Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q7T2Q1 (EM16A_ECHML)

Last modified November 24, 2009. Version 29. 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:
    EMS16 subunit A
      Short name=EMS16A
OrganismEchis multisquamatus (Central Asian sand viper)
Taxonomic identifier93050 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaViperidaeViperinaeEchis

Protein attributes

Sequence length157 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

EMS16 is a potent and selective inhibitor of alpha-2/beta-1 (ITGA2/ITGB1) integrin. Binds specifically to the I domain of the alpha-2 subunit, in a metal ion-independent fashion.

Subunit structure

Heterodimer of subunits A and B; disulfide-linked. Ref.3

Subcellular location

Secreted.

Sequence similarities

Contains 1 C-type lectin domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandLectin
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionsugar binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.1 Ref.2
Chain24 – 157134EMS16 subunit A
PRO_0000318802

Regions

Domain34 – 153120C-type lectin

Amino acid modifications

Disulfide bond27 ↔ 38 Ref.3
Disulfide bond55 ↔ 152 Ref.3
Disulfide bond104Interchain (with C-100 in subunit B) Ref.3
Disulfide bond127 ↔ 144 Ref.3

Secondary structure

...................... 157
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7T2Q1-1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: F0D9638C6D622AB3

FASTA15718,214
        10         20         30         40         50         60 
MGRFISVSFG LLVVFLSLSG TGADFDCPSD WTAYDQHCYL AIGEPQNWYE AERFCTEQAK 

        70         80         90        100        110        120 
DGHLVSIQSR EEGNFVAQLV SGFMHRSEIY VWIGLRDRRE EQQCNPEWND GSKIIYVNWK 

       130        140        150 
EGESKMCQGL TKWTNFHDWN NINCEDLYPF VCKFSAV 

« Hide

References

[1]"Characterization and preliminary crystallographic studies of EMS16, an antagonist of collagen receptor (GPIa/IIa) from the venom of Echis multisquamatus."
Okuda D., Horii K., Mizuno H., Morita T.
J. Biochem. 134:19-23(2003) [PubMed: 12944366] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-44.
[2]"Isolation and characterization of EMS16, a C-lectin type protein from Echis multisquamatus venom, a potent and selective inhibitor of the alpha2beta1 integrin."
Marcinkiewicz C., Lobb R.R., Marcinkiewicz M.M., Daniel J.L., Smith J.B., Dangelmaier C., Weinreb P.H., Beacham D.A., Niewiarowski S.
Biochemistry 39:9859-9867(2000) [PubMed: 10933804] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-82.
[3]"Structural characterization of EMS16, an antagonist of collagen receptor (GPIa/IIa) from the venom of Echis multisquamatus."
Horii K., Okuda D., Morita T., Mizuno H.
Biochemistry 42:12497-12502(2003) [PubMed: 14580195] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-157 IN COMPLEX WITH EMS16B, DISULFIDE BONDS.
[4]"Crystal structure of EMS16 in complex with the integrin alpha2-I domain."
Horii K., Okuda D., Morita T., Mizuno H.
J. Mol. Biol. 341:519-527(2004) [PubMed: 15276841] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-157 IN COMPLEX WITH EMS16B AND ITGA2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB098253 mRNA. Translation: BAC77706.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UKMX-ray1.90A24-157[»]
1V7PX-ray1.90A24-157[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENQ7T2Q1.

Family and domain databases

InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR003990. Pancreatis_ac.
[Graphical view]
Gene3DG3DSA:3.10.100.10. C-type_lectin-like. 1 hit.
PfamPF00059. Lectin_C. 1 hit.
[Graphical view]
PRINTSPR01504. PNCREATITSAP.
SMARTSM00034. CLECT. 1 hit.
[Graphical view]
PROSITEPS00615. C_TYPE_LECTIN_1. False negative.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEM16A_ECHML
AccessionPrimary (citable) accession number: Q7T2Q1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 1, 2003
Last modified: November 24, 2009
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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