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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.

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:
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 react with alpha-IIb/beta-3 and alpha-V/beta-3. 1 Publication1
Mutagenesisi27D → W: Shows increased binding to alpha-IIb/beta-3 and decreased binding to alpha-V/beta-3. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000072421 – 49Disintegrin echistatin-alpha-1Add BLAST49
ChainiPRO_00000072431 – 47Disintegrin echistatin-alpha-2Add BLAST47

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1Pyrrolidone carboxylic acid; in form alpha-21
Disulfide bondi2 ↔ 11
Disulfide bondi7 ↔ 32
Disulfide bondi8 ↔ 37
Disulfide bondi20 ↔ 39

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Expressioni

Tissue specificityi

Expressed by the venom gland.

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.

Cross-referencesi

Sequence databases

PIRiA32029.
A35982.

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...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005487.

Miscellaneous databases

EvolutionaryTraceiP17347.

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.
ProtoNetiSearch...

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: February 15, 2017
This is version 105 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

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.