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VM2H2_GLOHA
ID   VM2H2_GLOHA             Reviewed;         117 AA.
AC   Q90221;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
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 halystatin-2;
DE   Flags: Precursor; Fragment;
OS   Gloydius halys (Chinese water mocassin) (Agkistrodon halys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX   NCBI_TaxID=8714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RA   Fujisawa Y., Kuroda S., Notoya K., Konishi H., Terashita Z.;
RT   "Halystatin, a novel disintegrin from agkistrodon halys, is a potent
RT   inhibitor of bone resorption and platelet aggregation.";
RL   Takeda Kenkyusho Ho 53:39-56(1994).
CC   -!- FUNCTION: [Snake venom metalloproteinase]: Impairs hemostasis in the
CC       envenomed animal. {ECO:0000250}.
CC   -!- FUNCTION: [Disintegrin halystatin-2]: Inhibits platelet aggregation and
CC       bone resorption. {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. {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; D28871; BAA06027.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q90221; -.
DR   SMR; Q90221; -.
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..44
FT                   /note="Snake venom metalloproteinase"
FT                   /id="PRO_0000424451"
FT   CHAIN           45..117
FT                   /note="Disintegrin halystatin-2"
FT                   /id="PRO_0000424452"
FT   DOMAIN          36..117
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           95..97
FT                   /note="Cell attachment site"
FT   DISULFID        50..65
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..60
FT                   /evidence="ECO:0000250"
FT   DISULFID        59..82
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..79
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..103
FT                   /evidence="ECO:0000250"
FT   DISULFID        91..110
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   117 AA;  12686 MW;  B1F9A98056BAB07B CRC64;
     SYEFSDCNEN EYQTYVTDHS PQCILNDPLR PDTVSTPVSG NELLEAGEDC DCGAPANPCC
     DAATCKLRPG AQCAEGLCCD QCRFMKEGTI CRMARGDDMD DYCNGISAGC PRNPFHA
 
 
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