ID   VM2_METMX               Reviewed;          62 AA.
AC   P0DW30;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 1.
DT   03-AUG-2022, entry version 1.
DE   RecName: Full=Disintegrin atropoimin {ECO:0000303|PubMed:25457103};
DE   Flags: Fragments;
OS   Metlapilcoatlus mexicanus (Central American jumping pitviper) (Atropoides
OS   mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Metlapilcoatlus.
OX   NCBI_TaxID=2902644;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=25457103; DOI=10.1016/j.biochi.2014.10.010;
RA   Angulo Y., Castro A., Lomonte B., Rucavado A., Fernandez J., Calvete J.J.,
RA   Gutierrez J.M.;
RT   "Isolation and characterization of four medium-size disintegrins from the
RT   venoms of Central American viperid snakes of the genera Atropoides,
RT   Bothrops, Cerrophidion and Crotalus.";
RL   Biochimie 107:376-384(2014).
CC   -!- FUNCTION: Inhibits ADP- (IC(50)=63 nM) and collagen-induced (IC(50)=53
CC       nM) aggregation of human platelets. In vitro, inhibits adhesion of
CC       endothelial cells to vitronectin, type-I collagen and, to a lower
CC       degree, fibronectin and laminin. {ECO:0000269|PubMed:25457103}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P17497}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25457103}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:25457103}.
CC   -!- MASS SPECTROMETRY: Mass=7342; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:25457103};
CC   -!- MISCELLANEOUS: The disintegrin belongs to the medium disintegrin
CC       subfamily. {ECO:0000305|PubMed:25457103}.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC       subfamily. P-IIa sub-subfamily. {ECO:0000305}.
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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..62
FT                   /note="Disintegrin atropoimin"
FT                   /evidence="ECO:0000269|PubMed:25457103"
FT                   /id="PRO_0000456228"
FT   DOMAIN          2..61
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           <41..42
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000305"
FT   DISULFID        6..21
FT                   /evidence="ECO:0000250|UniProtKB:P21859"
FT   DISULFID        8..16
FT                   /evidence="ECO:0000250|UniProtKB:P21859"
FT   DISULFID        15..38
FT                   /evidence="ECO:0000250|UniProtKB:P21859"
FT   DISULFID        29..35
FT                   /evidence="ECO:0000250|UniProtKB:P21859"
FT   DISULFID        34..48
FT                   /evidence="ECO:0000250|UniProtKB:P21859"
FT   DISULFID        55..?
FT                   /evidence="ECO:0000305"
FT   NON_CONS        40..41
FT                   /evidence="ECO:0000305|PubMed:25457103"
SQ   SEQUENCE   62 AA;  6468 MW;  E75F0F87F8EBE9BD CRC64;
     EAGEECDCGT PANPCCDAAT CKLRPGAQCA EGLCCDQCRF GDWNDDTCTG QSADCPRNGL
     YG