ID   DID4_MACLO              Reviewed;          65 AA.
AC   P0C6A8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Disintegrin VLO4;
OS   Macrovipera lebetina obtusa (Levant blunt-nosed viper) (Vipera lebetina
OS   obtusa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Macrovipera.
OX   NCBI_TaxID=209528;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=12667142; DOI=10.1042/bj20021739;
RA   Calvete J.J., Moreno-Murciano M.P., Theakston R.D.G., Kisiel D.G.,
RA   Marcinkiewicz C.;
RT   "Snake venom disintegrins: novel dimeric disintegrins and structural
RT   diversification by disulphide bond engineering.";
RL   Biochem. J. 372:725-734(2003).
CC   -!- FUNCTION: Poor inhibitor of platelet aggregation. The disintegrin
CC       inhibits the adhesion of cells expressing the RGD-dependent integrin
CC       alpha-5/beta-1 (ITGA5/ITGB1) to immobilized fibronectin. Inhibition on
CC       alpha-2b/beta-3 (ITGA2B/ITGB3) is low. {ECO:0000269|PubMed:12667142}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:12667142}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12667142}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=14196; Method=MALDI; Note=Homodimer.;
CC       Evidence={ECO:0000269|PubMed:12667142};
CC   -!- MISCELLANEOUS: Does no inhibit alpha-1/beta-1 (ITGA1/ITGB1), alpha-
CC       2/beta-1 (ITGA2/ITGB1) and alpha-6/beta-1 (ITGA6/ITGB1).
CC       {ECO:0000305|PubMed:12667142}.
CC   -!- SIMILARITY: Belongs to the disintegrin family. Dimeric disintegrin
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C6A8; -.
DR   SMR; P0C6A8; -.
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   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..65
FT                   /note="Disintegrin VLO4"
FT                   /id="PRO_0000319023"
FT   DOMAIN          1..65
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           43..45
FT                   /note="Cell attachment site"
FT   DISULFID        7..30
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        8
FT                   /note="Interchain (with C-8)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        13
FT                   /note="Interchain (with C-13)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        21..27
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        26..51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        39..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ   SEQUENCE   65 AA;  7108 MW;  FF715C1D6BF713E3 CRC64;
     MNSGNPCCDP VTCKPRRGEH CVSGPCCRNC KFLNAGTICK RARGDDMNDY CTGISPDCPR
     NPWKG