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VM2S3_GLOBR
ID   VM2S3_GLOBR             Reviewed;         146 AA.
AC   O93515;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Zinc metalloproteinase-disintegrin salmosin-3;
DE            EC=3.4.24.-;
DE   AltName: Full=Snake venom metalloproteinase;
DE            Short=SVMP;
DE   Flags: Fragment;
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].
RC   TISSUE=Venom gland;
RX   PubMed=9856345;
RA   Park D.-S., Kang I.-C., Kim H.-D., Chung K.-H., Kim D.-S., Yun Y.-D.;
RT   "Cloning and characterization of novel disintegrins from Agkistrodon halys
RT   venom.";
RL   Mol. Cells 8:578-584(1998).
CC   -!- FUNCTION: Snake venom zinc metalloproteinase that inhibits ADP-induced
CC       platelet aggregation (probably by binding integrin alpha-IIb/beta-3
CC       (ITGA2B/ITGB3)) and degrades fibrinogen. {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 (disintegrin). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: The disintegrin domain belongs to the long disintegrin
CC       subfamily.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC       subfamily. P-IIb sub-subfamily. {ECO:0000305}.
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DR   EMBL; AF055336; AAC42596.1; -; mRNA.
DR   AlphaFoldDB; O93515; -.
DR   SMR; O93515; -.
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..146
FT                   /note="Zinc metalloproteinase-disintegrin salmosin-3"
FT                   /id="PRO_0000319477"
FT   DOMAIN          <1..57
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          65..146
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           127..129
FT                   /note="Cell attachment site"
FT   DISULFID        2..37
FT                   /evidence="ECO:0000250"
FT   DISULFID        4..9
FT                   /evidence="ECO:0000250"
FT   DISULFID        68..87
FT                   /evidence="ECO:0000255"
FT   DISULFID        79..97
FT                   /evidence="ECO:0000250"
FT   DISULFID        81..92
FT                   /evidence="ECO:0000250"
FT   DISULFID        91..114
FT                   /evidence="ECO:0000250"
FT   DISULFID        105..111
FT                   /evidence="ECO:0000250"
FT   DISULFID        110..135
FT                   /evidence="ECO:0000250"
FT   DISULFID        123..142
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   146 AA;  15620 MW;  64474D36967B9A93 CRC64;
     SCPCDANSCI MSATLSNEPS SRFSDCSFSL PSRFSDCSFN QYSSDIIHYH ECLLNEPSRT
     DIVSPPVCGN YYPEVGEDCD CGPPANCQNP CCDAATCGLT TGSQCAEGLC CDQCRLKKAG
     TICRKARGDN PDDRCTGQSG VCPRNT
 
 
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