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Protein

PI-stichotoxin-She2a

Gene
N/A
Organism
Stichodactyla helianthus (Sun anemone) (Stoichactis helianthus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Active against serine, cysteine, and aspartic proteinases. Can bind vertebrate trypsin and chymotrypsin.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei13 – 142Reactive bond for trypsin

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aspartic protease inhibitor, Protease inhibitor, Serine protease inhibitor

Names & Taxonomyi

Protein namesi
Recommended name:
PI-stichotoxin-She2a1 Publication
Short name:
PI-SHTX-She2a1 Publication
Alternative name(s):
Kunitz-type serine protease inhibitor ShPI-I1 Publication
OrganismiStichodactyla helianthus (Sun anemone) (Stoichactis helianthus)
Taxonomic identifieri6123 [NCBI]
Taxonomic lineageiEukaryotaMetazoaCnidariaAnthozoaHexacoralliaActiniariaStichodactylidaeStichodactyla

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nematocyst, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5555PI-stichotoxin-She2a1 PublicationPRO_0000155419Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi3 ↔ 533 Publications
Disulfide bondi12 ↔ 363 Publications
Disulfide bondi28 ↔ 493 Publications

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

55
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 44Combined sources
Beta strandi16 – 227Combined sources
Turni23 – 264Combined sources
Beta strandi27 – 337Combined sources
Beta strandi35 – 373Combined sources
Beta strandi43 – 453Combined sources
Helixi46 – 527Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SHPNMR-A1-55[»]
3M7QX-ray1.70B1-55[»]
3OFWX-ray2.50A1-54[»]
3T62X-ray2.00D/E/F1-54[»]
3UOUX-ray2.00B1-55[»]
ProteinModelPortaliP31713.
SMRiP31713. Positions 1-55.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31713.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 5351BPTI/Kunitz inhibitorPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 BPTI/Kunitz inhibitor domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di4.10.410.10. 1 hit.
InterProiIPR002223. Kunitz_BPTI.
IPR020901. Prtase_inh_Kunz-CS.
[Graphical view]
PfamiPF00014. Kunitz_BPTI. 1 hit.
[Graphical view]
PRINTSiPR00759. BASICPTASE.
SMARTiSM00131. KU. 1 hit.
[Graphical view]
SUPFAMiSSF57362. SSF57362. 1 hit.
PROSITEiPS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P31713-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SICSEPKKVG RCKGYFPRFY FDSETGKCTP FIYGGCGGNG NNFETLHQCR

AICRA
Length:55
Mass (Da):6,116
Last modified:July 1, 1993 - v1
Checksum:i532B96E3127000D4
GO

Mass spectrometryi

Molecular mass is 6110.60 Da from positions 1 - 55. Determined by FAB. 1 Publication

Sequence databases

PIRiS30332.

Cross-referencesi

Sequence databases

PIRiS30332.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SHPNMR-A1-55[»]
3M7QX-ray1.70B1-55[»]
3OFWX-ray2.50A1-54[»]
3T62X-ray2.00D/E/F1-54[»]
3UOUX-ray2.00B1-55[»]
ProteinModelPortaliP31713.
SMRiP31713. Positions 1-55.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP31713.

Family and domain databases

Gene3Di4.10.410.10. 1 hit.
InterProiIPR002223. Kunitz_BPTI.
IPR020901. Prtase_inh_Kunz-CS.
[Graphical view]
PfamiPF00014. Kunitz_BPTI. 1 hit.
[Graphical view]
PRINTSiPR00759. BASICPTASE.
SMARTiSM00131. KU. 1 hit.
[Graphical view]
SUPFAMiSSF57362. SSF57362. 1 hit.
PROSITEiPS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Purification, characterization and immobilization of proteinase inhibitors from Stichodactyla helianthus."
    Delfin J., Martinez I., Antuch W., Morera V., Gonzalez Y., Rodriguez R., Marquez M., Saroyan A., Larionova N., Diaz J., Padron G., Chavez M.
    Toxicon 34:1367-1376(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY.
  2. "Development of a rational nomenclature for naming peptide and protein toxins from sea anemones."
    Oliveira J.S., Fuentes-Silva D., King G.F.
    Toxicon 60:539-550(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE.
  3. "The NMR solution structure of a Kunitz-type proteinase inhibitor from the sea anemone Stichodactyla helianthus."
    Antuch W., Berndt K.D., Chavez M.A., Delfin J., Wuethrich K.
    Eur. J. Biochem. 212:675-684(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.
  4. "Structure of the recombinant BPTI/Kunitz-type inhibitor rShPI-1A from the marine invertebrate Stichodactyla helianthus."
    Garcia-Fernandez R., Pons T., Meyer A., Perbandt M., Gonzalez-Gonzalez Y., Gil D., de Los Angeles Chavez M., Betzel C., Redecke L.
    Acta Crystallogr. F 68:1289-1293(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), DISULFIDE BOND.
  5. "Structural insights into serine protease inhibition by a marine invertebrate BPTI Kunitz-type inhibitor."
    Garcia-Fernandez R., Pons T., Perbandt M., Valiente P.A., Talavera A., Gonzalez-Gonzalez Y., Rehders D., Chavez M.A., Betzel C., Redecke L.
    J. Struct. Biol. 180:271-279(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH TRYPSIN, FUNCTION, REACTIVE BOND, DISULFIDE BONDS.

Entry informationi

Entry nameiVKT1_STIHL
AccessioniPrimary (citable) accession number: P31713
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: December 9, 2015
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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

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.