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P00766 (CTRA_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chymotrypsinogen A

EC=3.4.21.1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.

Subcellular location

Secretedextracellular space.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processDigestion
   Cellular componentSecreted
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdigestion

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

OIHP101842EBI-6664027,EBI-6663991From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1313Chymotrypsin A chain A
PRO_0000027624
Propeptide14 – 152
PRO_0000027625
Chain16 – 146131Chymotrypsin A chain B
PRO_0000027626
Propeptide147 – 1482
PRO_0000027627
Chain149 – 24597Chymotrypsin A chain C
PRO_0000027628

Regions

Domain16 – 243228Peptidase S1

Sites

Active site571Charge relay system Ref.1 Ref.5
Active site1021Charge relay system Ref.1 Ref.5
Active site1951Charge relay system Ref.1 Ref.5

Amino acid modifications

Disulfide bond1 ↔ 122 Ref.1 Ref.4
Disulfide bond42 ↔ 58 Ref.1 Ref.4
Disulfide bond136 ↔ 201 Ref.1 Ref.4
Disulfide bond168 ↔ 182 Ref.1 Ref.4
Disulfide bond191 ↔ 220 Ref.1 Ref.4

Secondary structure

..................................................... 245
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00766 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 91A9F28E2F3E3142

FASTA24525,666
        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 

« Hide

References

[1]"Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A."
Brown J.R., Hartley B.S.
Biochem. J. 101:214-228(1966) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, DISULFIDE BONDS, ACTIVE SITE.
[2]"Role of a buried acid group in the mechanism of action of chymotrypsin."
Blow D.M., Birktoft J.J., Hartley B.S.
Nature 221:337-340(1969) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 102.
[3]"Amino-acid sequence of bovine chymotrypsinogen-A."
Hartley B.S.
Nature 201:1284-1287(1964) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE.
[4]"Covalent structure of bovine chymotrypsinogen A."
Meloun B., Kluh I., Kostka V., Moravek L., Prusik Z., Vanacek J., Keil B., Sorm F.
Biochim. Biophys. Acta 130:543-546(1966) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, DISULFIDE BONDS.
[5]"Histidine sequences in the active centres of some 'serine' proteinases."
Smillie L.B., Hartley B.S.
Biochem. J. 101:232-241(1966) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE.
[6]"I. Serine proteinases. The structure of alpha-chymotrypsin."
Birktoft J.J., Blow D.M., Henderson R., Steitz T.A.
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 257:67-76(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[7]"Chymotrypsinogen: 2.5-A crystal structure, comparison with alpha-chymotrypsin, and implications for zymogen activation."
Freer S.T., Kraut J., Robertus J.D., Wright H.T., Xuong N.H.
Biochemistry 9:1997-2009(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF CHYMOTRYPSINOGEN.
[8]"Refined crystal structure of gamma-chymotrypsin at 1.9-A resolution. Comparison with other pancreatic serine proteases."
Cohen G.H., Silverton E.W., Davies D.R.
J. Mol. Biol. 148:449-479(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF GAMMA-CHYMOTRYPSIN.
