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UniProtKB/Swiss-Prot entry P00766

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CTRA_BOVIN
Primary accession number P00766
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 93)
Name and origin of the protein
Protein name Chymotrypsinogen A
Synonym EC 3.4.21.1
Contains Chymotrypsin A chain A
Chymotrypsin A chain B
Chymotrypsin A chain C
Gene name None
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 1: Evidence at protein level;
References
[1]
 PROTEIN SEQUENCE, DISULFIDE BONDS, AND ACTIVE SITE.
PubMed=5971783 [NCBI, ExPASy, EBI, Israel, Japan]
Brown J.R., Hartley B.S.;
"Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A.";
Biochem. J. 101:214-228(1966).
[2]
 SEQUENCE REVISION TO 102.
PubMed=5764436 [NCBI, ExPASy, EBI, Israel, Japan]
Blow D.M., Birktoft J.J., Hartley B.S.;
"Role of a buried acid group in the mechanism of action of chymotrypsin.";
Nature 221:337-340(1969).
[3]
 PRELIMINARY PROTEIN SEQUENCE.
PubMed=14151403 [NCBI, ExPASy, EBI, Israel, Japan]
Hartley B.S.;
"Amino-acid sequence of bovine chymotrypsinogen-A.";
Nature 201:1284-1287(1964).
[4]
 PROTEIN SEQUENCE, AND DISULFIDE BONDS.
PubMed=5972866 [NCBI, ExPASy, EBI, Israel, Japan]
Meloun B., Kluh I., Kostka V., Moravek L., Prusik Z., Vanacek J., Keil B., Sorm F.;
"Covalent structure of bovine chymotrypsinogen A.";
Biochim. Biophys. Acta 130:543-546(1966).
[5]
 ACTIVE SITE.
PubMed=5971785 [NCBI, ExPASy, EBI, Israel, Japan]
Smillie L.B., Hartley B.S.;
"Histidine sequences in the active centres of some 'serine' proteinases.";
Biochem. J. 101:232-241(1966).
[6]
 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=4399050 [NCBI, ExPASy, EBI, Israel, Japan]
Birktoft J.J., Blow D.M., Henderson R., Steitz T.A.;
"I. Serine proteinases. The structure of alpha-chymotrypsin.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 257:67-76(1970).
[7]
 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF CHYMOTRYPSINOGEN.
DOI=10.1021/bi00811a022; PubMed=5442169 [NCBI, ExPASy, EBI, Israel, Japan]
Freer S.T., Kraut J., Robertus J.D., Wright H.T., Xuong N.H.;
"Chymotrypsinogen: 2.5-A crystal structure, comparison with alpha-chymotrypsin, and implications for zymogen activation.";
Biochemistry 9:1997-2009(1970).
[8]
 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF GAMMA-CHYMOTRYPSIN.
DOI=10.1016/0022-2836(81)90186-8; PubMed=6914398 [NCBI, ExPASy, EBI, Israel, Japan]
Cohen G.H., Silverton E.W., Davies D.R.;
"Refined crystal structure of gamma-chymotrypsin at 1.9-A resolution. Comparison with other pancreatic serine proteases.";
J. Mol. Biol. 148:449-479(1981).
[9]
 X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF ALPHA-CHYMOTRYPSIN.
DOI=10.1016/0022-2836(85)90314-6; PubMed=4046030 [NCBI, ExPASy, EBI, Israel, Japan]
Tsukada H., Blow D.M.;
"Structure of alpha-chymotrypsin refined at 1.68-A resolution.";
J. Mol. Biol. 184:703-711(1985).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
PIR A90235; KYBOA.
UniGene Bt.62239
3D structure databases
PDB
1AB9; X-ray; 1.60 A; A=1-13, B=16-146, C=149-245.[ExPASy / RCSB / EBI]
1ACB; X-ray; 2.00 A; E=1-245.[ExPASy / RCSB / EBI]
1AFQ; X-ray; 1.80 A; B=16-146, C=150-245.[ExPASy / RCSB / EBI]
1CA0; X-ray; 2.10 A; A/F=1-13, B/G=16-146, C/H=149-245.[ExPASy / RCSB / EBI]
