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MOKI_MONPI
ID   MOKI_MONPI              Reviewed;         543 AA.
AC   Q3S2U5;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Efflux pump mokI {ECO:0000303|PubMed:18578535};
DE   AltName: Full=Monacolin K biosynthesis protein I {ECO:0000303|PubMed:18578535};
GN   Name=mokI {ECO:0000303|PubMed:18578535};
OS   Monascus pilosus (Red mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Monascus.
OX   NCBI_TaxID=89488 {ECO:0000312|EMBL:ABA02247.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=18578535; DOI=10.1021/jf800595k;
RA   Chen Y.P., Tseng C.P., Liaw L.L., Wang C.L., Chen I.C., Wu W.J., Wu M.D.,
RA   Yuan G.F.;
RT   "Cloning and characterization of monacolin K biosynthetic gene cluster from
RT   Monascus pilosus.";
RL   J. Agric. Food Chem. 56:5639-5646(2008).
RN   [2]
RP   INDUCTION.
RX   PubMed=19968298; DOI=10.1021/jf903139x;
RA   Chen Y.-P., Yuan G.-F., Hsieh S.-Y., Lin Y.-S., Wang W.-Y., Liaw L.-L.,
RA   Tseng C.-P.;
RT   "Identification of the mokH gene encoding transcription factor for the
RT   upregulation of monacolin K biosynthesis in Monascus pilosus.";
RL   J. Agric. Food Chem. 58:287-293(2010).
RN   [3]
RP   BIOTECHNOLOGY.
RX   PubMed=21821946; DOI=10.1271/bbb.110195;
RA   Hong S.Y., Oh J.H., Lee I.;
RT   "Simultaneous enrichment of deglycosylated ginsenosides and monacolin K in
RT   red ginseng by fermentation with Monascus pilosus.";
RL   Biosci. Biotechnol. Biochem. 75:1490-1495(2011).
CC   -!- FUNCTION: Efflux pump; part of the gene cluster that mediates the
CC       biosynthesis of monakolin K, also known as lovastatin, and which acts
CC       as a potent competitive inhibitor of HMG-CoA reductase
CC       (PubMed:18578535, PubMed:19968298). {ECO:0000303|PubMed:18578535,
CC       ECO:0000303|PubMed:19968298}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is controlled by the monacolin K cluster
CC       transcription regulator mokH (PubMed:19968298).
CC       {ECO:0000269|PubMed:19968298}.
CC   -!- BIOTECHNOLOGY: Monacoline K acts as an inhibitor of HMG-CoA reductase
CC       involved in cholesterogenesis (PubMed:21821946). Its
CC       hypocholesterolemic activity might be useful for lowering cholesterol
CC       levels in the blood and reduce artherosclerosis and coronary heart
CC       disease (PubMed:21821946). {ECO:0000269|PubMed:21821946}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC       family. {ECO:0000305}.
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DR   EMBL; DQ176595; ABA02247.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3S2U5; -.
DR   SMR; Q3S2U5; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; -; 2.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 2.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..543
FT                   /note="Efflux pump mokI"
FT                   /id="PRO_0000436293"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        364..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        394..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        428..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        509..529
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   543 AA;  57408 MW;  DC8667750D18C61D CRC64;
     MASHQSEKEK PQSCTTEVQV SHVTGLKLGL VVTSVTLVVF LMLLDMSIIV TAIPHITAQF
     HSLGDVGWYG SAYLLSSCAL QPLAGKLYTL LTLKYTFLAF LGVFEVGSAL CGAARCSTML
     IVGRAVAGMG GSGLTNGAIT ILASAAPKQQ QPLLIGIMMG LSQIAIVCGP LLGGAFTQHA
     SWRWCFYINL PVGALAAILL LAIHIPKSVP TSDCTMPAPR AVGVRVILSQ LDLLGFVLFA
     AFAVMISLAL EWGGSDYMWD SSVIIGLFCG AGISLVVFGF WERYVGNSMA MIPFSVASRR
     QVWCSCLFLG FFSGALLTFS YYLPIYFQAV KDVSPTMSGV YMLPGIGGQI VMAIVSGAII
     GKTGYYIPWA LASGIIVSIS AGLVSTFQPH TSIAAWVMYQ FMGGFGRGCG MQTPIIAIQH
     ALPPQMSALG ISLAMFGQTF GGSLFLTLAK LVFSAGLDAG LREYAPAVSA EAVTAAGATG
     FRDVVPANLL SQVLLAYCKG IDHTFYLAVG ASGATFLFAW GMGQVGLIWW GEERTGFGRD
     ERV
 
 
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