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
//
