CTRA_BOVIN
ID CTRA_BOVIN Reviewed; 245 AA.
AC P00766;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 181.
DE RecName: Full=Chymotrypsinogen A;
DE EC=3.4.21.1;
DE Contains:
DE RecName: Full=Chymotrypsin A chain A;
DE Contains:
DE RecName: Full=Chymotrypsin A chain B;
DE Contains:
DE RecName: Full=Chymotrypsin A 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=5971783; DOI=10.1042/bj1010214;
RA Brown J.R., Hartley B.S.;
RT "Location of disulphide bridges by diagonal paper electrophoresis. The
RT disulphide bridges of bovine chymotrypsinogen A.";
RL Biochem. J. 101:214-228(1966).
RN [2]
RP SEQUENCE REVISION TO 102.
RX PubMed=5764436; DOI=10.1038/221337a0;
RA Blow D.M., Birktoft J.J., Hartley B.S.;
RT "Role of a buried acid group in the mechanism of action of chymotrypsin.";
RL Nature 221:337-340(1969).
RN [3]
RP PRELIMINARY PROTEIN SEQUENCE.
RX PubMed=14151403; DOI=10.1038/2011284a0;
RA Hartley B.S.;
RT "Amino-acid sequence of bovine chymotrypsinogen-A.";
RL Nature 201:1284-1287(1964).
RN [4]
RP PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RX PubMed=5972866; DOI=10.1016/0304-4165(66)90258-3;
RA Meloun B., Kluh I., Kostka V., Moravek L., Prusik Z., Vanacek J., Keil B.,
RA Sorm F.;
RT "Covalent structure of bovine chymotrypsinogen A.";
RL Biochim. Biophys. Acta 130:543-546(1966).
RN [5]
RP ACTIVE SITE.
RX PubMed=5971785; DOI=10.1042/bj1010232;
RA Smillie L.B., Hartley B.S.;
RT "Histidine sequences in the active centres of some 'serine' proteinases.";
RL Biochem. J. 101:232-241(1966).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=4399050; DOI=10.1098/rstb.1970.0009;
RA Birktoft J.J., Blow D.M., Henderson R., Steitz T.A.;
RT "I. Serine proteinases. The structure of alpha-chymotrypsin.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 257:67-76(1970).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF CHYMOTRYPSINOGEN.
RX PubMed=5442169; DOI=10.1021/bi00811a022;
RA Freer S.T., Kraut J., Robertus J.D., Wright H.T., Xuong N.H.;
RT "Chymotrypsinogen: 2.5-A crystal structure, comparison with alpha-
RT chymotrypsin, and implications for zymogen activation.";
RL Biochemistry 9:1997-2009(1970).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF GAMMA-CHYMOTRYPSIN.
RX PubMed=6914398; DOI=10.1016/0022-2836(81)90186-8;
RA Cohen G.H., Silverton E.W., Davies D.R.;
RT "Refined crystal structure of gamma-chymotrypsin at 1.9-A resolution.
RT Comparison with other pancreatic serine proteases.";
RL J. Mol. Biol. 148:449-479(1981).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF ALPHA-CHYMOTRYPSIN.
RX PubMed=4046030; DOI=10.1016/0022-2836(85)90314-6;
RA Tsukada H., Blow D.M.;
RT "Structure of alpha-chymotrypsin refined at 1.68-A resolution.";
RL J. Mol. Biol. 184:703-711(1985).
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 -!- INTERACTION:
CC P00766; P10184: SPINK5; Xeno; NbExp=2; IntAct=EBI-6664027, EBI-6663991;
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; A90235; KYBOA.
DR PDB; 1AB9; X-ray; 1.60 A; A=1-13, B=16-146, C=149-245.
DR PDB; 1ACB; X-ray; 2.00 A; E=1-245.
DR PDB; 1AFQ; X-ray; 1.80 A; A=1-13, B=16-146, C=150-245.
DR PDB; 1CA0; X-ray; 2.10 A; A/F=1-13, B/G=16-146, C/H=149-245.
DR PDB; 1CBW; X-ray; 2.60 A; B/G=16-146, C/H=149-245.
DR PDB; 1CGI; X-ray; 2.30 A; E=1-245.
