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 27-MAR-2024, entry version 187. 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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 BindingDB; P00766; -. DR ChEMBL; CHEMBL3314; -. DR DrugCentral; P00766; -. DR MEROPS; S01.001; -. DR MetOSite; P00766; -. DR PaxDb; 9913-ENSBTAP00000015915; -. DR eggNOG; KOG3627; Eukaryota. DR HOGENOM; CLU_006842_7_6_1; -. DR InParanoid; P00766; -. DR BRENDA; 3.4.21.1; 908. DR EvolutionaryTrace; P00766; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0005576; C:extracellular region; 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; Trypsin-like serine proteases; 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 PANTHER; PTHR24250; CHYMOTRYPSIN-RELATED; 1. DR PANTHER; PTHR24250:SF60; CHYMOTRYPSINOGEN B; 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 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 //