Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Chymotrypsinogen A

Gene
N/A
Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei57Charge relay system1
Active sitei102Charge relay system1
Active sitei195Charge relay system1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Digestion

Enzyme and pathway databases

BRENDAi3.4.21.1. 908.

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
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3314.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000276241 – 13Chymotrypsin A chain AAdd BLAST13
PropeptideiPRO_000002762514 – 152
ChainiPRO_000002762616 – 146Chymotrypsin A chain BAdd BLAST131
PropeptideiPRO_0000027627147 – 1482
ChainiPRO_0000027628149 – 245Chymotrypsin A chain CAdd BLAST97

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi1 ↔ 122
Disulfide bondi42 ↔ 58
Disulfide bondi136 ↔ 201
Disulfide bondi168 ↔ 182
Disulfide bondi191 ↔ 220

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiP00766.
PRIDEiP00766.

Miscellaneous databases

PMAP-CutDBP00766.

Expressioni

Gene expression databases

BgeeiENSBTAG00000011995.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP00766.

Structurei

Secondary structure

1245
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 15Combined sources4
Beta strandi16 – 18Combined sources3
Beta strandi26 – 28Combined sources3
Beta strandi30 – 34Combined sources5
Beta strandi36 – 38Combined sources3
Beta strandi40 – 48Combined sources9
Beta strandi51 – 54Combined sources4
Helixi56 – 58Combined sources3
Beta strandi64 – 69Combined sources6
Beta strandi71 – 74Combined sources4
Beta strandi76 – 78Combined sources3
Beta strandi81 – 90Combined sources10
Turni96 – 98Combined sources3
Beta strandi104 – 110Combined sources7
Beta strandi115 – 117Combined sources3
Beta strandi135 – 141Combined sources7
Helixi142 – 145Combined sources4
Turni147 – 149Combined sources3
Beta strandi156 – 162Combined sources7
Helixi165 – 172Combined sources8
Helixi173 – 175Combined sources3
Beta strandi180 – 184Combined sources5
Beta strandi186 – 188Combined sources3
Turni192 – 196Combined sources5
Beta strandi198 – 203Combined sources6
Beta strandi206 – 215Combined sources10
Beta strandi224 – 230Combined sources7
Helixi231 – 244Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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-ray2.30A1-13[»]
B16-146[»]
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[»]
4Q2KX-ray2.20A/B/C/D1-245[»]
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00766.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 243Peptidase S1PROSITE-ProRule annotationAdd BLAST228

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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

        10         20         30         40         50
CGVPAIQPVL SGLSRIVNGE EAVPGSWPWQ VSLQDKTGFH FCGGSLINEN
60 70 80 90 100
WVVTAAHCGV TTSDVVVAGE FDQGSSSEKI QKLKIAKVFK NSKYNSLTIN
110 120 130 140 150
NDITLLKLST AASFSQTVSA VCLPSASDDF AAGTTCVTTG WGLTRYTNAN
160 170 180 190 200
TPDRLQQASL PLLSNTNCKK YWGTKIKDAM ICAGASGVSS CMGDSGGPLV
210 220 230 240
CKKNGAWTLV GIVSWGSSTC STSTPGVYAR VTALVNWVQQ TLAAN
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

PIRiA90235. KYBOA.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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-ray2.30A1-13[»]
B16-146[»]
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[»]
4Q2KX-ray2.20A/B/C/D1-245[»]
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP00766.
ChEMBLiCHEMBL3314.

Protein family/group databases

MEROPSiS01.001.

Proteomic databases

PaxDbiP00766.
PRIDEiP00766.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.

Enzyme and pathway databases

BRENDAi3.4.21.1. 908.

Miscellaneous databases

EvolutionaryTraceiP00766.
PMAP-CutDBP00766.

Gene expression databases

BgeeiENSBTAG00000011995.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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]
ProtoNetiSearch...

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: November 2, 2016
This is version 156 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.