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Protein

Disintegrin schistatin

Gene
N/A
Organism
Echis carinatus (Saw-scaled viper)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May bind to both alpha-IIb/beta-3 (ITGA2B/ITGB3) and alpha-V/beta-3 (ITGAV/ITGB3) integrins, and may inhibit platelet aggregation.

Keywords - Molecular functioni

Cell adhesion impairing toxin, Hemostasis impairing toxin, Platelet aggregation inhibiting toxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Disintegrin schistatin
OrganismiEchis carinatus (Saw-scaled viper)Curated
Taxonomic identifieri40353 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeEchis

Subcellular locationi

  • Secreted Curated1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6464Disintegrin schistatinPRO_0000101800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi6 ↔ 29Curated
Disulfide bondi7 – 7Interchain (with C-12)
Disulfide bondi12 – 12Interchain (with C-7)
Disulfide bondi20 ↔ 26Curated
Disulfide bondi25 ↔ 50Curated
Disulfide bondi38 ↔ 57Curated

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.Curated1 Publication

Interactioni

Subunit structurei

Homodimer; disulfide-linked.2 Publications

Structurei

Secondary structure

1
64
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni9 – 113Combined sources
Beta strandi12 – 143Combined sources
Beta strandi37 – 393Combined sources
Beta strandi42 – 454Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RMRX-ray2.50A1-64[»]
ProteinModelPortaliP83658.
SMRiP83658. Positions 1-64.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83658.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6464DisintegrinPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi42 – 443Cell attachment site

Sequence similaritiesi

Contains 1 disintegrin domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG005487.

Family and domain databases

Gene3Di4.10.70.10. 1 hit.
InterProiIPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
[Graphical view]
PfamiPF00200. Disintegrin. 1 hit.
[Graphical view]
PRINTSiPR00289. DISINTEGRIN.
SMARTiSM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P83658-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
NSVHPCCDPV ICEPREGEHC ISGPCCENCY FLNSGTICKR ARGDGNQDYC
60
TGITPDCPRN RYNV
Length:64
Mass (Da):7,083
Last modified:October 1, 2003 - v1
Checksum:iFD0CA30A2048EE51
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81D → P AA sequence (PubMed:11679739).Curated

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RMRX-ray2.50A1-64[»]
ProteinModelPortaliP83658.
SMRiP83658. Positions 1-64.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005487.

Miscellaneous databases

EvolutionaryTraceiP83658.

Family and domain databases

Gene3Di4.10.70.10. 1 hit.
InterProiIPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
[Graphical view]
PfamiPF00200. Disintegrin. 1 hit.
[Graphical view]
PRINTSiPR00289. DISINTEGRIN.
SMARTiSM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Bilgrami S., Jabeen T., Kumar J., Yadav S., Sharma S., Kaur P., Singh T.P.
    Submitted (SEP-2003) to UniProtKB
    Cited for: PROTEIN SEQUENCE, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISULFIDE BONDS.
    Tissue: VenomCurated.
  2. "Purification, crystallization and preliminary X-ray diffraction studies of disintegrin (schistatin) from saw-scaled viper (Echis carinatus)."
    Tomar S., Yadav S., Chandra V., Kumar P., Singh T.P.
    Acta Crystallogr. D 57:1669-1670(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-19, X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    Tissue: Venom1 Publication.
  3. "Crystal structure of schistatin, a disintegrin homodimer from saw-scaled viper (Echis carinatus) at 2.5 A resolution."
    Bilgrami S., Tomar S., Yadav S., Kaur P., Kumar J., Jabeen T., Sharma S., Singh T.P.
    J. Mol. Biol. 341:829-837(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), DISULFIDE BONDS.

Entry informationi

Entry nameiDIDS_ECHCA
AccessioniPrimary (citable) accession number: P83658
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 1, 2003
Last modified: January 7, 2015
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata 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

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.