ID   VM2IA_CROAT             Reviewed;          61 AA.
AC   A2CJE5;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Disintegrin atroxatin;
DE   Flags: Fragment;
OS   Crotalus atrox (Western diamondback rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=17112685; DOI=10.1016/j.gene.2006.09.020;
RA   Soto J.G., White S.A., Reyes S.R., Regalado R., Sanchez E.E., Perez J.C.;
RT   "Molecular evolution of PIII-SVMP and RGD disintegrin genes from the genus
RT   Crotalus.";
RL   Gene 389:66-72(2007).
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 medium 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; DQ676502; ABG77586.1; -; mRNA.
DR   AlphaFoldDB; A2CJE5; -.
DR   SMR; A2CJE5; -.
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..61
FT                   /note="Disintegrin atroxatin"
FT                   /id="PRO_0000406573"
FT   DOMAIN          <1..61
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           39..41
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        9..23
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        17..47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        22..26
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        35..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   NON_TER         1
SQ   SEQUENCE   61 AA;  6467 MW;  15C2D033251BAC3E CRC64;
     NPCCDAATCK VTPGSQCAEG LCCDQCKFMK EGTVCRPARG DWNDDTCTGQ SADCPRKGIY
     G