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Protein

Snaclec rhodocytin subunit beta

Gene
N/A
Organism
Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Elicits platelet aggregation by the binding to the C-type lectin domain family 1 member B (CLEC1B/CLEC2). Binding leads to tyrosine phosphorylation in the cytoplasmic tail of CLEC1B, which promotes the binding of spleen tyrosine kinase (Syk), subsequent activation of PLCgamma2, and platelet activation and aggregation. Binding to GPIbalpha (GP1BA) and alpha2/beta-1 (ITGA2/ITGB1) may also induce aggregation, but this is controversial.8 Publications

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hemostasis impairing toxin, Platelet aggregation activating toxin, Toxin

Keywords - Ligandi

Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Snaclec rhodocytin subunit beta
Alternative name(s):
Aggretin beta chain
Rhodoaggretin subunit beta
OrganismiCalloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma)
Taxonomic identifieri8717 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeCalloselasma

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 234 PublicationsAdd BLAST23
ChainiPRO_000035523924 – 146Snaclec rhodocytin subunit betaAdd BLAST123

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi25 ↔ 36
Disulfide bondi53 ↔ 142
Disulfide bondi98Interchain (with C-83 in alpha chain)
Disulfide bondi119 ↔ 134

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Dimer (non-covalently linked) of heterodimers of subunits alpha and beta (disulfide-linked).4 Publications

Protein-protein interaction databases

DIPiDIP-61335N.

Structurei

Secondary structure

1146
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 32Combined sources3
Beta strandi35 – 44Combined sources10
Helixi46 – 55Combined sources10
Beta strandi56 – 58Combined sources3
Helixi68 – 78Combined sources11
Turni79 – 84Combined sources6
Beta strandi85 – 88Combined sources4
Beta strandi96 – 98Combined sources3
Beta strandi100 – 102Combined sources3
Beta strandi118 – 123Combined sources6
Beta strandi129 – 133Combined sources5
Beta strandi138 – 145Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VRPX-ray2.41B24-146[»]
3BX4X-ray1.70B/D1-146[»]
3WWKX-ray2.98B/E/H/K1-146[»]
ProteinModelPortaliQ9I840.
SMRiQ9I840.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9I840.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 143C-type lectinPROSITE-ProRule annotationAdd BLAST112

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.
IPR018378. C-type_lectin_CS.
IPR016187. CTDL_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9I840-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRFIFVSFG LLVVFLSLSG TGADCPSGWS SYEGHCYKPF NEPKNWADAE
60 70 80 90 100
RFCKLQPKHS HLVSFQSAEE ADFVVKLTRP RLKANLVWMG LSNIWHGCNW
110 120 130 140
QWSDGARLNY KDWQEQSECL AFRGVHTEWL NMDCSSTCSF VCKFKA
Length:146
Mass (Da):16,770
Last modified:October 1, 2000 - v1
Checksum:i930839140CFD8908
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF244901 mRNA. Translation: AAF79953.1.
PIRiJC7105.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF244901 mRNA. Translation: AAF79953.1.
PIRiJC7105.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VRPX-ray2.41B24-146[»]
3BX4X-ray1.70B/D1-146[»]
3WWKX-ray2.98B/E/H/K1-146[»]
ProteinModelPortaliQ9I840.
SMRiQ9I840.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61335N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG004151.

Miscellaneous databases

EvolutionaryTraceiQ9I840.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR016187. CTDL_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSLYB_CALRH
AccessioniPrimary (citable) accession number: Q9I840
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: October 1, 2000
Last modified: November 30, 2016
This is version 68 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.