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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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 4›4Sequence analysis
Chaini5 – 135131Snaclec echicetin subunit alphaPRO_0000355265Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi6 ↔ 17PROSITE-ProRule annotation1 Publication
Disulfide bondi34 ↔ 129PROSITE-ProRule annotation1 Publication
Disulfide bondi82 – 82Interchain (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

1
135
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 133Combined sources
Beta strandi16 – 2510Combined sources
Helixi27 – 3711Combined sources
Helixi49 – 6214Combined sources
Beta strandi67 – 759Combined sources
Helixi79 – 813Combined sources
Beta strandi87 – 904Combined sources
Beta strandi104 – 1085Combined sources
Helixi109 – 1113Combined sources
Beta strandi115 – 1195Combined sources
Beta strandi125 – 1317Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ7T248.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 130118C-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: 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)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1OZ7X-ray2.40A5-135[»]
ProteinModelPortaliQ7T248.
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.
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 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: March 4, 2015
This is version 46 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.