[9]"Structure of alpha-chymotrypsin refined at 1.68-A resolution."
Tsukada H., Blow D.M.
J. Mol. Biol. 184:703-711(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF ALPHA-CHYMOTRYPSIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRKYBOA. A90235.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AB9X-ray1.60A1-13[»]
B16-146[»]
C149-245[»]
1ACBX-ray2.00E1-245[»]
1AFQX-ray1.80A1-13[»]
B16-146[»]
C150-245[»]
1CA0X-ray2.10A/F1-13[»]
B/G16-146[»]
C/H149-245[»]
1CBWX-ray2.60B/G16-146[»]
C/H149-245[»]
1CGIX-ray2.30E1-245[»]
1CGJX-ray2.30E1-245[»]
1CHGX-ray2.50A1-245[»]
1CHOX-ray1.80E1-13[»]
F16-146[»]
G149-245[»]
1DLKX-ray2.14A/C1-13[»]
B/D16-245[»]
1EX3X-ray3.00A1-245[»]
1GCDX-ray1.90A1-245[»]
1GCTX-ray1.60A1-13[»]
B16-146[»]
C149-245[»]
1GG6X-ray1.40A1-10[»]
B16-146[»]
C149-245[»]
1GGDX-ray1.50A1-10[»]
B16-146[»]
C149-245[»]
1GHAX-ray2.20E1-13[»]
F16-146[»]
G149-245[»]
1GHBX-ray2.00E1-13[»]
F16-146[»]
G149-245[»]
1GL0X-ray3.00E1-245[»]
1GL1X-ray2.10A/B/C1-245[»]
1GMCX-ray2.20E1-13[»]
F16-146[»]
G149-245[»]
1GMDX-ray2.20E1-13[»]
F16-146[»]
G149-245[»]
1GMHX-ray2.10E1-13[»]
F16-146[»]
G149-245[»]
1HJAX-ray2.30B16-146[»]
C149-245[»]
1K2IX-ray1.8011-245[»]
1MTNX-ray2.80A/E1-13[»]
B/F16-146[»]
C/G149-245[»]
1N8OX-ray2.00A1-13[»]
B16-146[»]
C149-245[»]
1OXGX-ray2.20A1-245[»]
B16-29[»]
1P2MX-ray1.75A/C1-245[»]
1P2NX-ray1.80A/C1-245[»]
1P2OX-ray2.00A/C1-245[»]
1P2QX-ray1.80A/C1-245[»]
1T7CX-ray1.85A/C1-245[»]
1T8LX-ray1.75A/C1-245[»]
1T8MX-ray1.80A/C1-245[»]
1T8NX-ray1.75A/C1-245[»]
1T8OX-ray1.70A/C1-245[»]
1VGCX-ray1.90A1-13[»]
B16-146[»]
C149-245[»]
1YPHX-ray1.34A/B1-13[»]
C/D16-146[»]
E/F149-245[»]
2CGAX-ray1.80A/B1-245[»]
2CHAX-ray2.00A/E1-13[»]
B/F16-146[»]
C/G149-245[»]
2GCHX-ray1.90E1-13[»]
F16-146[»]
G149-245[»]
2GCTX-ray1.80A1-13[»]
B16-146[»]
C149-245[»]
2GMTX-ray1.80A1-13[»]
B16-146[»]
C149-245[»]
2P8OX-ray1.50A1-13[»]
B16-146[»]
C149-245[»]
2VGCX-ray1.80A1-13[»]
B16-146[»]
C149-245[»]
2Y6TX-ray2.74A/B/C/D1-245[»]
3BG4X-ray2.50B16-146[»]
C149-245[»]
3GCHX-ray1.90A1-13[»]
B16-146[»]
C149-245[»]
3GCTX-ray1.60E1-13[»]
F16-146[»]
G149-245[»]
3RU4X-ray1.68C1-11[»]
D16-146[»]
E150-245[»]
3T62X-ray2.00A/B/C1-245[»]
3VGCX-ray1.67A1-13[»]
B16-146[»]
C149-245[»]
4CHAX-ray1.68A/E1-13[»]
B/F16-146[»]
C/G149-245[»]
4GCHX-ray1.90E1-13[»]
F16-146[»]
G149-245[»]
4VGCX-ray2.10A1-13[»]
B16-146[»]
C149-245[»]
5CHAX-ray1.67A/E1-13[»]
B/F16-146[»]
C/G149-245[»]
5GCHX-ray2.70E1-13[»]
F16-146[»]
G149-245[»]
6CHAX-ray1.80A/E1-13[»]
B/F16-146[»]
C/G149-245[»]
6GCHX-ray2.10E1-13[»]
F16-146[»]
G149-245[»]
7GCHX-ray1.80E1-13[»]
F16-146[»]
G149-245[»]
8GCHX-ray1.60E1-13[»]
F16-146[»]
G149-245[»]
ProteinModelPortalP00766.
SMRP00766. Positions 1-245.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6068N.
IntActP00766. 1 interaction.
MINTMINT-206889.
STRING9913.ENSBTAP00000015915.

Chemistry

BindingDBP00766.
ChEMBLCHEMBL3314.

Protein family/group databases

MEROPSS01.001.

Proteomic databases

PRIDEP00766.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
HOVERGENHBG013304.
InParanoidP00766.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00766.
PMAP-CutDBP00766.

Entry information

Entry nameCTRA_BOVIN
AccessionPrimary (citable) accession number: P00766
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references