Hmdb loader
Identification
HMDB Protein ID HMDBP14152
Secondary Accession Numbers None
Name Zinc metalloproteinase/disintegrin
Synonyms Not Available
Gene Name Not Available
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function impairs hemostasis in the envenomed animal.inhibit platelet aggregation induced by ADP, thrombin, platelet-activating factor and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors alpha-IIb/beta-3 (ITGA2B/ITGB3).
Pathways Not Available
Reactions Not Available
GO Classification
Cellular Component
extracellular region
Molecular Function
metal ion binding
metalloendopeptidase activity
toxin activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues Not Available
Molecular Weight 54005.575
Theoretical pI Not Available
Pfam Domain Function
Signals
  • 1-20;
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P30403
UniProtKB/Swiss-Prot Entry Name VM2RH_CALRH
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Au LC, Chou JS, Chang KJ, Teh GW, Lin SB: Nucleotide sequence of a full-length cDNA encoding a common precursor of platelet aggregation inhibitor and hemorrhagic protein from Calloselasma rhodostoma venom. Biochim Biophys Acta. 1993 May 28;1173(2):243-5. doi: 10.1016/0167-4781(93)90190-o. [PubMed:7916635 ]
  2. Au LC, Huang YB, Huang TF, Teh GW, Lin HH, Choo KB: A common precursor for a putative hemorrhagic protein and rhodostomin, a platelet aggregation inhibitor of the venom of Calloselasma rhodostoma: molecular cloning and sequence analysis. Biochem Biophys Res Commun. 1991 Dec 16;181(2):585-93. doi: 10.1016/0006-291x(91)91230-a. [PubMed:1755841 ]
  3. Chang HH, Hu ST, Huang TF, Chen SH, Lee YH, Lo SJ: Rhodostomin, an RGD-containing peptide expressed from a synthetic gene in Escherichia coli, facilitates the attachment of human hepatoma cells. Biochem Biophys Res Commun. 1993 Jan 15;190(1):242-9. doi: 10.1006/bbrc.1993.1037. [PubMed:7916592 ]
  4. Chung MC, Ponnudurai G, Kataoka M, Shimizu S, Tan NH: Structural studies of a major hemorrhagin (rhodostoxin) from the venom of Calloselasma rhodostoma (Malayan pit viper). Arch Biochem Biophys. 1996 Jan 15;325(2):199-208. doi: 10.1006/abbi.1996.0025. [PubMed:8561498 ]
  5. Gould RJ, Polokoff MA, Friedman PA, Huang TF, Holt JC, Cook JJ, Niewiarowski S: Disintegrins: a family of integrin inhibitory proteins from viper venoms. Proc Soc Exp Biol Med. 1990 Nov;195(2):168-71. doi: 10.3181/00379727-195-43129b. [PubMed:2236100 ]
  6. Dennis MS, Henzel WJ, Pitti RM, Lipari MT, Napier MA, Deisher TA, Bunting S, Lazarus RA: Platelet glycoprotein IIb-IIIa protein antagonists from snake venoms: evidence for a family of platelet-aggregation inhibitors. Proc Natl Acad Sci U S A. 1990 Apr;87(7):2471-5. doi: 10.1073/pnas.87.7.2471. [PubMed:2320569 ]
  7. Adler M, Lazarus RA, Dennis MS, Wagner G: Solution structure of kistrin, a potent platelet aggregation inhibitor and GP IIb-IIIa antagonist. Science. 1991 Jul 26;253(5018):445-8. doi: 10.1126/science.1862345. [PubMed:1862345 ]
  8. Adler M, Wagner G: Sequential 1H NMR assignments of kistrin, a potent platelet aggregation inhibitor and glycoprotein IIb-IIIa antagonist. Biochemistry. 1992 Feb 4;31(4):1031-9. doi: 10.1021/bi00119a011. [PubMed:1734953 ]