VM2A6_VIPAA
ID VM2A6_VIPAA Reviewed; 64 AA.
AC P0C6A5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Disintegrin VA6;
OS Vipera ammodytes ammodytes (Western sand viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX NCBI_TaxID=8705;
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-IIb/beta-3 (ITGA2B/ITGB3) is low, and there is no inhibition on
CC alpha-1/beta-1 (ITGA1/ITGB1), alpha-2/beta-1 (ITGA2/ITGB1) and alpha-
CC 6/beta-1 (ITGA6/ITGB1). {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=14046; Method=MALDI; Note=Homodimer.;
CC Evidence={ECO:0000269|PubMed:12667142};
CC -!- MISCELLANEOUS: The disintegrin belongs to the dimeric disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IId sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0C6A5; -.
DR SMR; P0C6A5; -.
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..64
FT /note="Disintegrin VA6"
FT /id="PRO_0000319020"
FT DOMAIN 1..64
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 42..44
FT /note="Cell attachment site"
FT DISULFID 6..29
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 7
FT /note="Interchain (with C-7)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 12
FT /note="Interchain (with C-12)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 20..26
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 25..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 38..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 64 AA; 7023 MW; 8A29E7115E0115E3 CRC64;
NSANPCCDPV TCKPRRGEHC VSGPCCRNCK FLNAGTICRY ARGDDMNDYC TGVTSDCPRN
PYKS