1CBW; X-ray; 2.60 A; B/G=16-146, C/H=149-245.[ExPASy / RCSB / EBI]
1CGI; X-ray; 2.30 A; E=1-245.[ExPASy / RCSB / EBI]
1CGJ; X-ray; 2.30 A; E=1-245.[ExPASy / RCSB / EBI]
1CHG; X-ray; 2.50 A; A=1-245.[ExPASy / RCSB / EBI]
1CHO; X-ray; 1.80 A; E=1-13, F=16-146, G=149-245.[ExPASy / RCSB / EBI]
1DLK; X-ray; 2.14 A; A/C=1-13, B/D=16-245.[ExPASy / RCSB / EBI]
1EX3; X-ray; 3.00 A; A=1-245.[ExPASy / RCSB / EBI]
1GCD; X-ray; 1.90 A; A=1-245.[ExPASy / RCSB / EBI]
1GCT; X-ray; 1.60 A; A=1-245.[ExPASy / RCSB / EBI]
1GG6; X-ray; 1.40 A; A=1-10, B=16-146, C=149-245.[ExPASy / RCSB / EBI]
1GGD; X-ray; 1.50 A; A=1-10, B=16-146, C=149-245.[ExPASy / RCSB / EBI]
1GHA; X-ray; 2.20 A; E=1-13, F=16-146, G=149-245.[ExPASy / RCSB / EBI]
1GHB; X-ray; 2.00 A; E=1-13.[ExPASy / RCSB / EBI]
1GL0; X-ray; 3.00 A; E=1-245.[ExPASy / RCSB / EBI]
1GL1; X-ray; 2.10 A; A/B/C=1-245.[ExPASy / RCSB / EBI]
1GMC; X-ray; 2.20 A; A=-, F=16-146.[ExPASy / RCSB / EBI]
1GMD; X-ray; 2.20 A; A=-, F=16-146.[ExPASy / RCSB / EBI]
1GMH; X-ray; 2.10 A; F=16-146, G=149-245.[ExPASy / RCSB / EBI]
1HJA; X-ray; 2.30 A; B=16-146, C=149-245.[ExPASy / RCSB / EBI]
1K2I; X-ray; 1.80 A; 1=1-245.[ExPASy / RCSB / EBI]
1MTN; X-ray; 2.80 A; A/E=1-13, B/F=16-146, C/G=149-245.[ExPASy / RCSB / EBI]
1N8O; X-ray; 2.00 A; A=1-13, B=16-146, C=149-245.[ExPASy / RCSB / EBI]
1OXG; X-ray; 2.20 A; A=1-245, B=16-29.[ExPASy / RCSB / EBI]
1P2M; X-ray; 1.75 A; A/C=1-245.[ExPASy / RCSB / EBI]
1P2N; X-ray; 1.80 A; A/C=1-245.[ExPASy / RCSB / EBI]
1P2O; X-ray; 2.00 A; A/C=1-245.[ExPASy / RCSB / EBI]
1P2Q; X-ray; 1.80 A; A/C=1-245.[ExPASy / RCSB / EBI]
1T7C; X-ray; 1.85 A; A/C=1-245.[ExPASy / RCSB / EBI]
1T8L; X-ray; 1.75 A; A/C=1-245.[ExPASy / RCSB / EBI]
1T8M; X-ray; 1.80 A; A/C=1-245.[ExPASy / RCSB / EBI]
1T8N; X-ray; 1.75 A; A/C=1-245.[ExPASy / RCSB / EBI]
1T8O; X-ray; 1.70 A; A/C=1-245.[ExPASy / RCSB / EBI]
1VGC; X-ray; 1.90 A; A=1-13, B=16-146, C=149-245.[ExPASy / RCSB / EBI]
1YPH; X-ray; 1.34 A; A/B=1-13, C/D=16-146, E/F=149-245.[ExPASy / RCSB / EBI]
2CGA; X-ray; 1.80 A; A/B=1-245.[ExPASy / RCSB / EBI]
2CHA; X-ray; 2.00 A; A/E=1-13, B/F=16-146, C/G=149-245.[ExPASy / RCSB / EBI]
2GCH; X-ray; 1.90 A; F=16-146, G=149-245.[ExPASy / RCSB / EBI]
2GCT; X-ray; 1.80 A; A=1-245.[ExPASy / RCSB / EBI]
2GMT; X-ray; 1.80 A; A=1-245.[ExPASy / RCSB / EBI]
2P8O; X-ray; 1.50 A; A=1-13, B=16-146, C=149-245.[ExPASy / RCSB / EBI]
2VGC; X-ray; 1.80 A; A=1-13, B=16-146, C=149-245.[ExPASy / RCSB / EBI]
3BG4; X-ray; 2.50 A; B=16-146, C=149-245.[ExPASy / RCSB / EBI]
3GCH; X-ray; 1.90 A; A=1-245.[ExPASy / RCSB / EBI]
3GCT; X-ray; 1.60 A; A=-, F=16-146.[ExPASy / RCSB / EBI]
3VGC; X-ray; 1.67 A; A=1-13, B=16-146, C=149-245.[ExPASy / RCSB / EBI]
4CHA; X-ray; 1.68 A; A=1-13, B/F=16-146, C/G=149-245.[ExPASy / RCSB / EBI]
4GCH; X-ray; 1.90 A; E=1-13, F=16-146, G=149-245.[ExPASy / RCSB / EBI]
4VGC; X-ray; 2.10 A; A=1-13, B=16-146, C=149-245.[ExPASy / RCSB / EBI]
5CHA; X-ray; 1.67 A; A/E=1-13, B/F=16-146, C/G=149-245.[ExPASy / RCSB / EBI]
5GCH; X-ray; 2.70 A; F=16-146, G=149-245.[ExPASy / RCSB / EBI]
6CHA; X-ray; 1.80 A; A/E=1-13, B/F=16-146, C/G=149-245.[ExPASy / RCSB / EBI]
6GCH; X-ray; 2.10 A; E=1-13, F=16-146, G=149-245.[ExPASy / RCSB / EBI]
7GCH; X-ray; 1.80 A; E=1-13, F=16-146, G=149-245.[ExPASy / RCSB / EBI]
8GCH; X-ray; 1.60 A; F=16-146, G=149-245.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AB9; -.
