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Protein

Snaclec EMS16 subunit alpha

Gene
N/A
Organism
Echis multisquamatus (Central Asian sand viper)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei84 – 841Key residue for binding with integrin
Sitei90 – 901Key residue for binding with integrin
Sitei133 – 1331Key residue for binding with integrin

Keywords - Molecular functioni

Hemostasis impairing toxin, Platelet aggregation inhibiting toxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Snaclec EMS16 subunit alpha
Short name:
EMS16A
OrganismiEchis multisquamatus (Central Asian sand viper)
Taxonomic identifieri93050 [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
Signal peptidei1 – 23232 PublicationsAdd
BLAST
Chaini24 – 157134Snaclec EMS16 subunit alphaPRO_0000318802Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 38PROSITE-ProRule annotation1 Publication
Disulfide bondi55 ↔ 152PROSITE-ProRule annotation1 Publication
Disulfide bondi104 – 104Interchain (with C-100 in subunit B)PROSITE-ProRule annotation1 Publication
Disulfide bondi127 ↔ 144PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterodimer of subunits A and B; disulfide-linked.2 Publications

Structurei

Secondary structure

1
157
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 343Combined sources
Beta strandi37 – 4610Combined sources
Helixi48 – 5811Combined sources
Helixi70 – 7910Combined sources
Helixi81 – 855Combined sources
Beta strandi90 – 978Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi127 – 1315Combined sources
Helixi132 – 1343Combined sources
Beta strandi138 – 1425Combined sources
Beta strandi148 – 1558Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UKMX-ray1.90A24-157[»]
1V7PX-ray1.90A24-157[»]
ProteinModelPortaliQ7T2Q1.
SMRiQ7T2Q1. Positions 24-157.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7T2Q1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 153120C-type lectinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the snaclec family.Curated
Contains 1 C-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG004151.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q7T2Q1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRFISVSFG LLVVFLSLSG TGADFDCPSD WTAYDQHCYL AIGEPQNWYE
60 70 80 90 100
AERFCTEQAK DGHLVSIQSR EEGNFVAQLV SGFMHRSEIY VWIGLRDRRE
110 120 130 140 150
EQQCNPEWND GSKIIYVNWK EGESKMCQGL TKWTNFHDWN NINCEDLYPF

VCKFSAV
Length:157
Mass (Da):18,214
Last modified:October 1, 2003 - v1
Checksum:iF0D9638C6D622AB3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB098253 mRNA. Translation: BAC77706.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB098253 mRNA. Translation: BAC77706.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UKMX-ray1.90A24-157[»]
1V7PX-ray1.90A24-157[»]
ProteinModelPortaliQ7T2Q1.
SMRiQ7T2Q1. Positions 24-157.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG004151.

Miscellaneous databases

EvolutionaryTraceiQ7T2Q1.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-157 IN COMPLEX WITH EMS16B AND ITGA2, SITES.

Entry informationi

Entry nameiSLA_ECHML
AccessioniPrimary (citable) accession number: Q7T2Q1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 1, 2003
Last modified: October 14, 2015
This is version 52 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.