VM212_CROHD
ID VM212_CROHD Reviewed; 71 AA.
AC P0C7X6;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Disintegrin horridistatin-2;
DE Contains:
DE RecName: Full=Disintegrin horridistatin-1;
OS Crotalus horridus (Timber rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=35024;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX DOI=10.1139/v05-128;
RA Galan J.A., Sanchez E.E., Bashir S., Perez J.C.;
RT "Characterization and identification of disintegrins in Crotalus horridus
RT venom by liquid chromatography and tandem matrix-assisted laser desorption
RT ionization quadrupole ion trap time-of-flight (MALDI-QIT-TOF) mass
RT spectrometry.";
RL Can. J. Chem. 83:1124-1131(2005).
CC -!- FUNCTION: [Disintegrin horridistatin-1]: Inhibits ADP-induced platelet
CC aggregation (IC(50) is 16.2 nM) by binding to alpha-IIb/beta-3
CC (ITGA2B/ITGB3). {ECO:0000269|Ref.1}.
CC -!- FUNCTION: [Disintegrin horridistatin-2]: Inhibits ADP-induced platelet
CC aggregation (IC(50) is 16.2 nM) by binding to alpha-IIb/beta-3
CC (ITGA2B/ITGB3). {ECO:0000269|Ref.1}.
CC -!- SUBUNIT: Monomer (disintegrin). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: [Disintegrin horridistatin-2]: Mass=7451;
CC Method=MALDI; Evidence={ECO:0000269|Ref.1};
CC -!- MASS SPECTROMETRY: [Disintegrin horridistatin-1]: Mass=7231;
CC Method=MALDI; Evidence={ECO:0000269|Ref.1};
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 AlphaFoldDB; P0C7X6; -.
DR SMR; P0C7X6; -.
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..71
FT /note="Disintegrin horridistatin-2"
FT /id="PRO_0000345024"
FT CHAIN 1..69
FT /note="Disintegrin horridistatin-1"
FT /id="PRO_0000345025"
FT DOMAIN 1..71
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 49..51
FT /note="Cell attachment site"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 4..13
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 6..14
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 19..33
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 27..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 32..36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 45..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 71 AA; 7450 MW; BC3B66DF6237D376 CRC64;
GEECDCGSPA NPCCDAATCK LRPGAQCADG LCCDQCRFIK KGTVCRPARG DWNDDTCTGQ
SADCPRNGLY G
