VM2_DEIAC
ID VM2_DEIAC Reviewed; 48 AA.
AC P0DM77;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 25-MAY-2022, entry version 16.
DE RecName: Full=Disintegrin accutin;
OS Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Deinagkistrodon.
OX NCBI_TaxID=36307;
RN [1]
RP PROTEIN SEQUENCE, AMINO-ACID COMPOSITION, FUNCTION, PYROGLUTAMATE FORMATION
RP AT GLN-1, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=9838213; DOI=10.1016/s0304-4165(98)00104-4;
RA Yeh C.H., Peng H.C., Yih J.B., Huang T.F.;
RT "A new short chain RGD-containing disintegrin, accutin, inhibits the common
RT pathway of human platelet aggregation.";
RL Biochim. Biophys. Acta 1425:493-504(1998).
RN [2]
RP FUNCTION, AND BIOASSAY.
RX PubMed=9787163;
RA Yeh C.H., Peng H.C., Huang T.F.;
RT "Accutin, a new disintegrin, inhibits angiogenesis in vitro and in vivo by
RT acting as integrin alphavbeta3 antagonist and inducing apoptosis.";
RL Blood 92:3268-3276(1998).
CC -!- FUNCTION: Inhibit human platelet aggregation induced by ADP, collagen,
CC thrombin or the thromboxane analog U46619 in platelet suspension with
CC IC(50) values of 66-267 nM. Acts by inhibiting fibrinogen interaction
CC with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3) (PubMed:9838213).
CC It also inhibits angiogenesis in vivo and in vitro by blocking integrin
CC alpha-V/beta-3 (ITGAV/ITGB3) of endothelial cells and by inducing
CC apoptosis (PubMed:9787163). {ECO:0000269|PubMed:9787163,
CC ECO:0000269|PubMed:9838213}.
CC -!- SUBUNIT: Monomer (disintegrin). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=5241; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9838213};
CC -!- MISCELLANEOUS: Does not inhibit the binding of specific monoclonal
CC antibodies to alpha-2/beta-1 (ITGA2/ITGB1), alpha-3/beta-1
CC (ITGA3/ITGB1), and alpha-5/beta-1 (ITGA5/ITGB1) integrins.
CC {ECO:0000305|PubMed:9787163}.
CC -!- MISCELLANEOUS: The disintegrin belongs to the short disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIa sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: Lys-Phe-Leu-Lys residues at positions 15-18 are predicted by
CC comparison with orthologs and according to the data of amino acid
CC composition. Pyroglutamate residue at position 1 has been predicted by
CC comparison with orthologs and because the pyroglutamate aminopeptidase
CC was used to allow sequencing. It is noteworthy that the theoritical
CC mass of the peptide does not correspond to the measured mass of 5241
CC Da. {ECO:0000305}.
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DR AlphaFoldDB; P0DM77; -.
DR SMR; P0DM77; -.
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; 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; 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 Pyrrolidone carboxylic acid; Secreted; Toxin.
FT CHAIN 1..48
FT /note="Disintegrin accutin"
FT /id="PRO_0000424449"
FT DOMAIN 1..48
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 27..29
FT /note="Cell attachment site"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:9838213"
FT DISULFID 5..11
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 10..35
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 23..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT UNSURE 1
FT UNSURE 15..18
SQ SEQUENCE 48 AA; 5333 MW; A30A879929F0148F CRC64;
QGAQCTAGPC CWPCKFLKEG TICRRARGDD LDDYCNGISA DCPRNPYY
