VM25A_MACLO
ID VM25A_MACLO Reviewed; 64 AA.
AC P0C6A9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Disintegrin VLO5A;
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, AND SUBCELLULAR LOCATION.
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 the alpha-4/beta-1 (ITGA4/ITGB1) integrin to
CC VCAM-1. Inhibition on alpha-IIb/beta-3 (ITGA2B/ITGB3) is low.
CC {ECO:0000269|PubMed:12667142}.
CC -!- SUBUNIT: Heterodimer with VLO5B; disulfide-linked.
CC {ECO:0000269|PubMed:12667142}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12667142}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: Does not 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 -!- MISCELLANEOUS: The disintegrin belongs to the dimeric disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIe sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0C6A9; -.
DR SMR; P0C6A9; -.
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 VLO5A"
FT /id="PRO_0000319024"
FT DOMAIN 1..64
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 42..44
FT /note="Cell attachment site; atypical (VGD)"
FT DISULFID 6..29
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 7
FT /note="Interchain (with C-8 in VLO5B)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 12
FT /note="Interchain (with C-13 in VLO5B)"
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; 7005 MW; 8640F0F3DA3368F3 CRC64;
NSGNPCCDPV TCQPRRGEHC VSGKCCRNCK FLRAGTVCKR AVGDDMDDYC TGISSDCPRN
PYKD
