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VM2MC_GLOBR
ID   VM2MC_GLOBR             Reviewed;         476 AA.
AC   Q9YI19;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Zinc metalloproteinase/disintegrin;
DE   Contains:
DE     RecName: Full=Snake venom metalloproteinase brevilysin L6;
DE              Short=SVMP;
DE     AltName: Full=Snake venom metalloproteinase Mt-c;
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].
RC   TISSUE=Venom gland;
RA   Jeon O.H., Kim D.S.;
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 185-387, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   ACTIVITY REGULATION, AND PYROGLUTAMATE FORMATION AT GLN-185.
RC   TISSUE=Venom;
RX   PubMed=9880798; DOI=10.1093/oxfordjournals.jbchem.a022269;
RA   Terada S., Hori J., Fujimura S., Kimoto E.;
RT   "Purification and amino acid sequence of brevilysin L6, a non-hemorrhagic
RT   metalloprotease from Agkistrodon halys brevicaudus venom.";
RL   J. Biochem. 125:64-69(1999).
CC   -!- FUNCTION: [Snake venom metalloproteinase brevilysin L6]: Shows weak
CC       degradation of alpha-fibrinogen, but has no activity on beta- and
CC       gamma-chains. Digests luteinizing hormone-releasing hormone (LH-RH) and
CC       oxidized insulin at X-Leu, X-Phe, and X-Val bonds as well as X-His
CC       bond. Does not show fibrinogen-clotting activity. Does not show
CC       hemorrhagic activity. {ECO:0000269|PubMed:9880798}.
CC   -!- FUNCTION: [Disintegrin]: Inhibits ADP-induced platelet aggregation.
CC       {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   -!- ACTIVITY REGULATION: The metalloproteinase is inhibited by EDTA, o-
CC       phenanthroline, and cysteine. Glutathione does not inhibit the
CC       enzymatic activity. {ECO:0000269|PubMed:9880798}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is about 9. {ECO:0000269|PubMed:9880798};
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; AF051790; AAD02655.1; -; mRNA.
DR   PIR; A59421; A59421.
DR   AlphaFoldDB; Q9YI19; -.
DR   SMR; Q9YI19; -.
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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW   Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Pyrrolidone carboxylic acid; Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..184
FT                   /evidence="ECO:0000269|PubMed:9880798"
FT                   /id="PRO_0000424453"
FT   CHAIN           185..387
FT                   /note="Snake venom metalloproteinase brevilysin L6"
FT                   /id="PRO_0000424454"
FT   PROPEP          388..403
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000424455"
FT   CHAIN           404..476
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000424456"
FT   DOMAIN          191..387
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          395..476
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           454..456
FT                   /note="Cell attachment site"
FT   ACT_SITE        328
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         194
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         278
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         331
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         337
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         382
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         385
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         185
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:9880798"
FT   DISULFID        302..382
FT                   /evidence="ECO:0000250"
FT   DISULFID        342..366
FT                   /evidence="ECO:0000250"
FT   DISULFID        344..349
FT                   /evidence="ECO:0000250"
FT   DISULFID        418..441
FT                   /evidence="ECO:0000250"
FT   DISULFID        432..438
FT                   /evidence="ECO:0000250"
FT   DISULFID        437..462
FT                   /evidence="ECO:0000250"
FT   DISULFID        450..469
FT                   /evidence="ECO:0000250"
FT   CONFLICT        231
FT                   /note="S -> V (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        251
FT                   /note="N -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287
FT                   /note="E -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        293..295
FT                   /note="IGL -> LGI (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        329
FT                   /note="T -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   476 AA;  52802 MW;  F06B2E643D15605F CRC64;
     MIQVLLVIIC LADFPYQGTS IILESGNVND YEVVYPRKVT ALPKGAVQPK YEDAMQYEFK
     VNGEPVVLHL EKNKGLFSKG YSETHYSPDG RKITTNPPVE DHCYYHGRIQ NDADSTASIS
     ACNGLKGHFK HQGEMYLIEP LKLSDSEAHA VYKYENVEKE DEAPKMCGVT QTNWKSDEPI
     KASQQQRFPQ RYIELVVVAD HGMFTKYDSN LDTIRTWVHE LVNSINEFYR SLNIDVSLTE
     LEIWSNQDLI NVQSAAGDTL EAFGDWRETD LLNRISHDNA QLLTATELDG NTIGLAHVAS
     MCDPKRSTGV VQDHSAINLL VAVTMAHETG HNLGMNHDGN QCHCGANSCV MGDVLSEGVS
     YEFSDCSENE YQTYLTDRNP QCILNEPLRT DTVSTPVSGN ELLEAGKECD CGAPANPCCD
     AETCKLRPGQ QCAEGLCCDQ CRFMKEGTIC QEAKGDWNDD TCNGISAGCP RNGFYG
 
 
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