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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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23234 PublicationsAdd
BLAST
Chaini24 – 146123Snaclec rhodocytin subunit betaPRO_0000355239Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi25 ↔ 36
Disulfide bondi53 ↔ 142
Disulfide bondi98 – 98Interchain (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

1
146
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 323Combined sources
Beta strandi35 – 4410Combined sources
Helixi46 – 5510Combined sources
Beta strandi56 – 583Combined sources
Helixi68 – 7811Combined sources
Turni79 – 846Combined sources
Beta strandi85 – 884Combined sources
Beta strandi96 – 983Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi118 – 1236Combined sources
Beta strandi129 – 1335Combined sources
Beta strandi138 – 1458Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VRPX-ray2.41B24-146[»]
3BX4X-ray1.70B/D1-146[»]
3WWKX-ray2.98B/E/H/K1-146[»]
ProteinModelPortaliQ9I840.
SMRiQ9I840. Positions 24-146.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9I840.

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.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_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
EntryMethodResolution (Å)ChainPositionsPDBsum
2VRPX-ray2.41B24-146[»]
3BX4X-ray1.70B/D1-146[»]
3WWKX-ray2.98B/E/H/K1-146[»]
ProteinModelPortaliQ9I840.
SMRiQ9I840. Positions 24-146.
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.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_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...

Publicationsi

  1. "Molecular cloning and sequence analysis of aggretin, a collagen-like platelet aggregation inducer."
    Chung C.-H., Au L.-C., Huang T.-F.
    Biochem. Biophys. Res. Commun. 263:723-727(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-41.
    Tissue: Venom and Venom gland.
  2. "Aggretin, a heterodimeric C-type lectin from Calloselasma rhodostoma (malayan pit viper), stimulates platelets by binding to alpha 2beta 1 integrin and glycoprotein Ib, activating Syk and phospholipase Cgamma 2, but does not involve the glycoprotein VI/Fc receptor gamma chain collagen receptor."
    Navdaev A., Clemetson J.M., Polgar J., Kehrel B.E., Glauner M., Magnenat E., Wells T.N.C., Clemetson K.J.
    J. Biol. Chem. 276:20882-20889(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-53, FUNCTION.
  3. "Rhodocytin, a functional novel platelet agonist belonging to the heterodimeric C-type lectin family, induces platelet aggregation independently of glycoprotein Ib."
    Shin Y., Morita T.
    Biochem. Biophys. Res. Commun. 245:741-745(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-43, FUNCTION, SUBUNIT.
    Tissue: Venom.
  4. "A novel dimer of a C-type lectin-like heterodimer from the venom of Calloselasma rhodostoma (Malayan pit viper)."
    Wang R., Kong C., Kolatkar P., Chung M.C.
    FEBS Lett. 508:447-453(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-42, FUNCTION, SUBUNIT.
  5. "Aggretin, a novel platelet-aggregation inducer from snake (Calloselasma rhodostoma) venom, activates phospholipase C by acting as a glycoprotein Ia/IIa agonist."
    Huang T.-F., Liu C.-Z., Yang S.-H.
    Biochem. J. 309:1021-1027(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Tissue: Venom.
  6. "Aggretin, a C-type lectin protein, induces platelet aggregation via integrin alpha(2)beta(1) and GPIb in a phosphatidylinositol 3-kinase independent pathway."
    Chung C.-H., Peng H.-C., Huang T.-F.
    Biochem. Biophys. Res. Commun. 285:689-695(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Rhodocytin (aggretin) activates platelets lacking alpha(2)beta(1) integrin, glycoprotein VI, and the ligand-binding domain of glycoprotein Ibalpha."
    Bergmeier W., Bouvard D., Eble J.A., Mokhtari-Nejad R., Schulte V., Zirngibl H., Brakebusch C., Fassler R., Nieswandt B.
    J. Biol. Chem. 276:25121-25126(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Aggretin, a snake venom-derived endothelial integrin alpha 2 beta 1 agonist, induces angiogenesis via expression of vascular endothelial growth factor."
    Chung C.-H., Wu W.-B., Huang T.-F.
    Blood 103:2105-2113(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: FUNCTION.
  10. "The crystal structure of the platelet activator aggretin reveals a novel (alphabeta)2 dimeric structure."
    Hooley E., Papagrigoriou E., Navdaev A., Pandey A.V., Clemetson J.M., Clemetson K.J., Emsley J.
    Biochemistry 47:7831-7837(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 24-146, SUBUNIT, DISULFIDE BONDS.
  11. "Crystal structure of rhodocytin, a ligand for the platelet-activating receptor CLEC-2."
    Watson A.A., Eble J.A., O'Callaghan C.A.
    Protein Sci. 17:1611-1616(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 24-146, SUBUNIT, DISULFIDE BONDS.

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: October 14, 2015
This is version 64 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.