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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)DescriptionActionsGraphical viewLength
Sitei13 – 14Reactive bond for trypsin2

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001554191 – 55PI-stichotoxin-She2a1 PublicationAdd BLAST55

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi3 ↔ 533 Publications
Disulfide bondi12 ↔ 363 Publications
Disulfide bondi28 ↔ 493 Publications

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

155
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 4Combined sources4
Beta strandi16 – 22Combined sources7
Turni23 – 26Combined sources4
Beta strandi27 – 33Combined sources7
Beta strandi35 – 37Combined sources3
Beta strandi43 – 45Combined sources3
Helixi46 – 52Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31713.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 53BPTI/Kunitz inhibitorPROSITE-ProRule annotationAdd BLAST51

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
PDB 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.
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...

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: November 2, 2016
This is version 100 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.