NAG3_CANAL
ID NAG3_CANAL Reviewed; 561 AA.
AC A0A1D8PQG0;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Major facilitator superfamily multidrug transporter NAG3 {ECO:0000303|PubMed:12076781};
DE AltName: Full=Multidrug resistance protein 97 {ECO:0000303|PubMed:15387822};
DE AltName: Full=N-acetylglucosamine utilization protein 3 {ECO:0000303|PubMed:12076781};
DE AltName: Full=Transmembrane protein 1 {ECO:0000303|PubMed:12589826};
GN Name=NAG3 {ECO:0000303|PubMed:12076781};
GN Synonyms=MDR97 {ECO:0000303|PubMed:15387822},
GN TMP1 {ECO:0000303|PubMed:12589826}; OrderedLocusNames=CAALFM_C604610CA;
GN ORFNames=Aorf19.2158;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP IDENTIFICATION.
RX PubMed=11298769; DOI=10.1046/j.1432-1327.2001.02135.x;
RA Yamada-Okabe T., Sakamori Y., Mio T., Yamada-Okabe H.;
RT "Identification and characterization of the genes for N-acetylglucosamine
RT kinase and N-acetylglucosamine-phosphate deacetylase in the pathogenic
RT fungus Candida albicans.";
RL Eur. J. Biochem. 268:2498-2505(2001).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12076781; DOI=10.1111/j.1574-6968.2002.tb11238.x;
RA Yamada-Okabe T., Yamada-Okabe H.;
RT "Characterization of the CaNAG3, CaNAG4, and CaNAG6 genes of the pathogenic
RT fungus Candida albicans: possible involvement of these genes in the
RT susceptibilities of cytotoxic agents.";
RL FEMS Microbiol. Lett. 212:15-21(2002).
RN [6]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12589826; DOI=10.1016/s0006-291x(03)00094-9;
RA Sengupta M., Datta A.;
RT "Two membrane proteins located in the Nag regulon of Candida albicans
RT confer multidrug resistance.";
RL Biochem. Biophys. Res. Commun. 301:1099-1108(2003).
RN [7]
RP INDUCTION.
RX PubMed=15387822; DOI=10.1111/j.1365-2958.2004.04214.x;
RA Lan C.Y., Rodarte G., Murillo L.A., Jones T., Davis R.W., Dungan J.,
RA Newport G., Agabian N.;
RT "Regulatory networks affected by iron availability in Candida albicans.";
RL Mol. Microbiol. 53:1451-1469(2004).
RN [8]
RP FUNCTION.
RX PubMed=19648376; DOI=10.1128/aem.00053-09;
RA Wendland J., Schaub Y., Walther A.;
RT "N-acetylglucosamine utilization by Saccharomyces cerevisiae based on
RT expression of Candida albicans NAG genes.";
RL Appl. Environ. Microbiol. 75:5840-5845(2009).
RN [9]
RP INDUCTION.
RX PubMed=25784162; DOI=10.1111/mmi.13002;
RA Fox E.P., Bui C.K., Nett J.E., Hartooni N., Mui M.C., Andes D.R.,
RA Nobile C.J., Johnson A.D.;
RT "An expanded regulatory network temporally controls Candida albicans
RT biofilm formation.";
RL Mol. Microbiol. 96:1226-1239(2015).
RN [10]
RP INDUCTION.
RX PubMed=28607012; DOI=10.1128/aac.00436-17;
RA Li D.D., Chai D., Huang X.W., Guan S.X., Du J., Zhang H.Y., Sun Y.,
RA Jiang Y.Y.;
RT "Potent in vitro synergism of fluconazole and osthole against fluconazole-
RT resistant Candida albicans.";
RL Antimicrob. Agents Chemother. 61:0-0(2017).
CC -!- FUNCTION: MFS transporter involved in N-acetylglucosamine (GlcNAc)
CC uptake (PubMed:19648376). Confers resistance to cycloheximide, 4-
CC nitroquinoline-N-oxide, and 1,10-phenanthroline, and contributes to
CC virulence (PubMed:12076781, PubMed:12589826).
CC {ECO:0000269|PubMed:12076781, ECO:0000269|PubMed:12589826,
CC ECO:0000269|PubMed:19648376}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is induced in presence of cycloheximide, 4-
CC nitroquinoline-N-oxide, and 1,10-phenanthroline (PubMed:12589826).
CC Expression is up-regulated during biofilm formation (PubMed:25784162).
CC Expression is also increased in high-iron conditions (PubMed:15387822).
CC Expression is decreased after combined treatment with fluconazole and
CC osthole (PubMed:28607012). {ECO:0000269|PubMed:12589826,
CC ECO:0000269|PubMed:15387822, ECO:0000269|PubMed:25784162,
CC ECO:0000269|PubMed:28607012}.
CC -!- DISRUPTION PHENOTYPE: Leads to increased susceptibility to
CC cycloheximide, 4-nitroquinoline-N-oxide, and 1,10-phenanthroline, but
CC not to actinomycin D, fluconazole, ketoconazole and colchicine
CC (PubMed:12076781). Leads also to attenuated virulence in mice
CC (PubMed:12076781). {ECO:0000269|PubMed:12076781}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family.
CC Polyamines/proton antiporter (TC 2.A.1.2.16) subfamily. {ECO:0000305}.
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DR EMBL; CP017628; AOW30377.1; -; Genomic_DNA.
DR RefSeq; XP_712434.2; XM_707341.2.
DR AlphaFoldDB; A0A1D8PQG0; -.
DR GeneID; 3645969; -.
DR KEGG; cal:CAALFM_C604610CA; -.
DR CGD; CAL0000181510; NAG3.
DR VEuPathDB; FungiDB:C6_04610C_A; -.
DR eggNOG; KOG0255; Eukaryota.
DR OrthoDB; 608951at2759; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008645; P:hexose transmembrane transport; IMP:CGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
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; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Virulence.
FT CHAIN 1..561
FT /note="Major facilitator superfamily multidrug transporter
FT NAG3"
FT /id="PRO_0000445245"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 561 AA; 62604 MW; 5863F46D3A02A6BF CRC64;
MSDNTTLDNI SVNSEKVVDY TIHHDDRKEL ERLVSHNKGV EKIVSELAEG AGQLGPLEQP
YDIHKVETHP DPHTDYNDAD PWKYPIDKET KLRLVDWTEG DKHNPKNFGK GFKWLCTVLL
GMICFVVALG SAIVTGDLER PAADFGVSEE VIILASVTMF VIGFGVGPLV FAPMSEEVGR
KPIYVVTLFV AVVFIVPCGA AQNIATLLIC RLIDGTAFSA PMTLIGGSLA DIWEGPERGT
AMAVFSAAPF LGPVCGPIFG GLLCDYAPTW RWVYWTFLIV AGFFYVVFIV VVPETHHGIL
LKKRAKKLRK DTGDSRYRSF NELQIRTFAQ VAKTSLLRPF VLLSELIVFL VTMYMSVLYG
LLYMFFFAYP IVYQEGKGWS ASKTGVMFIP IGVGVIASSL AAPFFNKDYN RRAQEYRDRG
ELPPAELRLI PMMIGCWFVP AGLFAFAWSS YQRLSWAGPC FSGFAVGFGF LLLYNPANNY
IVDSYQHYAA SALAAKTFVR SIWGACVPLF TIQMYHRLGD EWATSLMAFI SLACCAIPYL
FYIFGARIRT FSKYAYAPNM D
