Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P01074

- ITR1_CUCMA

UniProt

P01074 - ITR1_CUCMA

Protein

Trypsin inhibitor 1

Gene
N/A
Organism
Cucurbita maxima (Pumpkin) (Winter squash)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Inhibits trypsin.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei5 – 62Reactive bond

    GO - Molecular functioni

    1. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Protein family/group databases

    MEROPSiI07.005.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trypsin inhibitor 1
    Alternative name(s):
    CMTI-I
    ITD-I
    Trypsin inhibitor I
    OrganismiCucurbita maxima (Pumpkin) (Winter squash)
    Taxonomic identifieri3661 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeCucurbiteaeCucurbita

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Peptidei1 – 2929Trypsin inhibitor 1PRO_0000044376Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi3 ↔ 201 Publication
    Disulfide bondi10 ↔ 221 Publication
    Disulfide bondi16 ↔ 281 Publication

    Keywords - PTMi

    Disulfide bond

    Miscellaneous databases

    PMAP-CutDBP01074.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-365052.

    Structurei

    Secondary structure

    1
    29
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 153
    Beta strandi21 – 233
    Beta strandi26 – 283

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CTINMR-A1-29[»]
    1LU0X-ray1.03A/B1-29[»]
    1PPEX-ray2.00I1-29[»]
    2CTINMR-A1-29[»]
    2STAX-ray1.80I1-29[»]
    2V1VNMR-A1-29[»]
    3CTINMR-A1-29[»]
    ProteinModelPortaliP01074.
    SMRiP01074. Positions 2-29.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01074.

    Family & Domainsi

    Domaini

    The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.

    Sequence similaritiesi

    Keywords - Domaini

    Knottin

    Family and domain databases

    InterProiIPR000737. Prot_inh_squash.
    IPR011052. Proteinase_amylase_inhib_dom.
    [Graphical view]
    PfamiPF00299. Squash. 1 hit.
    [Graphical view]
    PRINTSiPR00293. SQUASHINHBTR.
    SUPFAMiSSF57027. SSF57027. 1 hit.
    PROSITEiPS00286. SQUASH_INHIBITOR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P01074-1 [UniParc]FASTAAdd to Basket

    « Hide

    RVCPRILMEC KKDSDCLAEC VCLEHGYCG                          29
    Length:29
    Mass (Da):3,275
    Last modified:July 21, 1986 - v1
    Checksum:iCD509120BA52C01F
    GO

    Sequence databases

    PIRiA01313. TIPU.

    Cross-referencesi

    Sequence databases

    PIRi A01313. TIPU.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CTI NMR - A 1-29 [» ]
    1LU0 X-ray 1.03 A/B 1-29 [» ]
    1PPE X-ray 2.00 I 1-29 [» ]
    2CTI NMR - A 1-29 [» ]
    2STA X-ray 1.80 I 1-29 [» ]
    2V1V NMR - A 1-29 [» ]
    3CTI NMR - A 1-29 [» ]
    ProteinModelPortali P01074.
    SMRi P01074. Positions 2-29.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-365052.

    Protein family/group databases

    MEROPSi I07.005.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P01074.
    PMAP-CutDB P01074.

    Family and domain databases

    InterProi IPR000737. Prot_inh_squash.
    IPR011052. Proteinase_amylase_inhib_dom.
    [Graphical view ]
    Pfami PF00299. Squash. 1 hit.
    [Graphical view ]
    PRINTSi PR00293. SQUASHINHBTR.
    SUPFAMi SSF57027. SSF57027. 1 hit.
    PROSITEi PS00286. SQUASH_INHIBITOR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Amino-acid sequence of two trypsin isoinhibitors, ITD I and ITD III from squash seeds (Cucurbita maxima)."
      Wilusz T., Wieczorek M., Polanowski A., Denton A., Cook J., Laskowski M. Jr.
      Hoppe-Seyler's Z. Physiol. Chem. 364:93-95(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Tissue: Seed.
    2. "The refined 2.0 A X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes."
      Bode W., Greyling H.J., Huber R., Otlewski J., Wilusz T.
      FEBS Lett. 242:285-292(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    3. "Determination of the complete three-dimensional structure of the trypsin inhibitor from squash seeds in aqueous solution by nuclear magnetic resonance and a combination of distance geometry and dynamical simulated annealing."
      Holak T.A., Gondol D., Otlewski J., Wilusz T.
      J. Mol. Biol. 210:635-648(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    4. "Conservative mutation Met8 --> Leu affects the folding process and structural stability of squash trypsin inhibitor CMTI-I."
      Zhukov I., Jaroszewski L., Bierzynski A.
      Protein Sci. 9:273-279(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiITR1_CUCMA
    AccessioniPrimary (citable) accession number: P01074
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 86 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3