VM2IC_CROAT
ID VM2IC_CROAT Reviewed; 72 AA.
AC P68520; P31980;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Disintegrin crotatroxin {ECO:0000303|PubMed:8419314};
DE AltName: Full=Platelet aggregation activation inhibitor;
DE Contains:
DE RecName: Full=Disintegrin crotatroxin-2 {ECO:0000303|PubMed:18387648};
DE Contains:
DE RecName: Full=Disintegrin crotatroxin-4 {ECO:0000305};
DE Contains:
DE RecName: Full=Disintegrin crotatroxin-5 {ECO:0000305};
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 PROTEIN SEQUENCE (DISINTEGRIN CROTATROXIN), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Venom;
RX PubMed=8419314; DOI=10.1016/s0021-9258(18)54041-2;
RA Scarborough R.M., Rose J.W., Naughton M.A., Phillips D.R., Nannizzi L.,
RA Arfsten A., Campbell A.M., Charo I.F.;
RT "Characterization of the integrin specificities of disintegrins isolated
RT from American pit viper venoms.";
RL J. Biol. Chem. 268:1058-1065(1993).
RN [2]
RP PROTEIN SEQUENCE OF 2-72 (DISINTEGRIN CROTATROXIN-2), FUNCTION, MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=18387648; DOI=10.1016/j.toxicon.2008.02.004;
RA Galan J.A., Sanchez E.E., Rodriguez-Acosta A., Soto J.G., Bashir S.,
RA McLane M.A., Paquette-Straub C., Perez J.C.;
RT "Inhibition of lung tumor colonization and cell migration with the
RT disintegrin crotatroxin 2 isolated from the venom of Crotalus atrox.";
RL Toxicon 51:1186-1196(2008).
RN [3]
RP PROTEIN SEQUENCE OF 1-67 (DISINTEGRIN CROTATROXIN), PROTEIN SEQUENCE OF
RP 2-67 (DISINTEGRIN CROTATROXIN-2), PROTEIN SEQUENCE OF 4-67 (DISINTEGRIN
RP CROTATROXIN-4), PROTEIN SEQUENCE OF 5-67 (DISINTEGRIN CROTATROXIN-5), MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=19371136; DOI=10.1021/pr900249q;
RA Calvete J.J., Fasoli E., Sanz L., Boschetti E., Righetti P.G.;
RT "Exploring the venom proteome of the western diamondback rattlesnake,
RT Crotalus atrox, via snake venomics and combinatorial peptide ligand library
RT approaches.";
RL J. Proteome Res. 8:3055-3067(2009).
CC -!- FUNCTION: [Disintegrin crotatroxin]: Inhibits fibrinogen interaction
CC with platelets. Acts by binding to the alpha-IIb/beta-3 (ITGA2B/ITGB3)
CC on the platelet surface and inhibits aggregation induced by ADP,
CC thrombin, platelet-activating factor and collagen.
CC -!- FUNCTION: [Disintegrin crotatroxin-2]: Inhibits ADP-induced platelet
CC aggregation (IC(50) = 17.5nM), cancer cell migration in vitro, and
CC experimental lung tumor colonization of cancer cells.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18387648,
CC ECO:0000269|PubMed:19371136, ECO:0000269|PubMed:8419314}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:18387648, ECO:0000305|PubMed:19371136,
CC ECO:0000305|PubMed:8419314}.
CC -!- MASS SPECTROMETRY: [Disintegrin crotatroxin]: Mass=7505.4;
CC Method=Unknown; Note=Average mass.;
CC Evidence={ECO:0000269|PubMed:19371136};
CC -!- MASS SPECTROMETRY: [Disintegrin crotatroxin-2]: Mass=7384;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:18387648};
CC -!- MASS SPECTROMETRY: [Disintegrin crotatroxin-2]: Mass=7434.1;
CC Method=Unknown; Note=Average mass.;
CC Evidence={ECO:0000269|PubMed:19371136};
CC -!- MASS SPECTROMETRY: [Disintegrin crotatroxin-4]: Mass=7248.1;
CC Method=Unknown; Note=Average mass.;
CC Evidence={ECO:0000269|PubMed:19371136};
CC -!- MASS SPECTROMETRY: [Disintegrin crotatroxin-5]: Mass=7061.8;
CC Method=Unknown; Note=Average mass.;
CC Evidence={ECO:0000269|PubMed:19371136};
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 PIR; B43019; B43019.
DR AlphaFoldDB; P68520; -.
DR SMR; P68520; -.
DR BRENDA; 3.4.24.1; 1710.
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..72
FT /note="Disintegrin crotatroxin"
FT /evidence="ECO:0000269|PubMed:19371136,
FT ECO:0000269|PubMed:8419314"
FT /id="PRO_0000101790"
FT CHAIN 2..72
FT /note="Disintegrin crotatroxin-2"
FT /evidence="ECO:0000269|PubMed:18387648,
FT ECO:0000269|PubMed:19371136"
FT /id="PRO_0000344503"
FT CHAIN 4..72
FT /note="Disintegrin crotatroxin-4"
FT /evidence="ECO:0000269|PubMed:19371136"
FT /id="PRO_0000407582"
FT CHAIN 5..70
FT /note="Disintegrin crotatroxin-5"
FT /evidence="ECO:0000269|PubMed:19371136"
FT /id="PRO_0000407583"
FT DOMAIN 1..72
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 50..52
FT /note="Cell attachment site"
FT DISULFID 5..14
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 7..15
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 20..34
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 28..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 33..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 46..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 72 AA; 7521 MW; 193E368A6737D31B CRC64;
AGEECDCGSP ANPCCDAATC KLRPGAQCAD GLCCDQCRFI KKGTVCRPAR GDWNDDTCTG
QSADCPRNGL YG