DR PDB; 1CGJ; X-ray; 2.30 A; E=1-245.
DR PDB; 1CHG; X-ray; 2.50 A; A=1-245.
DR PDB; 1CHO; X-ray; 1.80 A; E=1-13, F=16-146, G=149-245.
DR PDB; 1DLK; X-ray; 2.14 A; A/C=1-13, B/D=16-245.
DR PDB; 1EX3; X-ray; 3.00 A; A=1-245.
DR PDB; 1GCD; X-ray; 1.90 A; A=1-245.
DR PDB; 1GCT; X-ray; 1.60 A; A=1-13, B=16-146, C=149-245.
DR PDB; 1GG6; X-ray; 1.40 A; A=1-10, B=16-146, C=149-245.
DR PDB; 1GGD; X-ray; 1.50 A; A=1-10, B=16-146, C=149-245.
DR PDB; 1GHA; X-ray; 2.20 A; E=1-13, F=16-146, G=149-245.
DR PDB; 1GHB; X-ray; 2.00 A; E=1-13, F=16-146, G=149-245.
DR PDB; 1GL0; X-ray; 3.00 A; E=1-245.
DR PDB; 1GL1; X-ray; 2.10 A; A/B/C=1-245.
DR PDB; 1GMC; X-ray; 2.20 A; E=1-13, F=16-146, G=149-245.
DR PDB; 1GMD; X-ray; 2.20 A; E=1-13, F=16-146, G=149-245.
DR PDB; 1GMH; X-ray; 2.10 A; E=1-13, F=16-146, G=149-245.
DR PDB; 1HJA; X-ray; 2.30 A; A=1-13, B=16-146, C=149-245.
DR PDB; 1K2I; X-ray; 1.80 A; 1=1-245.
DR PDB; 1MTN; X-ray; 2.80 A; A/E=1-13, B/F=16-146, C/G=149-245.
DR PDB; 1N8O; X-ray; 2.00 A; A=1-13, B=16-146, C=149-245.
DR PDB; 1OXG; X-ray; 2.20 A; A=1-245, B=16-29.
DR PDB; 1P2M; X-ray; 1.75 A; A/C=1-245.
DR PDB; 1P2N; X-ray; 1.80 A; A/C=1-245.
DR PDB; 1P2O; X-ray; 2.00 A; A/C=1-245.
DR PDB; 1P2Q; X-ray; 1.80 A; A/C=1-245.
DR PDB; 1T7C; X-ray; 1.85 A; A/C=1-245.
DR PDB; 1T8L; X-ray; 1.75 A; A/C=1-245.
DR PDB; 1T8M; X-ray; 1.80 A; A/C=1-245.
DR PDB; 1T8N; X-ray; 1.75 A; A/C=1-245.
DR PDB; 1T8O; X-ray; 1.70 A; A/C=1-245.
DR PDB; 1VGC; X-ray; 1.90 A; A=1-13, B=16-146, C=149-245.
DR PDB; 1YPH; X-ray; 1.34 A; A/B=1-13, C/D=16-146, E/F=149-245.
DR PDB; 2CGA; X-ray; 1.80 A; A/B=1-245.
DR PDB; 2CHA; X-ray; 2.00 A; A/E=1-13, B/F=16-146, C/G=149-245.
DR PDB; 2GCH; X-ray; 1.90 A; E=1-13, F=16-146, G=149-245.
DR PDB; 2GCT; X-ray; 1.80 A; A=1-13, B=16-146, C=149-245.
DR PDB; 2GMT; X-ray; 1.80 A; A=1-13, B=16-146, C=149-245.
DR PDB; 2P8O; X-ray; 1.50 A; A=1-13, B=16-146, C=149-245.
DR PDB; 2VGC; X-ray; 1.80 A; A=1-13, B=16-146, C=149-245.
DR PDB; 2Y6T; X-ray; 2.74 A; A/B/C/D=1-245.
DR PDB; 3BG4; X-ray; 2.50 A; B=16-146, C=149-245.
DR PDB; 3GCH; X-ray; 1.90 A; A=1-13, B=16-146, C=149-245.
