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P00766

- CTRA_BOVIN

UniProt

P00766 - CTRA_BOVIN

Protein

Chymotrypsinogen A

Gene
N/A
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Sites

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. digestion Source: UniProtKB-KW

    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

    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 ↔ 122
    Disulfide bondi42 ↔ 58
    Disulfide bondi136 ↔ 201
    Disulfide bondi168 ↔ 182
    Disulfide bondi191 ↔ 220

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00766.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 243228Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    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: October 1, 2014
    This is version 141 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