VM2_CROSM
ID VM2_CROSM Reviewed; 71 AA.
AC C0HJM4;
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 simusmin {ECO:0000303|PubMed:25457103};
OS Crotalus simus (Central American rattlesnake) (Caudisona simus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=1043007 {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)=56 nM) and collagen-induced (IC(50)=49
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=7106; 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; C0HJM4; -.
DR SMR; C0HJM4; -.
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; 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..71
FT /note="Disintegrin simusmin"
FT /evidence="ECO:0000269|PubMed:25457103"
FT /id="PRO_0000440582"
FT DOMAIN 1..71
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 50..52
FT /note="Cell attachment site"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 5..20
FT /evidence="ECO:0000250|UniProtKB:P21859"
FT DISULFID 7..15
FT /evidence="ECO:0000250|UniProtKB:P21859"
FT DISULFID 14..37
FT /evidence="ECO:0000250|UniProtKB:P21859"
FT DISULFID 28..34
FT /evidence="ECO:0000250|UniProtKB:P21859"
FT DISULFID 33..58
FT /evidence="ECO:0000250|UniProtKB:P21859"
FT DISULFID 46..65
FT /evidence="ECO:0000250|UniProtKB:P21859,
FT ECO:0000255|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 71 AA; 7512 MW; F488757737D31B54 CRC64;
AGEECDCGSP ANPCCDAATC KLRPGAQCAD GLCCDQCRFI KKGTVCRPAR GDWNDDTCTG
QSADCPRNPF H