DR PDB; 3GCT; X-ray; 1.60 A; E=1-13, F=16-146, G=149-245.
DR PDB; 3RU4; X-ray; 1.68 A; C=1-11, D=16-146, E=150-245.
DR PDB; 3T62; X-ray; 2.00 A; A/B/C=1-245.
DR PDB; 3VGC; X-ray; 1.67 A; A=1-13, B=16-146, C=149-245.
DR PDB; 4CHA; X-ray; 1.68 A; A/E=1-13, B/F=16-146, C/G=149-245.
DR PDB; 4GCH; X-ray; 1.90 A; E=1-13, F=16-146, G=149-245.
DR PDB; 4Q2K; X-ray; 2.20 A; A/B/C/D=1-245.
DR PDB; 4VGC; X-ray; 2.10 A; A=1-13, B=16-146, C=149-245.
DR PDB; 5CHA; X-ray; 1.67 A; A/E=1-13, B/F=16-146, C/G=149-245.
DR PDB; 5GCH; X-ray; 2.70 A; E=1-13, F=16-146, G=149-245.
DR PDB; 5J4Q; X-ray; 2.30 A; A=1-245.
DR PDB; 5J4S; X-ray; 2.10 A; A=1-245.
DR PDB; 6CHA; X-ray; 1.80 A; A/E=1-13, B/F=16-146, C/G=149-245.
DR PDB; 6GCH; X-ray; 2.10 A; E=1-13, F=16-146, G=149-245.
DR PDB; 7GCH; X-ray; 1.80 A; E=1-13, F=16-146, G=149-245.
DR PDB; 7KTY; X-ray; 2.00 A; A=1-245.
DR PDB; 7KTZ; X-ray; 2.00 A; A=1-245.
DR PDB; 7KU0; X-ray; 2.02 A; A=1-245.
DR PDB; 7KU1; X-ray; 2.39 A; A=1-245.
DR PDB; 7KU2; X-ray; 2.19 A; A=1-245.
DR PDB; 7KU3; X-ray; 2.00 A; A=1-245.
DR PDB; 8GCH; X-ray; 1.60 A; E=1-13, F=16-146, G=149-245.
DR PDBsum; 1AB9; -.
DR PDBsum; 1ACB; -.
DR PDBsum; 1AFQ; -.
DR PDBsum; 1CA0; -.
DR PDBsum; 1CBW; -.
DR PDBsum; 1CGI; -.
DR PDBsum; 1CGJ; -.
DR PDBsum; 1CHG; -.
DR PDBsum; 1CHO; -.
DR PDBsum; 1DLK; -.
DR PDBsum; 1EX3; -.
DR PDBsum; 1GCD; -.
DR PDBsum; 1GCT; -.
DR PDBsum; 1GG6; -.
DR PDBsum; 1GGD; -.
DR PDBsum; 1GHA; -.
DR PDBsum; 1GHB; -.
DR PDBsum; 1GL0; -.
DR PDBsum; 1GL1; -.
DR PDBsum; 1GMC; -.
DR PDBsum; 1GMD; -.
DR PDBsum; 1GMH; -.
DR PDBsum; 1HJA; -.
DR PDBsum; 1K2I; -.
DR PDBsum; 1MTN; -.
DR PDBsum; 1N8O; -.
DR PDBsum; 1OXG; -.
DR PDBsum; 1P2M; -.
DR PDBsum; 1P2N; -.
DR PDBsum; 1P2O; -.
DR PDBsum; 1P2Q; -.
DR PDBsum; 1T7C; -.
DR PDBsum; 1T8L; -.
DR PDBsum; 1T8M; -.
DR PDBsum; 1T8N; -.
DR PDBsum; 1T8O; -.
DR PDBsum; 1VGC; -.
DR PDBsum; 1YPH; -.
DR PDBsum; 2CGA; -.
DR PDBsum; 2CHA; -.
DR PDBsum; 2GCH; -.
DR PDBsum; 2GCT; -.
DR PDBsum; 2GMT; -.
DR PDBsum; 2P8O; -.
DR PDBsum; 2VGC; -.
DR PDBsum; 2Y6T; -.
DR PDBsum; 3BG4; -.
