ID VM2OI_ECHOC Reviewed; 49 AA.
AC P0C6R6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 22-FEB-2023, entry version 43.
DE RecName: Full=Disintegrin ocellatin;
OS Echis ocellatus (Ocellated saw-scaled viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX NCBI_TaxID=99586;
RN [1]
RP PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=11275562; DOI=10.1093/oxfordjournals.jbchem.a002898;
RA Okuda D., Nozaki C., Sekiya F., Morita T.;
RT "Comparative biochemistry of disintegrins isolated from snake venom:
RT consideration of the taxonomy and geographical distribution of snakes in
RT the genus Echis.";
RL J. Biochem. 129:615-620(2001).
CC -!- FUNCTION: Inhibits ADP-induced human platelet aggregation.
CC {ECO:0000269|PubMed:11275562}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: The disintegrin belongs to the short disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIa sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0C6R6; -.
DR SMR; P0C6R6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 1: Evidence at protein level;
KW Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Platelet aggregation inhibiting toxin;
KW Secreted; Toxin.
FT CHAIN 1..49
FT /note="Disintegrin ocellatin"
FT /id="PRO_0000326266"
FT DOMAIN 1..47
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 24..26
FT /note="Cell attachment site"
FT DISULFID 2..11
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 7..32
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 8..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 20..39
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 49 AA; 5526 MW; 4D839AE169A704F2 CRC64;
DCESGPCCDN CKFLKEGTIC KMARGDNMHH YCNGKTCDCP RNPYKGEHD
//
