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Protein

Snaclec rhodocetin subunit alpha

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

Potent inhibitor of collagen-induced platelet aggregation. It acts by binding to the integrin alpha2A domain and blocks collagen binding to integrin alpha-2/beta-1 (ITGA2/ITGB1). The gamma/delta subunits mainly contribute to this activity.3 Publications

Keywords - Molecular functioni

Hemostasis impairing toxin, Platelet aggregation inhibiting toxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Snaclec rhodocetin subunit alpha
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
Chaini1 – 133133Snaclec rhodocetin subunit alphaPRO_0000046706Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi2 ↔ 13
Disulfide bondi30 ↔ 127
Disulfide bondi102 ↔ 119

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterotetramer of subunit alpha, beta, gamma and delta; only the gamma and the delta subunits are disulfide-linked. Alpha-beta heterodimer and gamma-delta heterodimer associate orthogonally, giving a cruciform conformation (PubMed:19369383). This heterotetramer may covalently dimerizes thanks to the gamma subunit (PubMed:11121411).3 Publications

Structurei

Secondary structure

1
133
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 2112Combined sources
Helixi23 – 319Combined sources
Beta strandi33 – 353Combined sources
Helixi45 – 5814Combined sources
Turni59 – 613Combined sources
Beta strandi64 – 7310Combined sources
Helixi76 – 783Combined sources
Beta strandi79 – 835Combined sources
Beta strandi94 – 963Combined sources
Beta strandi100 – 11112Combined sources
Beta strandi113 – 1175Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi123 – 1308Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SB2X-ray1.90A1-133[»]
3GPRX-ray3.20A1-133[»]
ProteinModelPortaliP81397.
SMRiP81397. Positions 1-132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81397.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 129129C-type lectinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the snaclec family.Curated
Contains 1 C-type lectin domain.PROSITE-ProRule annotation

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.

P81397-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
DCPDGWSSTK SYCYRPFKEK KTWEEAERFC TEQEKEAHLV SMENRLEAVF
60 70 80 90 100
VDMVMENNFE NKIYRSWIGL KIENKGQRSN LEWSDGSSIS YENLYEPYME
110 120 130
KCFLMDHQSG LPKWHTADCE EKNVFMCKFQ LPR
Length:133
Mass (Da):15,962
Last modified:July 15, 1998 - v1
Checksum:i386EAC519DFC674D
GO

Mass spectrometryi

Molecular mass is 15955.90±1.44 Da from positions 1 - 133. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti63 – 631I → K.1 Publication
Natural varianti70 – 701L → K.1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SB2X-ray1.90A1-133[»]
3GPRX-ray3.20A1-133[»]
ProteinModelPortaliP81397.
SMRiP81397. Positions 1-132.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG004151.

Miscellaneous databases

EvolutionaryTraceiP81397.

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...

Publicationsi

  1. "Rhodocetin, a novel platelet aggregation inhibitor from the venom of Calloselasma rhodostoma (Malayan pit viper): synergistic and noncovalent interaction between its subunits."
    Wang R., Kini R.M., Chung M.C.M.
    Biochemistry 38:7584-7593(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY.
    Tissue: Venom.
  2. "The alpha2beta1 integrin-specific antagonist rhodocetin is a cruciform, heterotetrameric molecule."
    Eble J.A., Niland S., Bracht T., Mormann M., Peter-Katalinic J., Pohlentz G., Stetefeld J.
    FASEB J. 23:2917-2927(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, SUBUNIT, DISULFIDE BONDS, VARIANT LYS-70, X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF HETEROTETRAMER, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Venom.
  3. "Purification and characterization of a variant of rhodocetin from Calloselasma rhodostoma (Malayan pit viper) venom."
    Kong C., Chung M.C.
    J. Protein Chem. 20:383-390(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, VARIANT LYS-63.
  4. "alpha 2beta 1 integrin is not recognized by rhodocytin but is the specific, high affinity target of rhodocetin, an RGD-independent disintegrin and potent inhibitor of cell adhesion to collagen."
    Eble J.A., Beermann B., Hinz H.J., Schmidt-Hederich A.
    J. Biol. Chem. 276:12274-12284(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-21, FUNCTION.
  5. "The alpha2beta1 integrin inhibitor rhodocetin binds to the A-domain of the integrin alpha2 subunit proximal to the collagen-binding site."
    Eble J.A., Tuckwell D.S.
    Biochem. J. 376:77-85(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Structure of rhodocetin reveals noncovalently bound heterodimer interface."
    Paaventhan P., Kong C., Joseph J.S., Chung M.C., Kolatkar P.R.
    Protein Sci. 14:169-175(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH RHCB, DISULFIDE BONDS.

Entry informationi

Entry nameiSLEA_CALRH
AccessioniPrimary (citable) accession number: P81397
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: October 14, 2015
This is version 80 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.