProRule:PRU10079};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
CC   -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC       URL="https://www.worthington-biochem.com/CHY/";
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DR   PIR; A00953; KYBOB.
DR   PDB; 1CBW; X-ray; 2.60 A; A/F=1-13.
DR   PDB; 1HJA; X-ray; 2.30 A; A=1-13.
DR   PDB; 3BG4; X-ray; 2.50 A; A=1-13.
DR   PDBsum; 1CBW; -.
DR   PDBsum; 1HJA; -.
DR   PDBsum; 3BG4; -.
DR   AlphaFoldDB; P00767; -.
DR   SMR; P00767; -.
DR   STRING; 9913.ENSBTAP00000011204; -.
DR   BindingDB; P00767; -.
DR   ChEMBL; CHEMBL3063; -.
DR   MEROPS; S01.152; -.
DR   PaxDb; P00767; -.
DR   PRIDE; P00767; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   EvolutionaryTrace; P00767; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Digestion; Direct protein sequencing; Disulfide bond;
KW   Hydrolase; Protease; Reference proteome; Secreted; Serine protease;
KW   Zymogen.
FT   CHAIN           1..13
FT                   /note="Chymotrypsin B chain A"
FT                   /id="PRO_0000027629"
FT   PROPEP          14..15
FT                   /id="PRO_0000027630"
FT   CHAIN           16..146
FT                   /note="Chymotrypsin B chain B"
FT                   /id="PRO_0000027631"
FT   PROPEP          147..148
FT                   /id="PRO_0000027632"
FT   CHAIN           149..245
FT                   /note="Chymotrypsin B chain C"
FT                   /id="PRO_0000027633"
FT   DOMAIN          16..243
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        57
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000269|PubMed:5649671"
FT   ACT_SITE        102
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000269|PubMed:5649671"
FT   ACT_SITE        195
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000269|PubMed:5649671"
FT   DISULFID        1..122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:5649671"
FT   DISULFID        42..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:5649671"
FT   DISULFID        136..201
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:5649671"
FT   DISULFID        168..182
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:5649671"
FT   DISULFID        191..220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT                   ECO:0000269|PubMed:5649671"
SQ   SEQUENCE   245 AA;  25755 MW;  678016446FF5FEB5 CRC64;
     CGVPAIQPVL SGLARIVNGE DAVPGSWPWQ VSLQDSTGFH FCGGSLISED WVVTAAHCGV
     TTSDVVVAGE FDQGLETEDT QVLKIGKVFK NPKFSILTVR NDITLLKLAT PAQFSETVSA
     VCLPSADEDF PAGMLCATTG WGKTKYNALK TPDKLQQATL PIVSNTDCRK YWGSRVTDVM
     ICAGASGVSS CMGDSGGPLV CQKNGAWTLA GIVSWGSSTC STSTPAVYAR VTALMPWVQE
     TLAAN