ID   VM2DI_GLOHA             Reviewed;         477 AA.
AC   Q1PBD1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 70.
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;
DE     AltName: Full=Disintegrin brevicaudin-1b;
DE   Flags: Precursor;
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 [MRNA].
RC   TISSUE=Venom gland;
RA   Zhang S.-T., Guo A.-G.;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: [Snake venom metalloproteinase]: Impairs hemostasis in the
CC       envenomed animal. {ECO:0000250}.
CC   -!- FUNCTION: [Disintegrin halystatin]: 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: 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   -!- CAUTION: The disintegrin is also encoded by another precursor (AC
CC       Q90220). {ECO:0000305}.
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DR   EMBL; DQ457057; ABE73077.1; -; mRNA.
DR   AlphaFoldDB; Q1PBD1; -.
DR   SMR; Q1PBD1; -.
DR   MEROPS; M12.326; -.
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:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
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; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 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.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion impairing toxin; Collagen degradation;
KW   Disulfide bond; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW   Metalloprotease; Platelet aggregation inhibiting toxin; Protease; Secreted;
KW   Signal; Toxin; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..186
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000319488"
FT   CHAIN           187..388
FT                   /note="Snake venom metalloproteinase"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000319489"
FT   PROPEP          389..404
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000424448"
FT   CHAIN           405..477
FT                   /note="Disintegrin halystatin"
FT                   /id="PRO_0000319490"
FT   DOMAIN          192..388
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          396..477
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           455..457
FT                   /note="Cell attachment site"
FT   ACT_SITE        329
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         195
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         279
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         328
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         332
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         338
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         383
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         386
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        303..383
FT                   /evidence="ECO:0000250"
FT   DISULFID        343..367
FT                   /evidence="ECO:0000250"
FT   DISULFID        345..350
FT                   /evidence="ECO:0000250"
FT   DISULFID        410..425
FT                   /evidence="ECO:0000250"
FT   DISULFID        412..420
FT                   /evidence="ECO:0000250"
FT   DISULFID        419..442
FT                   /evidence="ECO:0000250"
FT   DISULFID        433..439
FT                   /evidence="ECO:0000250"
FT   DISULFID        438..463
FT                   /evidence="ECO:0000250"
FT   DISULFID        451..470
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   477 AA;  53142 MW;  295ABD3A3E6C787E CRC64;
     MIQVLLVIIC LAVPYQGSSI ILESGNVNDY EVVYPRKVTA LPKGAVQPKY EDAMQYELKV
     NGEPVVLHLE KNKGLFSKDY IETHYSPDGR KITTNPPVED HCYYHGRIQN DADSTASISA
     CNGLKGHFKL QGETYLIEPL KLSNSEAHAV YKYEDVEKED EAPKMCGVTQ NWESYEPIKK
     ASQSNLTPAH QRYIELVIVA DHGMFTKYDS NLDTIRTWVH ELVNSINEFY RSLNIDVSLT
     ELEIWSNEDL INVQPAAPHT LDSFGKWRER DLLHRIHHDN AMLLTAIDFD EPTIGLAYVG
     TMCNPKGSTG VVQDHSTINL RVAVTMAHEI GHNLGIHHDT GSCSCGGYSC IMSPVISHEP
     SKYFSDCSYT QCWDFIMNQK PQCILNKPLR TDTVSTPVSG NELLEAGEEC DCGSPGNPCC
     DAATCKLRQG AQCAEGLCCD QCRFMKKGTV CRIARGDDMD DYCNGISAGC PRNPFHA