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P00766

- CTRA_BOVIN

UniProt

P00766 - CTRA_BOVIN

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Protein

Chymotrypsinogen A

Gene
N/A
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei57 – 571Charge relay system2 Publications
Active sitei102 – 1021Charge relay system2 Publications
Active sitei195 – 1951Charge relay system2 Publications

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. digestion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Digestion

Protein family/group databases

MEROPSiS01.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Chymotrypsinogen A (EC:3.4.21.1)
Cleaved into the following 3 chains:
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1313Chymotrypsin A chain APRO_0000027624Add
BLAST
Propeptidei14 – 152PRO_0000027625
Chaini16 – 146131Chymotrypsin A chain BPRO_0000027626Add
BLAST
Propeptidei147 – 1482PRO_0000027627
Chaini149 – 24597Chymotrypsin A chain CPRO_0000027628Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi1 ↔ 1222 Publications
Disulfide bondi42 ↔ 582 Publications
Disulfide bondi136 ↔ 2012 Publications
Disulfide bondi168 ↔ 1822 Publications
Disulfide bondi191 ↔ 2202 Publications

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PRIDEiP00766.

Miscellaneous databases

PMAP-CutDBP00766.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
OIHP101842EBI-6664027,EBI-6663991From a different organism.

Protein-protein interaction databases

DIPiDIP-6068N.
IntActiP00766. 1 interaction.
MINTiMINT-206889.
STRINGi9913.ENSBTAP00000015915.

Structurei

Secondary structure

1
245
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 154
Beta strandi16 – 183
Beta strandi26 – 283
Beta strandi30 – 345
Beta strandi36 – 383
Beta strandi40 – 489
Beta strandi51 – 544
Helixi56 – 583
Beta strandi64 – 696
Beta strandi71 – 744
Beta strandi76 – 783
Beta strandi81 – 9010
Turni96 – 983
Beta strandi104 – 1107
Beta strandi115 – 1173
Beta strandi135 – 1417
Helixi142 – 1454
Turni147 – 1493
Beta strandi156 – 1627
Helixi165 – 1728
Helixi173 – 1753
Beta strandi180 – 1845
Beta strandi186 – 1883
Turni192 – 1965
Beta strandi198 – 2036
Beta strandi206 – 21510
Beta strandi224 – 2307
Helixi231 – 24414

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP00766.
SMRiP00766. Positions 1-245.

Miscellaneous databases

EvolutionaryTraceiP00766.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 243228Peptidase S1Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP00766.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00766-1 [UniParc]FASTAAdd to Basket

« Hide

CGVPAIQPVL SGLSRIVNGE EAVPGSWPWQ VSLQDKTGFH FCGGSLINEN    50
WVVTAAHCGV TTSDVVVAGE FDQGSSSEKI QKLKIAKVFK NSKYNSLTIN 100
NDITLLKLST AASFSQTVSA VCLPSASDDF AAGTTCVTTG WGLTRYTNAN 150
TPDRLQQASL PLLSNTNCKK YWGTKIKDAM ICAGASGVSS CMGDSGGPLV 200
CKKNGAWTLV GIVSWGSSTC STSTPGVYAR VTALVNWVQQ TLAAN 245
Length:245
Mass (Da):25,666
Last modified:July 21, 1986 - v1
Checksum:i91A9F28E2F3E3142
GO

