ID   VM2D3_BITAR             Reviewed;          83 AA.
AC   Q4JCS0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Disintegrin isoform D-3;
OS   Bitis arietans (African puff adder).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Bitis.
OX   NCBI_TaxID=8692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Oliver J., Theakston R.D.G., Harrison R.A.;
RT   "Isolation of cDNAs encoding five Bitis arietans disintegrin isoforms and
RT   identification of shared antigenic epitopes.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inhibits fibrinogen interaction with platelets. Acts by
CC       binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) on the platelet surface and
CC       inhibits aggregation induced by ADP, thrombin, platelet-activating
CC       factor and collagen (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer (disintegrin). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: The disintegrin belongs to the long 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   EMBL; AY924404; AAY43683.1; -; mRNA.
DR   AlphaFoldDB; Q4JCS0; -.
DR   SMR; Q4JCS0; -.
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; -; 1.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   Pfam; PF00200; Disintegrin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion impairing toxin; Disulfide bond; Hemostasis impairing toxin;
KW   Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT   CHAIN           1..83
FT                   /note="Disintegrin isoform D-3"
FT                   /id="PRO_0000318183"
FT   DOMAIN          2..83
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           64..66
FT                   /note="Cell attachment site"
FT   DISULFID        5..24
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        16..34
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        18..29
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        28..51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        42..48
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        47..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        60..79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ   SEQUENCE   83 AA;  9064 MW;  967B1F1A7176967C CRC64;
     SPPVCGNELL EEGEECDCGS PANCQDRCCN AATCKLTPGS QCSYGECCDQ CKFKKARTVC
     RIARGDWNDD YCTGKSSDCP WNH