DR PDBsum; 3GCH; -.
DR PDBsum; 3GCT; -.
DR PDBsum; 3RU4; -.
DR PDBsum; 3T62; -.
DR PDBsum; 3VGC; -.
DR PDBsum; 4CHA; -.
DR PDBsum; 4GCH; -.
DR PDBsum; 4Q2K; -.
DR PDBsum; 4VGC; -.
DR PDBsum; 5CHA; -.
DR PDBsum; 5GCH; -.
DR PDBsum; 5J4Q; -.
DR PDBsum; 5J4S; -.
DR PDBsum; 6CHA; -.
DR PDBsum; 6GCH; -.
DR PDBsum; 7GCH; -.
DR PDBsum; 7KTY; -.
DR PDBsum; 7KTZ; -.
DR PDBsum; 7KU0; -.
DR PDBsum; 7KU1; -.
DR PDBsum; 7KU2; -.
DR PDBsum; 7KU3; -.
DR PDBsum; 8GCH; -.
DR AlphaFoldDB; P00766; -.
DR BMRB; P00766; -.
DR PCDDB; P00766; -.
DR SASBDB; P00766; -.
DR SMR; P00766; -.
DR DIP; DIP-6068N; -.
DR IntAct; P00766; 2.
DR MINT; P00766; -.
DR STRING; 9913.ENSBTAP00000015915; -.
DR BindingDB; P00766; -.
DR ChEMBL; CHEMBL3314; -.
DR DrugCentral; P00766; -.
DR MEROPS; S01.001; -.
DR MetOSite; P00766; -.
DR PaxDb; P00766; -.
DR PRIDE; P00766; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_7_6_1; -.
DR BRENDA; 3.4.21.1; 908.
DR EvolutionaryTrace; P00766; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0097180; C:serine protease inhibitor complex; IDA:CAFA.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0097655; F:serpin family protein binding; IDA:CAFA.
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; -; 2.
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 A chain A"
FT /id="PRO_0000027624"
FT PROPEP 14..15
FT /id="PRO_0000027625"
FT CHAIN 16..146
FT /note="Chymotrypsin A chain B"
FT /id="PRO_0000027626"
FT PROPEP 147..148
FT /id="PRO_0000027627"
FT CHAIN 149..245
FT /note="Chymotrypsin A chain C"
FT /id="PRO_0000027628"
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 ACT_SITE 102
FT /note="Charge relay system"
FT ACT_SITE 195
FT /note="Charge relay system"
FT DISULFID 1..122
FT DISULFID 42..58
FT DISULFID 136..201
FT DISULFID 168..182
FT DISULFID 191..220
FT HELIX 12..15
FT /evidence="ECO:0007829|PDB:2CGA"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1CGI"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1OXG"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1YPH"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:6CHA"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:1YPH"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1YPH"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1YPH"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1YPH"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:2GCT"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1YPH"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:1YPH"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1YPH"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:1YPH"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6CHA"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:1YPH"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:2CGA"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:2CGA"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:1YPH"
FT HELIX 165..172
FT /evidence="ECO:0007829|PDB:1YPH"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1YPH"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:1YPH"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2CGA"
FT TURN 192..196
FT /evidence="ECO:0007829|PDB:1GMD"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:1YPH"
FT STRAND 206..215
FT /evidence="ECO:0007829|PDB:1YPH"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:1YPH"
FT HELIX 231..244
FT /evidence="ECO:0007829|PDB:1YPH"
SQ SEQUENCE 245 AA; 25666 MW; 91A9F28E2F3E3142 CRC64;
CGVPAIQPVL SGLSRIVNGE EAVPGSWPWQ VSLQDKTGFH FCGGSLINEN WVVTAAHCGV
TTSDVVVAGE FDQGSSSEKI QKLKIAKVFK NSKYNSLTIN NDITLLKLST AASFSQTVSA
VCLPSASDDF AAGTTCVTTG WGLTRYTNAN TPDRLQQASL PLLSNTNCKK YWGTKIKDAM
ICAGASGVSS CMGDSGGPLV CKKNGAWTLV GIVSWGSSTC STSTPGVYAR VTALVNWVQQ
TLAAN
