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Protein

Pancreatic secretory trypsin inhibitor

Gene

SPINK1

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

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

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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 ↔ 38PROSITE-ProRule annotation1 Publication
Disulfide bondi16 ↔ 35PROSITE-ProRule annotation1 Publication
Disulfide bondi24 ↔ 56PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

MINTiMINT-1505130.
STRINGi9823.ENSSSCP00000022179.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP00998.
OMAiCTKIYNP.
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

        10         20         30         40         50
TSPQREATCT SEVSGCPKIY NPVCGTDGIT YSNECVLCSE NKKRQTPVLI

QKSGPC
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

PIRiA91174. TIPG.

3D structure databases

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

Protein-protein interaction databases

MINTiMINT-1505130.
STRINGi9823.ENSSSCP00000022179.

Protein family/group databases

MEROPSiI01.011.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000026654; ENSSSCP00000022179; ENSSSCG00000027244.

Phylogenomic databases

GeneTreeiENSGT00530000064228.
HOVERGENiHBG006182.
InParanoidiP00998.
OMAiCTKIYNP.
OrthoDBiEOG7BW0M2.

Miscellaneous databases

EvolutionaryTraceiP00998.

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 98 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

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 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.