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FLR2_CANGA
ID   FLR2_CANGA              Reviewed;         589 AA.
AC   Q6FRT5;
DT   28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Multidrug transporter FLR2 {ECO:0000303|PubMed:28066366};
DE   AltName: Full=Drug:H(+) antiporter FLR2 {ECO:0000303|PubMed:28066366};
DE            Short=DHA FLR2 {ECO:0000303|PubMed:28066366};
DE   AltName: Full=Flucytosine exporter FLR2 {ECO:0000303|PubMed:28066366};
GN   Name=FLR2 {ECO:0000303|PubMed:28066366}; OrderedLocusNames=CAGL0H06039g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
RN   [2]
RP   DISRUPTION PHENOTYPE, FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=28066366; DOI=10.3389/fmicb.2016.02045;
RA   Pais P., Pires C., Costa C., Okamoto M., Chibana H., Teixeira M.C.;
RT   "Membrane Proteomics analysis of the Candida glabrata response to 5-
RT   flucytosine: unveiling the role and regulation of the drug efflux
RT   transporters CgFlr1 and CgFlr2.";
RL   Front. Microbiol. 7:2045-2045(2016).
CC   -!- FUNCTION: Multidrug transporter that confers resistance to 5-
CC       flucytosine (5-FC) and clotrimazole (PubMed:28066366). Further confers
CC       azole drug resistance (PubMed:28066366). Plays direct roles in
CC       extrusion of 5-flucytosine and clotrimazole (PubMed:28066366).
CC       {ECO:0000269|PubMed:28066366}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28066366};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is regulated by the transcription factors AP1 and
CC       PDR1 (PubMed:28066366). {ECO:0000269|PubMed:28066366}.
CC   -!- DISRUPTION PHENOTYPE: Increases the intracellular accumulation of 5-
CC       flucytosine and clotrimazole (PubMed:28066366).
CC       {ECO:0000269|PubMed:28066366}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR380954; CAG59992.1; -; Genomic_DNA.
DR   RefSeq; XP_447059.1; XM_447059.1.
DR   AlphaFoldDB; Q6FRT5; -.
DR   STRING; 5478.XP_447059.1; -.
DR   EnsemblFungi; CAG59992; CAG59992; CAGL0H06039g.
DR   GeneID; 2888685; -.
DR   KEGG; cgr:CAGL0H06039g; -.
DR   CGD; CAL0130474; FLR2.
DR   VEuPathDB; FungiDB:CAGL0H06039g; -.
DR   eggNOG; KOG0255; Eukaryota.
DR   HOGENOM; CLU_008455_11_1_1; -.
DR   InParanoid; Q6FRT5; -.
DR   OMA; RDYMIAI; -.
DR   Proteomes; UP000002428; Chromosome H.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR   GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IMP:CGD.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR004734; Multidrug-R.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00880; 2_A_01_02; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..589
FT                   /note="Multidrug transporter FLR2"
FT                   /id="PRO_0000443412"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        301..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        455..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        480..500
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        516..536
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        551..571
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          50..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   589 AA;  65989 MW;  4CBCC6ED9F5618B3 CRC64;
     MYIGAFQDTL FVDMLEYFGW VTVGKEYLDI YRPNGVPVAP NAVAASISGK EEMKQDNQTS
     TDSMSTSTQQ ETDASNEDIE RAMDTDNGLD KAMSGGQGVF GTEEDDSSTK DASKPEEADP
     FLVEFLGEDD PRKPWNWSFS KKTFVIVQLM VLTCINYMGS SIYTPGQEQI QHEFHVGHVV
     GTLNLSMYVL GYAIGPIIFS PLSEVSSIGR MPLYLWTFIL FTILQVACAL VRNIAGLVIL
     RFITGILCSP VLATGGASVG DVCFPRYVPR FLGAWAVGAV AAPVMAPILG AAMVVAKDWR
     WIFWLMLFMC GATLLSIIFF FPETSHECIL HRRAKRLRKL TGDDRYYTKK EKQEEALPVS
     VFIKNTLWRP IKMIALEPII LAFDVYIALC YGAFYLFFEA FPIVFAGIYH FTLVEVGLAF
     LGFCVGCVFA YTALIIFQEK VIRKKFLEGK FRPELFLILA MCLGWCLPFS LFFFGWTARI
     HWILPIIAEL FFVLSVFNLF QATFSYLAVC YPEYVASVFA GNGLCRGAFA AAFPLFGKAM
     YDRLSTKKYP VAWGSTLIGF ITVVLSLIPF VLYKYGPALR ARSRFSPDS
 
 
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