ID   VM2_CERSA               Reviewed;          72 AA.
AC   C0HJM5;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=Disintegrin sasaimin {ECO:0000303|PubMed:25457103};
OS   Cerrophidion sasai (Costa Rica montane pitviper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Cerrophidion.
OX   NCBI_TaxID=1200835 {ECO:0000303|PubMed:25457103};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000303|PubMed:25457103};
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)=66 nM) and collagen-induced (IC(50)=100
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=7450; 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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DR   AlphaFoldDB; C0HJM5; -.
DR   SMR; C0HJM5; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0035893; P:negative regulation of platelet aggregation in another organism; IDA:UniProtKB.
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   Secreted; Toxin.
FT   CHAIN           1..72
FT                   /note="Disintegrin sasaimin"
FT                   /evidence="ECO:0000269|PubMed:25457103"
FT                   /id="PRO_0000440581"
FT   DOMAIN          1..72
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           51..53
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
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..59
FT                   /evidence="ECO:0000250|UniProtKB:P21859"
FT   DISULFID        47..66
FT                   /evidence="ECO:0000250|UniProtKB:P21859,
FT                   ECO:0000255|PROSITE-ProRule:PRU00068"
SQ   SEQUENCE   72 AA;  7614 MW;  C87A1E34BF2FE7BF CRC64;
     EAGEECDCGA PANPCCDAAT CKLRPGAQCA EGLCCDQCRF MKEGTVCHRA RGDDVDDYCN
     GISAGCPRNP FH