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P81397 (RHCA_CALRH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Rhodocetin subunit alpha
OrganismCalloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma)
Taxonomic identifier8717 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaViperidaeCrotalinaeCalloselasma

Protein attributes

Sequence length133 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

A potent inhibitor of collagen-induced platelet aggregation. Individually, neither subunit inhibits platelet aggregation. Both subunits are essential. Ref.1

Subunit structure

Heterodimer of subunits alpha and beta; held together by noncovalent interactions rather than by intersubunit disulfide bridges. Ref.1

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Contains 1 C-type lectin domain.

Mass spectrometry

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

Ontologies

Keywords
   Cellular componentSecreted
   LigandLectin
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionsugar binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 133133Rhodocetin subunit alpha
PRO_0000046706

Regions

Domain1 – 129129C-type lectin

Amino acid modifications

Disulfide bond2 ↔ 13 Ref.2
Disulfide bond30 ↔ 127 Ref.2
Disulfide bond102 ↔ 119 Ref.2

Secondary structure

...................... 133
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P81397 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: 386EAC519DFC674D

FASTA13315,962
        10         20         30         40         50         60 
DCPDGWSSTK SYCYRPFKEK KTWEEAERFC TEQEKEAHLV SMENRLEAVF VDMVMENNFE 

        70         80         90        100        110        120 
NKIYRSWIGL KIENKGQRSN LEWSDGSSIS YENLYEPYME KCFLMDHQSG LPKWHTADCE 

       130 
EKNVFMCKFQ LPR 

« Hide

References

[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: 10360956] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, MASS SPECTROMETRY.
Tissue: Venom.
[2]"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: 15576563] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH RHCB, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SB2X-ray1.90A1-133[»]
3GPRX-ray3.20A1-133[»]
ProteinModelPortalP81397.
SMRP81397. Positions 1-132.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG004151.

Family and domain databases

InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
Gene3DG3DSA:3.10.100.10. C-type_lectin-like. 1 hit.
PfamPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMSSF56436. C-type_lectin_fold. 1 hit.
PROSITEPS00615. C_TYPE_LECTIN_1. False negative.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRHCA_CALRH
AccessionPrimary (citable) accession number: P81397
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families