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P00998

- ISK1_PIG

UniProt

P00998 - ISK1_PIG

Protein

Pancreatic secretory trypsin inhibitor

Gene

SPINK1

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    This is a trypsin inhibitor, its physiological function is to prevent the trypsin-catalyzed premature activation of zymogens within the pancreas.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei18 – 192Reactive bond

    GO - Molecular functioni

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

    GO - Biological processi

    1. negative regulation of calcium ion import Source: Ensembl
    2. negative regulation of nitric oxide mediated signal transduction Source: Ensembl
    3. negative regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
    4. negative regulation of serine-type endopeptidase activity Source: Ensembl
    5. regulation of acrosome reaction Source: Ensembl
    6. regulation of store-operated calcium entry Source: Ensembl

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Protein family/group databases

    MEROPSiI01.011.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pancreatic secretory trypsin inhibitor
    Alternative name(s):
    Serine protease inhibitor Kazal-type 1
    Gene namesi
    Name:SPINK1
    Synonyms:PSTI
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Chromosome 2

    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
    Chaini1 – 5656Pancreatic secretory trypsin inhibitorPRO_0000073027Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi9 ↔ 381 PublicationPROSITE-ProRule annotation
    Disulfide bondi16 ↔ 351 PublicationPROSITE-ProRule annotation
    Disulfide bondi24 ↔ 561 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-1505130.

    Structurei

    Secondary structure

    1
    56
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 176
    Beta strandi23 – 253
    Beta strandi30 – 334
    Helixi34 – 429
    Beta strandi50 – 545

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TGSX-ray1.80I1-56[»]
    ProteinModelPortaliP00998.
    SMRiP00998. Positions 1-56.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00998.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 5654Kazal-likePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 Kazal-like domain.PROSITE-ProRule annotation

    Phylogenomic databases

    GeneTreeiENSGT00530000064228.
    HOVERGENiHBG006182.
    OMAiNKEREVP.
    OrthoDBiEOG7BW0M2.

    Family and domain databases

    InterProiIPR002350. Kazal_dom.
    IPR001239. Prot_inh_Kazal-m.
    [Graphical view]
    PfamiPF00050. Kazal_1. 1 hit.
    [Graphical view]
    PRINTSiPR00290. KAZALINHBTR.
    SMARTiSM00280. KAZAL. 1 hit.
    [Graphical view]
    PROSITEiPS00282. KAZAL_1. 1 hit.
    PS51465. KAZAL_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P00998-1 [UniParc]FASTAAdd to Basket

    « Hide

    TSPQREATCT SEVSGCPKIY NPVCGTDGIT YSNECVLCSE NKKRQTPVLI   50
    QKSGPC 56
    Length:56
    Mass (Da):6,023
    Last modified:July 21, 1986 - v1
    Checksum:i39A3649DADF16D25
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1 – 44Missing in a second inhibitor.

    Sequence databases

    PIRiA91174. TIPG.

    Genome annotation databases

    EnsembliENSSSCT00000026654; ENSSSCP00000022179; ENSSSCG00000027244.

    Cross-referencesi

    Sequence databases

    PIRi A91174. TIPG.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TGS X-ray 1.80 I 1-56 [» ]
    ProteinModelPortali P00998.
    SMRi P00998. Positions 1-56.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1505130.

    Protein family/group databases

    MEROPSi I01.011.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSSSCT00000026654 ; ENSSSCP00000022179 ; ENSSSCG00000027244 .

    Phylogenomic databases

    GeneTreei ENSGT00530000064228.
    HOVERGENi HBG006182.
    OMAi NKEREVP.
    OrthoDBi EOG7BW0M2.

    Miscellaneous databases

    EvolutionaryTracei P00998.

    Family and domain databases

    InterProi IPR002350. Kazal_dom.
    IPR001239. Prot_inh_Kazal-m.
    [Graphical view ]
    Pfami PF00050. Kazal_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00290. KAZALINHBTR.
    SMARTi SM00280. KAZAL. 1 hit.
    [Graphical view ]
    PROSITEi PS00282. KAZAL_1. 1 hit.
    PS51465. KAZAL_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The structure of the porcine pancreatic secretory trypsin inhibitor. I. A sequence determination by Edman degradation and mass spectral identification of the p-bromophenyl-thiohydantoins."
      Tschesche H., Wachter E.
      Eur. J. Biochem. 16:187-198(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    2. "The primary structure of the porcine pancreatic secretory trypsin inhibitor. I. Amino acid sequence of the reduced S-aminoethylated protein."
      Bartelt D.C., Greene L.J.
      J. Biol. Chem. 246:2218-2229(1971) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    3. "Disulfide bridges of the secretory trypsin inhibitor from procine pancreas and the degradation of covalent structure during the temporary inhibition."
      Tschesche H., Schneider M., Reidel G., Klein H.
      Hoppe-Seyler's Z. Physiol. Chem. 353:763-764(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    4. "Trypsin inhibitors. VII. Primary structure of the specific trypsin inhibitor II (Kazal-type) from porcine pancreas. Sequence analysis with mass spectrometry identification of the p-bromophenylthio-hydantoins from the Edman degradation."
      Tschesche H., Wachter E.
      Hoppe-Seyler's Z. Physiol. Chem. 351:1449-1459(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF A SECOND INHIBITOR.
    5. "Three-dimensional structure of the complex between pancreatic secretory trypsin inhibitor (Kazal type) and trypsinogen at 1.8-A resolution. Structure solution, crystallographic refinement and preliminary structural interpretation."
      Bolognesi M., Gatti G., Menegatti E., Guarneri M., Marquart M., Papamokos E., Huber R.
      J. Mol. Biol. 162:839-868(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

    Entry informationi

    Entry nameiISK1_PIG
    AccessioniPrimary (citable) accession number: P00998
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 92 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3