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Protein

Disintegrin schistatin-like subunit A

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.By similarity

Keywords - Molecular functioni

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

Names & Taxonomyi

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

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6262Disintegrin schistatin-like subunit APRO_0000319469Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi5 ↔ 28PROSITE-ProRule annotation1 Publication
Disulfide bondi6 – 6Interchain (with C-12 in subunit B)PROSITE-ProRule annotation1 Publication
Disulfide bondi11 – 11Interchain (with C-7 in subunit B)PROSITE-ProRule annotation1 Publication
Disulfide bondi19 ↔ 25PROSITE-ProRule annotation1 Publication
Disulfide bondi24 ↔ 49PROSITE-ProRule annotation1 Publication
Disulfide bondi37 ↔ 56PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterodimer with subunit B; disulfide-linked.1 Publication

Structurei

Secondary structure

1
62
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni8 – 114Combined sources
Beta strandi20 – 223Combined sources
Beta strandi36 – 383Combined sources
Beta strandi41 – 444Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TEJX-ray1.90A1-62[»]
ProteinModelPortaliP0C6B4.
SMRiP0C6B4. Positions 1-62.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C6B4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6262DisintegrinPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi41 – 433Cell attachment site

Sequence similaritiesi

Contains 1 disintegrin domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG005487.

Family and domain databases

Gene3Di4.10.70.10. 1 hit.
InterProiIPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
[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.

P0C6B4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SVNPCCDPVI CKPRDGEHCI SGPCCNNCKF LNSGTICQRA RGDGNHDYCT
60
GITTDCPRNR YN
Length:62
Mass (Da):6,795
Last modified:February 26, 2008 - v1
Checksum:i56078548214143F1
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TEJX-ray1.90A1-62[»]
ProteinModelPortaliP0C6B4.
SMRiP0C6B4. Positions 1-62.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005487.

Miscellaneous databases

EvolutionaryTraceiP0C6B4.

Family and domain databases

Gene3Di4.10.70.10. 1 hit.
InterProiIPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
[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. "Crystal structure of the disintegrin heterodimer from saw-scaled viper (Echis carinatus) at 1.9 A resolution."
    Bilgrami S., Yadav S., Kaur P., Sharma S., Perbandt M., Betzel C., Singh T.P.
    Biochemistry 44:11058-11066(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, SUBUNIT, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), DISULFIDE BONDS.
    Tissue: Venom.

Entry informationi

Entry nameiDIDLA_ECHCA
AccessioniPrimary (citable) accession number: P0C6B4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: December 9, 2015
This is version 38 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

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.