1ACB; -.
1AFQ; -.
1CA0; -.
1CBW; -.
1CGI; -.
1CGJ; -.
1CHG; -.
1CHO; -.
1DLK; -.
1EX3; -.
1GCD; -.
1GCT; -.
1GG6; -.
1GGD; -.
1GHA; -.
1GHB; -.
1GL0; -.
1GL1; -.
1GMC; -.
1GMD; -.
1GMH; -.
1HJA; -.
1K2I; -.
1MTN; -.
1N8O; -.
1OXG; -.
1P2M; -.
1P2N; -.
1P2O; -.
1P2Q; -.
1T7C; -.
1T8L; -.
1T8M; -.
1T8N; -.
1T8O; -.
1VGC; -.
1YPH; -.
2CGA; -.
2CHA; -.
2GCH; -.
2GCT; -.
2GMT; -.
2P8O; -.
2VGC; -.
3BG4; -.
3GCH; -.
3GCT; -.
3VGC; -.
4CHA; -.
4GCH; -.
4VGC; -.
5CHA; -.
5GCH; -.
6CHA; -.
6GCH; -.
7GCH; -.
8GCH; -.
ModBase P00766.
Protein-protein interaction databases
DIP DIP:6068N; -.
Protein family/group databases
MEROPS S01.001; -.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0007586; Biological process: digestion (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.
Pfam PF00089; Trypsin; 1.
Pfam graphical view of domain structure.
PRINTS PR00722; CHYMOTRYPSIN.
SMART SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.
PROSITE PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P00766.
ProtoNet P00766.
Other
SWISS-3DIMAGE P00766.
Genome annotation databases
Ensembl ENSBTAG00000011995; Bos taurus. [Contig view]
Phylogenomic databases
HOVERGEN P00766; -.
Other
LinkHub P00766; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Digestion; Direct protein sequencing; Hydrolase; Protease; Secreted; Serine protease; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1    13  13     Chymotrypsin A chain A. PRO_0000027624
PROPEP   14    15  2      PRO_0000027625
CHAIN   16   146  131     Chymotrypsin A chain B. PRO_0000027626
PROPEP   147   148  2      PRO_0000027627
CHAIN   149   245  97     Chymotrypsin A chain C. PRO_0000027628
DOMAIN   16   243  228     Peptidase S1. 
ACT_SITE   57    57        Charge relay system. 
ACT_SITE   102   102        Charge relay system. 
ACT_SITE   195   195        Charge relay system. 
DISULFID   1   122         
DISULFID   42    58         
DISULFID   136   201         
DISULFID   168   182         
DISULFID   191   220         
STRAND   30    34  5      
STRAND   40    54  15      
HELIX   56    58  3      
STRAND   64    69  6      
STRAND   81    90  10      
TURN   96    99  4      
STRAND   104   110  7      
STRAND   135   142  8      
STRAND   156   162  7      
HELIX   165   172  8      
HELIX   173   175  3      
STRAND   180   184  5      
STRAND   198   203  6      
STRAND   206   215  10      
STRAND   224   230  7      
HELIX   231   233  3      
HELIX   235   244  10      
Sequence information
Length: 245 AA [This is the length of the unprocessed precursor] Molecular weight: 25666 Da [This is the MW of the unprocessed precursor] CRC64: 91A9F28E2F3E3142 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
CGVPAIQPVL SGLSRIVNGE EAVPGSWPWQ VSLQDKTGFH FCGGSLINEN WVVTAAHCGV 

        70         80         90        100        110        120 
TTSDVVVAGE FDQGSSSEKI QKLKIAKVFK NSKYNSLTIN NDITLLKLST AASFSQTVSA 

       130        140        150        160        170        180 
VCLPSASDDF AAGTTCVTTG WGLTRYTNAN TPDRLQQASL PLLSNTNCKK YWGTKIKDAM 

       190        200        210        220        230        240 
ICAGASGVSS CMGDSGGPLV CKKNGAWTLV GIVSWGSSTC STSTPGVYAR VTALVNWVQQ 


TLAAN
P00766 in FASTA format

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