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VM212_CROSS
ID   VM212_CROSS             Reviewed;          73 AA.
AC   P0C7X7; A2CJE7; D0EUY8;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Disintegrin mojastin-2;
DE   Contains:
DE     RecName: Full=Disintegrin mojastin-1;
OS   Crotalus scutulatus scutulatus (Mojave rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8738;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=16084550; DOI=10.1016/j.taap.2005.07.004;
RA   Sanchez E.E., Galan J.A., Russell W.K., Soto J.G., Russell D.H.,
RA   Perez J.C.;
RT   "Isolation and characterization of two disintegrins inhibiting ADP-induced
RT   human platelet aggregation from the venom of Crotalus scutulatus scutulatus
RT   (Mohave Rattlesnake).";
RL   Toxicol. Appl. Pharmacol. 212:59-68(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-73, PROTEIN SEQUENCE OF 23-39 AND 52-68,
RP   FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=20598348; DOI=10.1016/j.thromres.2010.06.006;
RA   Sanchez E.E., Lucena S.E., Reyes S.R., Soto J.G., Cantu E.,
RA   Lopez-Johnston J.C., Guerrero B., Salazar A.M., Rodriguez-Acosta A.,
RA   Galan J.A., Tao W.A., Perez J.C.;
RT   "Cloning, expression, and hemostatic activities of a disintegrin, r-
RT   mojastin 1, from the mohave rattlesnake (Crotalus scutulatus scutulatus).";
RL   Thromb. Res. 126:E211-E219(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 13-73.
RC   TISSUE=Venom gland;
RX   PubMed=17112685; DOI=10.1016/j.gene.2006.09.020;
RA   Soto J.G., White S.A., Reyes S.R., Regalado R., Sanchez E.E., Perez J.C.;
RT   "Molecular evolution of PIII-SVMP and RGD disintegrin genes from the genus
RT   Crotalus.";
RL   Gene 389:66-72(2007).
CC   -!- FUNCTION: [Disintegrin mojastin-1]: Inhibits the three processes
CC       involved in platelet function (adhesion, activation and aggregation).
CC       It inhibits platelet adhesion to fibronectin with an IC(50) of 58.6 nM.
CC       It inhibits ATP release from platelet induced by ADP with an IC(50) of
CC       19.5 nM on platelet-rich plasma, probably by binding to ADP receptors
CC       (P2RY1 and P2RY12). Finally, it inhibits ADP-induced platelet
CC       aggregation with IC(50) of 44.7 nM on platelet-rich plasma and 19.3 nM
CC       on whole blood, probably by binding to alpha-IIb/beta-3 (ITGA2B/ITGB3)
CC       (PubMed:20598348). {ECO:0000269|PubMed:20598348}.
CC   -!- FUNCTION: [Disintegrin mojastin-2]: Inhibits ADP-induced platelet
CC       aggregation (IC(50) = 13.8 nM) probably by binding to alpha-IIb/beta-3
CC       (ITGA2B/ITGB3) located on the platelet surface.
CC       {ECO:0000269|PubMed:16084550}.
CC   -!- SUBUNIT: Monomer (disintegrin). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: [Disintegrin mojastin-2]: Mass=7636; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16084550};
CC   -!- MASS SPECTROMETRY: [Disintegrin mojastin-1]: Mass=7436; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16084550};
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   EMBL; GQ891042; ACX42437.1; -; mRNA.
DR   EMBL; DQ677629; ABG77588.1; -; mRNA.
DR   AlphaFoldDB; P0C7X7; -.
DR   SMR; P0C7X7; -.
DR   TopDownProteomics; P0C7X7; -.
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..73
FT                   /note="Disintegrin mojastin-2"
FT                   /id="PRO_0000345026"
FT   CHAIN           3..73
FT                   /note="Disintegrin mojastin-1"
FT                   /id="PRO_0000345027"
FT   DOMAIN          1..73
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           51..53
FT                   /note="Cell attachment site"
FT   DISULFID        6..15
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        8..16
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        21..35
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        29..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        34..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        47..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ   SEQUENCE   73 AA;  7650 MW;  4C7A27DF2326D31B CRC64;
     EAGEECDCGS PANPCCDAAT CKLRPGAQCA DGLCCDQCRF IKKGTVCRPA RGDWNDDTCT
     GQSADCPRNG LYG
 
 
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