Sequence databases

PIRiA90235. KYBOA.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

PIRi A90235. KYBOA.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AB9 X-ray 1.60 A 1-13 [» ]
B 16-146 [» ]
C 149-245 [» ]
1ACB X-ray 2.00 E 1-245 [» ]
1AFQ X-ray 1.80 A 1-13 [» ]
B 16-146 [» ]
C 150-245 [» ]
1CA0 X-ray 2.10 A/F 1-13 [» ]
B/G 16-146 [» ]
C/H 149-245 [» ]
1CBW X-ray 2.60 B/G 16-146 [» ]
C/H 149-245 [» ]
1CGI X-ray 2.30 E 1-245 [» ]
1CGJ X-ray 2.30 E 1-245 [» ]
1CHG X-ray 2.50 A 1-245 [» ]
1CHO X-ray 1.80 E 1-13 [» ]
F 16-146 [» ]
G 149-245 [» ]
1DLK X-ray 2.14 A/C 1-13 [» ]
B/D 16-245 [» ]
1EX3 X-ray 3.00 A 1-245 [» ]
1GCD X-ray 1.90 A 1-245 [» ]
1GCT X-ray 1.60 A 1-13 [» ]
B 16-146 [» ]
C 149-245 [» ]
1GG6 X-ray 1.40 A 1-10 [» ]
B 16-146 [» ]
C 149-245 [» ]
1GGD X-ray 1.50 A 1-10 [» ]
B 16-146 [» ]
C 149-245 [» ]
1GHA X-ray 2.20 E 1-13 [» ]
F 16-146 [» ]
G 149-245 [» ]
1GHB X-ray 2.00 E 1-13 [» ]
F 16-146 [» ]
G 149-245 [» ]
1GL0 X-ray 3.00 E 1-245 [» ]
1GL1 X-ray 2.10 A/B/C 1-245 [» ]
1GMC X-ray 2.20 E 1-13 [» ]
F 16-146 [» ]
G 149-245 [» ]
1GMD X-ray 2.20 E 1-13 [» ]
F 16-146 [» ]
G 149-245 [» ]
1GMH X-ray 2.10 E 1-13 [» ]
F 16-146 [» ]
G 149-245 [» ]
1HJA X-ray 2.30 B 16-146 [» ]
C 149-245 [» ]
1K2I X-ray 1.80 1 1-245 [» ]
1MTN X-ray 2.80 A/E 1-13 [» ]
B/F 16-146 [» ]
C/G 149-245 [» ]
1N8O X-ray 2.00 A 1-13 [» ]
B 16-146 [» ]
C 149-245 [» ]
1OXG X-ray 2.20 A 1-245 [» ]
B 16-29 [» ]
1P2M X-ray 1.75 A/C 1-245 [» ]
1P2N X-ray 1.80 A/C 1-245 [» ]
1P2O X-ray 2.00 A/C 1-245 [» ]
1P2Q X-ray 1.80 A/C 1-245 [» ]
1T7C X-ray 1.85 A/C 1-245 [» ]
1T8L X-ray 1.75 A/C 1-245 [» ]
1T8M X-ray 1.80 A/C 1-245 [» ]
1T8N X-ray 1.75 A/C 1-245 [» ]
1T8O X-ray 1.70 A/C 1-245 [» ]
1VGC X-ray 1.90 A 1-13 [» ]
B 16-146 [» ]
C 149-245 [» ]
1YPH X-ray 1.34 A/B 1-13 [» ]
C/D 16-146 [» ]
E/F 149-245 [» ]
2CGA X-ray 1.80 A/B 1-245 [» ]
2CHA X-ray 2.00 A/E 1-13 [» ]
B/F 16-146 [» ]
C/G 149-245 [» ]
2GCH X-ray 1.90 E 1-13 [» ]
F 16-146 [» ]
G 149-245 [» ]
2GCT X-ray 1.80 A 1-13 [» ]
B 16-146 [» ]
C 149-245 [» ]
2GMT X-ray 1.80 A 1-13 [» ]
B 16-146 [» ]
C 149-245 [» ]
2P8O X-ray 1.50 A 1-13 [» ]
B 16-146 [» ]
C 149-245 [» ]
2VGC X-ray 1.80 A 1-13 [» ]
B 16-146 [» ]
C 149-245 [» ]
2Y6T X-ray 2.74 A/B/C/D 1-245 [» ]
3BG4 X-ray 2.50 B 16-146 [» ]
C 149-245 [» ]
3GCH X-ray 1.90 A 1-13 [» ]
B 16-146 [» ]
C 149-245 [» ]
3GCT X-ray 1.60 E 1-13 [» ]
F 16-146 [» ]
G 149-245 [» ]
3RU4 X-ray 1.68 C 1-11 [» ]
D 16-146 [» ]
E 150-245 [» ]
3T62 X-ray 2.00 A/B/C 1-245 [» ]
3VGC X-ray 1.67 A 1-13 [» ]
B 16-146 [» ]
C 149-245 [» ]
4CHA X-ray 1.68 A/E 1-13 [» ]
B/F 16-146 [» ]
C/G 149-245 [» ]
4GCH X-ray 1.90 E 1-13 [» ]
F 16-146 [» ]
G 149-245 [» ]
4VGC X-ray 2.10 A 1-13 [» ]
B 16-146 [» ]
C 149-245 [» ]
5CHA X-ray 1.67 A/E 1-13 [» ]
B/F 16-146 [» ]
C/G 149-245 [» ]
5GCH X-ray 2.70 E 1-13 [» ]
F 16-146 [» ]
G 149-245 [» ]
6CHA X-ray 1.80 A/E 1-13 [» ]
B/F 16-146 [» ]
C/G 149-245 [» ]
6GCH X-ray 2.10 E 1-13 [» ]
F 16-146 [» ]
G 149-245 [» ]
7GCH X-ray 1.80 E 1-13 [» ]
F 16-146 [» ]
G 149-245 [» ]
8GCH X-ray 1.60 E 1-13 [» ]
F 16-146 [» ]
G 149-245 [» ]
ProteinModelPortali P00766.
SMRi P00766. Positions 1-245.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6068N.
IntActi P00766. 1 interaction.
MINTi MINT-206889.
STRINGi 9913.ENSBTAP00000015915.

Chemistry

BindingDBi P00766.
ChEMBLi CHEMBL3314.

Protein family/group databases

MEROPSi S01.001.

Proteomic databases

PRIDEi P00766.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG5640.
HOGENOMi HOG000251820.
HOVERGENi HBG013304.
InParanoidi P00766.

Miscellaneous databases

EvolutionaryTracei P00766.
PMAP-CutDB P00766.

Family and domain databases

InterProi IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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.

Entry informationi

Entry nameiCTRA_BOVIN
AccessioniPrimary (citable) accession number: P00766
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 3, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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