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P00766 (CTRA_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 118. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·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

Cleaved into the following 3 chains:

  1. Chymotrypsin A chain A
  2. Chymotrypsin A chain B
  3. Chymotrypsin A chain C
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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

Secreted › extracellular 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...

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

1 ................................. 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: 5971783] [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: 5764436] [Abstract]
Cited for: SEQUENCE REVISION TO 102.
[3]"Amino-acid sequence of bovine chymotrypsinogen-A."
Hartley B.S.
Nature 201:1284-1287(1964) [PubMed: 14151403] [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: 5972866] [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: 5971785] [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: 4399050] [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: 5442169] [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: 6914398] [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: 4046030] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF ALPHA-CHYMOTRYPSIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

IPIIPI00690731.
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[»]
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...

Protein-protein interaction databases

DIPDIP-6068N.
MINTMINT-206889.

Protein family/group databases

MEROPSS01.001.

Proteomic databases

PRIDEP00766.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGmaNOG10829.
GeneTreeENSGT00550000074117.
HOVERGENHBG013304.
InParanoidP00766.
OrthoDBEOG4VMFG1.
PhylomeDBP00766.

Family and domain databases

InterProIPR009003. Pept_cys/ser_Trypsin-like.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

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: November 16, 2011
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents