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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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