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Protein

Snaclec EMS16 subunit beta

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
Sitei88 – 881Key residue for binding with integrin
Sitei118 – 1181Key residue for binding with integrin
Sitei127 – 1271Key residue for binding with integrin
Sitei140 – 1401Key residue for binding with integrin
Sitei141 – 1411Key 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 beta
Short name:
EMS16B
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 – 26262 PublicationsAdd
BLAST
Chaini27 – 154128Snaclec EMS16 subunit betaPRO_0000318803Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 38PROSITE-ProRule annotation1 Publication
Glycosylationi47 – 471N-linked (GlcNAc...)1 Publication
Disulfide bondi55 ↔ 146PROSITE-ProRule annotation1 Publication
Disulfide bondi100 – 100Interchain (with C-104 in subunit A)PROSITE-ProRule annotation1 Publication
Disulfide bondi121 ↔ 138PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

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
154
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 343Combined sources
Beta strandi37 – 4610Combined sources
Helixi48 – 5811Combined sources
Helixi70 – 8314Combined sources
Beta strandi88 – 947Combined sources
Turni96 – 994Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi120 – 1267Combined sources
Beta strandi131 – 1377Combined sources
Beta strandi142 – 1498Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UKMX-ray1.90B27-154[»]
1V7PX-ray1.90B27-154[»]
ProteinModelPortaliQ7T2Q0.
SMRiQ7T2Q0. Positions 27-153.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7T2Q0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 147114C-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.

Q7T2Q0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRLISVRFS LLVVFLSLSG IGAGLCCPLG WSSFDQHCYK VFEPVKNWTE
60 70 80 90 100
AEEICMQQHK GSRLASIHGS EEEAFVSKLA SKALKFTSMW IGLNNPWKDC
110 120 130 140 150
KWEWSDNARF DYKAWKRRPY CTVMVVKPDR IFWFTRGCEK SVSFVCKFLT

DPAV
Length:154
Mass (Da):17,761
Last modified:October 1, 2003 - v1
Checksum:i65CD672DDB29168E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691G → S (PubMed:14580195).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB098254 mRNA. Translation: BAC77707.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB098254 mRNA. Translation: BAC77707.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UKMX-ray1.90B27-154[»]
1V7PX-ray1.90B27-154[»]
ProteinModelPortaliQ7T2Q0.
SMRiQ7T2Q0. Positions 27-153.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG004151.

Miscellaneous databases

EvolutionaryTraceiQ7T2Q0.

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 27-52.
    Tissue: Venom gland.
  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 27-67.
  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 27-154 IN COMPLEX WITH EMS16A, GLYCOSYLATION AT ASN-47, 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 27-154 IN COMPLEX WITH EMS16A AND ITGA2, SITES.

Entry informationi

Entry nameiSLB_ECHML
AccessioniPrimary (citable) accession number: Q7T2Q0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 1, 2003
Last modified: October 14, 2015
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin 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.