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Reviewed, UniProtKB/Swiss-Prot P83658 (DISS_ECHCA)

Last modified November 24, 2009. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Disintegrin schistatin
OrganismEchis carinatus (Saw-scaled viper)
Taxonomic identifier40353 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaViperidaeViperinaeEchis

Protein attributes

Sequence length64 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May bind with both glycoprotein IIb-IIIa (ITGA2B/ITGB3) and alphavbeta3 (ITGAV/ITGB3) integrins, and may inhibit platelet aggregation.

Subunit structure

Homodimer; disulfide-linked. Ref.1 Ref.3

Subcellular location

Secreted Ref.1.

Tissue specificity

Expressed by the venom gland. Ref.1

Sequence similarities

Belongs to the disintegrin family.

Contains 1 disintegrin domain.

Ontologies

Keywords
   Biological processBlood coagulation
Cell adhesion
   Cellular componentSecreted
   Molecular functionToxin
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processblood coagulation

Inferred from electronic annotation. Source: UniProtKB-KW

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

pathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6464Disintegrin schistatin
PRO_0000101800

Regions

Domain1 – 6464Disintegrin
Motif42 – 443Cell attachment site By similarity UniProtKB P81631

Amino acid modifications

Disulfide bond6 ↔ 29 Ref.1 Ref.3
Disulfide bond7Interchain (with C-12) Ref.1 Ref.3
Disulfide bond12Interchain (with C-7) Ref.1 Ref.3
Disulfide bond20 ↔ 26 Ref.1 Ref.3
Disulfide bond25 ↔ 50 Ref.1 Ref.3
Disulfide bond38 ↔ 57 Ref.1 Ref.3

Experimental info

Sequence conflict81D → P AA sequence Ref.2

Secondary structure

......... 64
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P83658-1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: FD0CA30A2048EE51

FASTA647,083
        10         20         30         40         50         60 
NSVHPCCDPV ICEPREGEHC ISGPCCENCY FLNSGTICKR ARGDGNQDYC TGITPDCPRN 


RYNV 

« Hide

References

[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: Venom.
[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: 11679739] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-19, X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Tissue: Venom.
[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: 15317139] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1RMRX-ray2.50A1-64[»]
1TEJX-ray1.90A/B1-64[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENP83658.

Family and domain databases

InterProIPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
[Graphical view]
Gene3DG3DSA:4.10.70.10. Blood-coag_inhib_Disintegrin. 1 hit.
PfamPF00200. Disintegrin. 1 hit.
[Graphical view]
PRINTSPR00289. DISINTEGRIN.
SMARTSM00050. DISIN. 1 hit.
[Graphical view]
PROSITEPS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDISS_ECHCA
AccessionPrimary (citable) accession number: P83658
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 1, 2003
Last modified: November 24, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectTox-Prot (Toxin Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents