VM2S3_GLOBR
ID VM2S3_GLOBR Reviewed; 146 AA.
AC O93515;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Zinc metalloproteinase-disintegrin salmosin-3;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Fragment;
OS Gloydius brevicaudus (Korean slamosa snake) (Agkistrodon halys
OS brevicaudus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=259325;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=9856345;
RA Park D.-S., Kang I.-C., Kim H.-D., Chung K.-H., Kim D.-S., Yun Y.-D.;
RT "Cloning and characterization of novel disintegrins from Agkistrodon halys
RT venom.";
RL Mol. Cells 8:578-584(1998).
CC -!- FUNCTION: Snake venom zinc metalloproteinase that inhibits ADP-induced
CC platelet aggregation (probably by binding integrin alpha-IIb/beta-3
CC (ITGA2B/ITGB3)) and degrades fibrinogen. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer (disintegrin). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: The disintegrin domain belongs to the long disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIb sub-subfamily. {ECO:0000305}.
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DR EMBL; AF055336; AAC42596.1; -; mRNA.
DR AlphaFoldDB; O93515; -.
DR SMR; O93515; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; 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 InterPro; IPR001590; Peptidase_M12B.
DR Pfam; PF00200; Disintegrin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion impairing toxin; Disulfide bond; Hemostasis impairing toxin;
KW Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease; Secreted; Toxin; Zinc;
KW Zymogen.
FT CHAIN <1..146
FT /note="Zinc metalloproteinase-disintegrin salmosin-3"
FT /id="PRO_0000319477"
FT DOMAIN <1..57
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 65..146
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 127..129
FT /note="Cell attachment site"
FT DISULFID 2..37
FT /evidence="ECO:0000250"
FT DISULFID 4..9
FT /evidence="ECO:0000250"
FT DISULFID 68..87
FT /evidence="ECO:0000255"
FT DISULFID 79..97
FT /evidence="ECO:0000250"
FT DISULFID 81..92
FT /evidence="ECO:0000250"
FT DISULFID 91..114
FT /evidence="ECO:0000250"
FT DISULFID 105..111
FT /evidence="ECO:0000250"
FT DISULFID 110..135
FT /evidence="ECO:0000250"
FT DISULFID 123..142
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 146 AA; 15620 MW; 64474D36967B9A93 CRC64;
SCPCDANSCI MSATLSNEPS SRFSDCSFSL PSRFSDCSFN QYSSDIIHYH ECLLNEPSRT
DIVSPPVCGN YYPEVGEDCD CGPPANCQNP CCDAATCGLT TGSQCAEGLC CDQCRLKKAG
TICRKARGDN PDDRCTGQSG VCPRNT
