Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Disintegrin echistatin-alpha

Gene
N/A
Organism
Echis carinatus sochureki (Saw-scaled viper)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Potent inhibitor of ligand binding to the integrins alpha-V/beta-3 (ITGAV/ITGB3), alpha-5/beta-1 (ITGA5/ITGB1) and alpha-IIb/beta-3 (ITGA2B/ITGB3). Competition with fibrinogen for the RGD recognition sites on the alpha-IIb/beta-3 integrin (glyco-protein IIb/IIIa complex) results in the inhibition of platelet aggregation and other antithrombotic properties such as an ability to prevent coronary thrombosis in animal models. Is also a potent inhibitor of bone resorption. This results from the blocking of the interaction of alpha-V/beta-3 integrin on the surface of osteoclasts with bone extracellular matrix. In addition, interaction with alpha-V/beta-3 also inhibits adhesion of human umbilical vein endothelial cells (HUVEC) to immobilized vitronectin and fibronectin.3 Publications

Miscellaneous

This peptide has served as a model to produce tirofiban (Aggrastat), a nonpeptide drug available in the market as antiplatelet agent.1 Publication
The disintegrin belongs to the short disintegrin subfamily.Curated

Keywordsi

Molecular functionCell adhesion impairing toxin, Hemostasis impairing toxin, Platelet aggregation inhibiting toxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Disintegrin echistatin-alpha
Alternative name(s):
Carinatin
Platelet aggregation activation inhibitor
Cleaved into the following 2 chains:
Disintegrin echistatin-alpha-11 Publication
Disintegrin echistatin-alpha-21 Publication
OrganismiEchis carinatus sochureki (Saw-scaled viper)
Taxonomic identifieri124223 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeEchis

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi24R → A: Does not act on alpha-IIb/beta-3 and alpha-V/beta-3. 1 Publication1
Mutagenesisi27D → W: Increase in binding to alpha-IIb/beta-3 and decrease in binding to alpha-V/beta-3. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000072421 – 49Disintegrin echistatin-alpha-12 PublicationsAdd BLAST49
ChainiPRO_00000072431 – 47Disintegrin echistatin-alpha-21 PublicationAdd BLAST47

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1Pyrrolidone carboxylic acid; in form alpha-21 Publication1
Disulfide bondi2 ↔ 114 Publications
Disulfide bondi7 ↔ 323 Publications
Disulfide bondi8 ↔ 373 Publications
Disulfide bondi20 ↔ 394 Publications

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Expressioni

Tissue specificityi

Expressed by the venom gland.2 Publications

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

149
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 13Combined sources6
Beta strandi15 – 21Combined sources7
Turni23 – 25Combined sources3
Beta strandi37 – 39Combined sources3
Beta strandi44 – 46Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RO3NMR-A1-49[»]
2ECHNMR-A2-49[»]
ProteinModelPortaliP17347.
SMRiP17347.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17347.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 47DisintegrinPROSITE-ProRule annotationAdd BLAST47

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi24 – 26Cell attachment site3

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG005487.

Family and domain databases

Gene3Di4.10.70.10. 1 hit.
InterProiView protein in InterPro
IPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
PRINTSiPR00289. DISINTEGRIN.
SMARTiView protein in SMART
SM00050. DISIN. 1 hit.
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiView protein in PROSITE
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17347-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
QCESGPCCRN CKFLKEGTIC KRARGDDMDD YCNGKTCDCP RNPHKGPAT
Length:49
Mass (Da):5,424
Last modified:February 1, 1994 - v2
Checksum:i04CC79B297A4F99F
GO

Sequence databases

PIRiA32029.
A35982.

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.

Entry informationi

Entry nameiVM2EA_ECHCS
AccessioniPrimary (citable) accession number: P17347
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 1994
Last modified: July 5, 2017
This is version 106 of the entry and version 2 of the sequence. See 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