ID   VM2S2_GLOBR             Reviewed;         108 AA.
AC   O93516;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Zinc metalloproteinase/disintegrin;
DE   Contains:
DE     RecName: Full=Snake venom metalloproteinase;
DE              Short=SVMP;
DE              EC=3.4.24.-;
DE   Contains:
DE     RecName: Full=Disintegrin salmosin-2;
DE   Flags: Precursor; 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 metalloproteinase]: Impairs hemostasis in the
CC       envenomed animal. {ECO:0000250}.
CC   -!- FUNCTION: [Disintegrin salmosin-2]: Inhibits platelet aggregation
CC       induced by ADP, thrombin, platelet-activating factor and collagen. Acts
CC       by inhibiting fibrinogen interaction with platelet receptors
CC       GPIIb/GPIIIa (ITGA2B/ITGB3) (By similarity). {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: Monomeric (disintegrin). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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   EMBL; AF055337; AAC42597.1; -; mRNA.
DR   AlphaFoldDB; O93516; -.
DR   SMR; O93516; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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   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   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..19
FT                   /note="Snake venom metalloproteinase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000319472"
FT   PROPEP          20..35
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000319473"
FT   CHAIN           36..108
FT                   /note="Disintegrin salmosin-2"
FT                   /id="PRO_0000319474"
FT   DOMAIN          <1..19
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          27..108
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           86..88
FT                   /note="Cell attachment site; atypical (KGD)"
FT   DISULFID        41..56
FT                   /evidence="ECO:0000250"
FT   DISULFID        43..51
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..73
FT                   /evidence="ECO:0000250"
FT   DISULFID        64..70
FT                   /evidence="ECO:0000250"
FT   DISULFID        69..94
FT                   /evidence="ECO:0000250"
FT   DISULFID        82..101
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   108 AA;  11726 MW;  573F0B6918970C8C CRC64;
     NEYQTYLTDR NPQCILNEPL RTDTVSTPVS GNELLEAGKE CDCGAPANPC CDAATCKLRP
     GEQCAEGLCC DQCRFMKEGT ICQEAKGDWN DDTCTGQSAD CPRNGFYG