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Protein

Snaclec echicetin subunit beta

Gene
N/A
Organism
Echis carinatus (Saw-scaled viper)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Binding of echicetin to glycoprotein Ibalpha (GP1BA) receptor on platelets alone results in inhibition of platelet aggregation, while binding to both GPIba receptor and IgMk promotes platelet aggregation and signal transduction.By similarity

Keywords - Molecular functioni

Hemostasis impairing toxin, Platelet aggregation activating toxin, Platelet aggregation inhibiting toxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Snaclec echicetin subunit beta
OrganismiEchis carinatus (Saw-scaled viper)
Taxonomic identifieri40353 [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 – 2323Sequence analysisAdd
BLAST
Chaini24 – 146123Snaclec echicetin subunit betaPRO_0000355266Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi25 ↔ 36PROSITE-ProRule annotation1 Publication
Disulfide bondi53 ↔ 142PROSITE-ProRule annotation1 Publication
Disulfide bondi98 – 98Interchain (with C-78 in subunit alpha)PROSITE-ProRule annotation1 Publication
Disulfide bondi119 ↔ 134PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterodimer of subunits alpha and beta; disulfide-linked.1 Publication

Structurei

Secondary structure

1
146
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 323Combined sources
Beta strandi35 – 4410Combined sources
Helixi46 – 5611Combined sources
Helixi70 – 767Combined sources
Turni80 – 834Combined sources
Beta strandi85 – 928Combined sources
Helixi97 – 993Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi119 – 1235Combined sources
Turni124 – 1274Combined sources
Beta strandi128 – 1325Combined sources
Beta strandi138 – 1458Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OZ7X-ray2.40B24-146[»]
ProteinModelPortaliQ7T247.
SMRiQ7T247. Positions 24-146.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7T247.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 143112C-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.

Q7T247-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRFISVSFG LLVLLLSLSG TGANCLPDWS VYEGYCYKVF KERMNWADAE
60 70 80 90 100
KFCTKQHKDG HLVSFRNSKE VDFVISLAFP MLKNDLVWIG LTDYWRDCNW
110 120 130 140
EWSDGAQLDY KAWDNERHCF IYKNTDNQWT RRDCTWTFSF VCKCPA
Length:146
Mass (Da):17,243
Last modified:October 1, 2003 - v1
Checksum:iE2F46A51D6DC6831
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY268948 mRNA. Translation: AAP41219.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY268948 mRNA. Translation: AAP41219.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OZ7X-ray2.40B24-146[»]
ProteinModelPortaliQ7T247.
SMRiQ7T247. Positions 24-146.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG004151.

Miscellaneous databases

EvolutionaryTraceiQ7T247.

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...

Entry informationi

Entry nameiSLB_ECHCA
AccessioniPrimary (citable) accession number: Q7T247
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: October 1, 2003
Last modified: October 14, 2015
This is version 51 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

Caution

The name echicetin has been given to 2 different proteins, this one from E.carinatus and another one for which the subspecies has been specified (E.carinatus sochureki). Most experiments have been done on E.carinatus sochureki.Curated

Keywords - Technical termi

3D-structure

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.