VM2US_GLOUS
ID VM2US_GLOUS Reviewed; 478 AA.
AC Q7SZD9; Q7SZD5; Q7SZD8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Zinc metalloproteinase/disintegrin ussurin;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase ussurin;
DE Short=SVMP;
DE EC=3.4.24.-;
DE Contains:
DE RecName: Full=Disintegrin ussurin;
DE Flags: Precursor;
OS Gloydius ussuriensis (Ussuri mamushi) (Gloydius blomhoffii ussuriensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=35671;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=15969021;
RA Sun D.-J., Gu H.D., Yang C.W., Hu C.G., Yang T.-S., Yan W.Q.;
RT "Molecular cloning and sequence analysis of ussurin, a new
RT metalloproteinases/disintegrin from Gloydius ussuriensis.";
RL Sheng Wu Gong Cheng Xue Bao 19:353-357(2003).
CC -!- FUNCTION: [Snake venom metalloproteinase ussurin]: Impairs hemostasis
CC in the envenomed animal. {ECO:0000250}.
CC -!- FUNCTION: [Disintegrin ussurin]: Inhibits platelet aggregation induced
CC by ADP, thrombin, platelet-activating factor and collagen. Acts by
CC inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa
CC (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 -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIa sub-subfamily. {ECO:0000305}.
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DR EMBL; AY204245; AAP20640.1; -; mRNA.
DR EMBL; AY204246; AAP20641.1; -; mRNA.
DR EMBL; AY204249; AAP20644.1; -; mRNA.
DR AlphaFoldDB; Q7SZD9; -.
DR SMR; Q7SZD9; -.
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: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 Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease; Secreted; Signal; Toxin;
KW Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..190
FT /evidence="ECO:0000250"
FT /id="PRO_0000321886"
FT CHAIN 191..389
FT /note="Snake venom metalloproteinase ussurin"
FT /id="PRO_0000321887"
FT PROPEP 390..413
FT /evidence="ECO:0000250"
FT /id="PRO_0000321888"
FT CHAIN 414..478
FT /note="Disintegrin ussurin"
FT /id="PRO_0000321889"
FT DOMAIN 193..389
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 397..478
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 456..458
FT /note="Cell attachment site"
FT ACT_SITE 330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 304..384
FT /evidence="ECO:0000250"
FT DISULFID 344..368
FT /evidence="ECO:0000250"
FT DISULFID 346..351
FT /evidence="ECO:0000250"
FT DISULFID 420..443
FT /evidence="ECO:0000250"
FT DISULFID 434..440
FT /evidence="ECO:0000250"
FT DISULFID 439..464
FT /evidence="ECO:0000250"
FT DISULFID 452..471
FT /evidence="ECO:0000250"
SQ SEQUENCE 478 AA; 53444 MW; CD2FBC975F62A771 CRC64;
MIQVLLVTIC LAAFPYQGSS IILESGNVND YEIVYPRKVT ALPKGAVQPK YEDTMQYELK
VNGEPVVLHL EKNKGLFSKD YSETHYSPDG RKITTNPPVE DHCYYHGRIQ NDADSTASIS
ACNGLKGHFK LQGEMYLIEP LKLSDSEAHA VFKYEHIEKE DEDPKMCGVT ETNWESYEPI
KKASPLVVTT YQRYVELVVV ADHRMVTKYN GNLIIIRTWV YEIFNTINEI YQRMNIHVAL
VGLEIWSNGD KIIVQSSADV TLDLFGTWGE IDLLKRKSHD NAQLLTPTDF DGPTIGLAYV
GTMCDPKRST GVVQDFSPIN LLVAVTMAHE IGHNLGMNHD ENYCSCGGFA CIMSPVISPQ
PSKLFSYCSY IHYWTYINYR NPQCILNKPL RTDIVSTPVS GNELLEAGEE CDCDSPGNPC
CDAATCKLRP GAQCAEGLCC EQCRFMKEGT VCRIARGDDM DDYCNGISAG CPRNPFHA
