Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P00766 (CTRA_BOVIN)

Last modified June 16, 2009. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Chymotrypsinogen A
    EC=3.4.21.1
Cleaved into the following 3 chains:
    1- Recommended name:
            Chymotrypsin A chain A
    2- Recommended name:
            Chymotrypsin A chain B
    3- Recommended name:
            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

Hide | Top

Protein attributes

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

Hide | Top

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.

Hide | Top

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis involved in cellular protein catabolic process

Inferred from direct assay. Source: MGI

   Cellular componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding

Inferred from direct assay. Source: MGI

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Hide | Top

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...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P00766-1 [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

Hide | Top

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.

Hide | Top

Cross-references

Sequence databases

IPIIPI00690731.
PIRKYBOA. A90235.
UniGeneBt.62239

3D structure databases

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[»]
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[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:6068N.

Protein family/group databases

MEROPSS01.001.

Genome annotation databases

EnsemblENSBTAG00000011995. Bos taurus. [Contig view]

Phylogenomic databases

HOVERGENP00766.

Enzyme and pathway databases

BRENDA3.4.21.1. 251.

Family and domain databases

InterProIPR018114. 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]
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

PMAP-CutDBP00766.

Hide | Top

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: June 16, 2009
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents