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Protein

Snaclec echicetin subunit alpha

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 GPIbalpha (GP1BA) receptor on platelets alone results in inhibition of platelet aggregation, while binding to both GP1BA 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 alpha
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)DescriptionActionsGraphical viewLength
Signal peptidei‹1 – 4Sequence analysis›4
ChainiPRO_00003552655 – 135Snaclec echicetin subunit alphaAdd BLAST131

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi6 ↔ 17PROSITE-ProRule annotation1 Publication
Disulfide bondi34 ↔ 129PROSITE-ProRule annotation1 Publication
Disulfide bondi82Interchain (with C-98 in subunit beta)PROSITE-ProRule annotation1 Publication
Disulfide bondi104 ↔ 121PROSITE-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

1135
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 13Combined sources3
Beta strandi16 – 25Combined sources10
Helixi27 – 37Combined sources11
Helixi49 – 62Combined sources14
Beta strandi67 – 75Combined sources9
Helixi79 – 81Combined sources3
Beta strandi87 – 90Combined sources4
Beta strandi104 – 108Combined sources5
Helixi109 – 111Combined sources3
Beta strandi115 – 119Combined sources5
Beta strandi125 – 131Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OZ7X-ray2.40A5-135[»]
ProteinModelPortaliQ7T248.
SMRiQ7T248.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7T248.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 130C-type lectinPROSITE-ProRule annotationAdd BLAST118

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-like.
IPR016186. C-type_lectin-like/link.
IPR016187. CTDL_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: Fragment.

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

Q7T248-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
GADEMCPPGW SSNGVYCYML FKEPKTWDEA EKFCNKQGKD GHLLSIESKK
60 70 80 90 100
EEILVDIVVS ENIGKMYKIW TGLSERSKEQ HCSSRWSDGS FFRSYEIAIR
110 120 130
YSECFVLEKQ SVFRTWVATP CENTFPFMCK YPVPR
Length:135
Mass (Da):15,735
Last modified:November 25, 2008 - v2
Checksum:i5095AA5AA7BE5024
GO

Sequence cautioni

The sequence AAP41218 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY268947 mRNA. Translation: AAP41218.2. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY268947 mRNA. Translation: AAP41218.2. Different initiation.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OZ7X-ray2.40A5-135[»]
ProteinModelPortaliQ7T248.
SMRiQ7T248.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG004151.

Miscellaneous databases

EvolutionaryTraceiQ7T248.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR016187. CTDL_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 nameiSLA_ECHCA
AccessioniPrimary (citable) accession number: Q7T248
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 25, 2008
Last modified: November 30, 2016
This is version 48 of the entry and version 2 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.