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Protein

Snaclec botrocetin subunit alpha

Gene
N/A
Organism
Bothrops jararaca (Jararaca) (Bothrops jajaraca)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Snaclec that binds to von Willebrand factor (VWF) and induces its interaction with GPIbalpha (GP1BA) (via the vWF A1 domain), resulting in platelet aggregation.

Keywords - Molecular functioni

Hemostasis impairing toxin, Platelet aggregation activating toxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Snaclec botrocetin subunit alpha
Alternative name(s):
Platelet coagglutinin
OrganismiBothrops jararaca (Jararaca) (Bothrops jajaraca)
Taxonomic identifieri8724 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Biotechnological usei

Is a standard reagent for testing vWF/platelet interactions and detection of the defects in von Willebrand disease and in GPIb-related disorders such as Bernard-Soulier syndrome.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000466971 – 133Snaclec botrocetin subunit alphaAdd BLAST133

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi2 ↔ 13PROSITE-ProRule annotation1 Publication
Disulfide bondi30 ↔ 128
Disulfide bondi80Interchain (with C-75 in beta chain)
Disulfide bondi103 ↔ 120

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterodimer of subunits alpha and beta; disulfide-linked. Botrocetin and vWF form a soluble complex.4 Publications

Structurei

Secondary structure

1133
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 9Combined sources3
Beta strandi12 – 21Combined sources10
Helixi23 – 33Combined sources11
Beta strandi44 – 46Combined sources3
Helixi48 – 59Combined sources12
Beta strandi66 – 73Combined sources8
Beta strandi76 – 80Combined sources5
Beta strandi85 – 87Combined sources3
Helixi97 – 99Combined sources3
Beta strandi103 – 107Combined sources5
Turni108 – 111Combined sources4
Beta strandi114 – 118Combined sources5
Beta strandi124 – 130Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FVUX-ray1.80A/C1-133[»]
1IJKX-ray2.60B1-133[»]
1U0NX-ray2.95B1-133[»]
1U0OX-ray2.70A1-133[»]
ProteinModelPortaliP22029.
SMRiP22029.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22029.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 129C-type lectinPROSITE-ProRule annotationAdd BLAST121

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-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.

P22029-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
DCPSGWSSYE GNCYKFFQQK MNWADAERFC SEQAKGGHLV SIKIYSKEKD
60 70 80 90 100
FVGDLVTKNI QSSDLYAWIG LRVENKEKQC SSEWSDGSSV SYENVVERTV
110 120 130
KKCFALEKDL GFVLWINLYC AQKNPFVCKS PPP
Length:133
Mass (Da):15,215
Last modified:July 1, 1993 - v2
Checksum:iE4CF4502946AC74B
GO

Sequence databases

PIRiA47267.

Cross-referencesi

Sequence databases

PIRiA47267.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FVUX-ray1.80A/C1-133[»]
1IJKX-ray2.60B1-133[»]
1U0NX-ray2.95B1-133[»]
1U0OX-ray2.70A1-133[»]
ProteinModelPortaliP22029.
SMRiP22029.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG004151.

Miscellaneous databases

EvolutionaryTraceiP22029.

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 nameiSLEA_BOTJA
AccessioniPrimary (citable) accession number: P22029
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 1, 1993
Last modified: November 30, 2016
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

There are two distinct forms of the vWF-dependent platelet coagglutinin. The dimeric form (snaclec) is 34-fold more active than the metalloprotease botrocetin in promoting vWF binding to platelets (PubMed:1993206).1 Publication

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.