VM2MD_GLOBR
ID VM2MD_GLOBR Reviewed; 482 AA.
AC Q9PVK9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Zinc metalloproteinase/disintegrin;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase Mt-d;
DE Short=SVMP;
DE EC=3.4.24.-;
DE Contains:
DE RecName: Full=Disintegrin;
DE Flags: Precursor;
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], AND FUNCTION.
RC TISSUE=Venom gland;
RX PubMed=10406963; DOI=10.1046/j.1432-1327.1999.00525.x;
RA Jeon O.-H., Kim D.-S.;
RT "Molecular cloning and functional characterization of a snake venom
RT metalloprotease.";
RL Eur. J. Biochem. 263:526-533(1999).
CC -!- FUNCTION: [Snake venom metalloproteinase Mt-d]: This recombinant
CC protein hydrolyzes fibronectin, but has no effect on type I gelatin and
CC type I to V collagens. Selectively hydrolyzes the Aalpha-chain of
CC fibrinogen (FGA), but has no effect on fibrin.
CC {ECO:0000269|PubMed:10406963}.
CC -!- FUNCTION: [Disintegrin]: Inhibits ADP-induced platelet aggregation.
CC {ECO:0000250}.
CC -!- FUNCTION: Recombinant metalloproteinase-disintegrin Mt-d-I (393-408):
CC hydrolyzes type I gelatin, type III and V collagens, but has no effect
CC on type I, II, IV collagens and fibronectin. Selectively hydrolyzes the
CC Aalpha-chain of fibrinogen, but has no effect on fibrin. May induce
CC hemorrhage in vascular tissue. Strongly inhibits ADP-induced platelet
CC aggregation. When concentrated, Mt-d-I undergoes autoproteolytic
CC processing into metalloproteinase and disintegrin.
CC {ECO:0000269|PubMed:10406963}.
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: Homodimer; disulfide-linked (disintegrin). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: The disintegrin belongs to the dimeric disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IId sub-subfamily. {ECO:0000305}.
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DR EMBL; AF051789; AAD02654.1; -; mRNA.
DR AlphaFoldDB; Q9PVK9; -.
DR SMR; Q9PVK9; -.
DR MEROPS; M12.178; -.
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 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; Disulfide bond;
KW Fibrinogenolytic toxin; Hemostasis impairing toxin; Hydrolase;
KW Metal-binding; Metalloprotease; Platelet aggregation inhibiting toxin;
KW Protease; Secreted; Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..189
FT /evidence="ECO:0000250"
FT /id="PRO_0000340293"
FT CHAIN 190..393
FT /note="Snake venom metalloproteinase Mt-d"
FT /id="PRO_0000340294"
FT PROPEP 394..409
FT /evidence="ECO:0000250"
FT /id="PRO_0000340295"
FT CHAIN 410..482
FT /note="Disintegrin"
FT /id="PRO_0000340296"
FT DOMAIN 197..393
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 401..482
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 460..462
FT /note="Cell attachment site"
FT ACT_SITE 334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 308..388
FT /evidence="ECO:0000250"
FT DISULFID 348..372
FT /evidence="ECO:0000250"
FT DISULFID 424..447
FT /evidence="ECO:0000250"
FT DISULFID 438..444
FT /evidence="ECO:0000250"
FT DISULFID 443..468
FT /evidence="ECO:0000250"
FT DISULFID 456..475
FT /evidence="ECO:0000250"
SQ SEQUENCE 482 AA; 53410 MW; C6014BBE87BC8B15 CRC64;
MIQVLLVTIC LAAFPYQGSS MILESGNVND YEVVYPQKVP ALPKGAVPQK YEDAMQYEFK
VNGEPVVLHL EKNKGLFSKD YSETHYSPDG RKITTNPPVE DHCYYHGHIQ NDADSTASIS
ACNGLKGHFK HQGEMYLIEP LKLSDSEAHA VYKYENVEKE DEAPKMCGVT QTNWKSDEPI
KASQLVVTAE QQRFPQRYIE LVVVADHGMF TKYDSNLDTI TTWVHELVNN INEFYRSLNV
RVSLTELEIW SNQDLINVQS AAADTLEAFG DWRETDLLNR ISHDNAQLLT TIDLDGNTIG
LAHVGTMCDP KYSVGIVQDH SAINLLVAVT MAHELGHNLG MDHDGNQCHC GANSSVMGDV
LRVGVSYEFS DCNENEYQTY VTDHNPQCIL NEPLRTDTVS TPVSGNELLE AGVECDCGAP
ANPCCDAATC KLRPGAQCAE GLCCDQCRFM KEGTICRMAR GDDMDDYCNG ISAGCPRNPF
HA
