ID   CTRB_GADMO              Reviewed;         245 AA.
AC   P80646;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=Chymotrypsin 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   Flags: Precursor;
OS   Gadus morhua (Atlantic cod).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX   NCBI_TaxID=8049;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Pyloric caecum;
RX   PubMed=8841380; DOI=10.1016/0167-4838(96)00088-x;
RA   Leth-Larsen R., Asgeirsson B., Thorolfsson M., Noerregaard-Madsen M.,
RA   Hoejrup P.;
RT   "Structure of chymotrypsin variant B from Atlantic cod, Gadus morhua.";
RL   Biochim. Biophys. Acta 1297:49-56(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-12 AND 16-31.
RC   TISSUE=Pyloric caecum;
RX   PubMed=1764912; DOI=10.1016/0305-0491(91)90050-n;
RA   Asgeirsson B., Bjarnason J.B.;
RT   "Structural and kinetic properties of chymotrypsin from Atlantic cod (Gadus
RT   morhua). Comparison with bovine chymotrypsin.";
RL   Comp. Biochem. Physiol. 99B:327-335(1991).
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}.
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DR   AlphaFoldDB; P80646; -.
DR   SMR; P80646; -.
DR   STRING; 8049.ENSGMOP00000010246; -.
DR   MEROPS; S01.437; -.
DR   HOGENOM; CLU_006842_7_6_1; -.
DR   TreeFam; TF330455; -.
DR   Proteomes; UP000694546; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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   PANTHER; PTHR24250; CHYMOTRYPSIN-RELATED; 1.
DR   PANTHER; PTHR24250:SF54; ZGC:112160; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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   Digestion; Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Zymogen.
FT   CHAIN           1..13
FT                   /note="Chymotrypsin B chain A"
FT                   /id="PRO_0000027647"
FT   PROPEP          14..15
FT                   /evidence="ECO:0000269|PubMed:1764912"
FT                   /id="PRO_0000027648"
FT   CHAIN           16..245
FT                   /note="Chymotrypsin B chain B"
FT                   /id="PRO_0000027649"
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:0000250"
FT   ACT_SITE        101
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        195
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        1..121
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        42..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        135..201
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        167..182
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        191..220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        9..11
FT                   /note="QVT -> VIS (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        26
FT                   /note="S -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        28..29
FT                   /note="PW -> Y (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   245 AA;  26260 MW;  74FE0D425517AB02 CRC64;
     CGSPAIQPQV TGYARIVNGE EAVPHSWPWQ VSLQQSNGFH FCGGSLINEN WVVTAAHCNV
     RTYHRVIVGE HDKASDENIQ ILKPSMVFTH PKWDSRTINN DISLIKLASP AVLGTNVSPV
     CLGESSDVFA PGMKCVTSGW GLTRYNAPGT PNKLQQAALP LMSNEECSQT WGNNMISDVM
     ICAGAAGATS CMGDSGGPLV CQKDNVWTLV GIVSWGSSRC SVTTPAVYAR VTELRGWVDQ
     ILAAN
//