DTR1_CANGA
ID DTR1_CANGA Reviewed; 542 AA.
AC Q6FJH4;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Multidrug transporter DTR1 {ECO:0000303|PubMed:29184852};
DE AltName: Full=Acetic acid exporter DTR1 {ECO:0000303|PubMed:29184852};
DE AltName: Full=Drug:H(+) antiporter DTR1 {ECO:0000303|PubMed:29184852};
DE Short=DHA DTR1 {ECO:0000303|PubMed:29184852};
GN Name=DTR1 {ECO:0000303|PubMed:29184852}; OrderedLocusNames=CAGL0M06281g;
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, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=29184852; DOI=10.3389/fcimb.2017.00473;
RA Romao D., Cavalheiro M., Mil-Homens D., Santos R., Pais P., Costa C.,
RA Takahashi-Nakaguchi A., Fialho A.M., Chibana H., Teixeira M.C.;
RT "A New Determinant of Candida glabrata Virulence: The Acetate Exporter
RT CgDtr1.";
RL Front. Cell. Infect. Microbiol. 7:473-473(2017).
CC -!- FUNCTION: Plasma membrane acetic acid exporter, relieving the stress
CC induced upon cells within hemocytes, and thus enabling increased
CC proliferation and virulence against Galleria mellonella larvae. Confers
CC resistance to weak acid and oxidative stress, but not to antifungal
CC drugs (PubMed:29184852). {ECO:0000269|PubMed:29184852}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29184852};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is up-regulated during internalization in
CC hemocytes and in the presence of hydrogen peroxide stress, but
CC surprisingly, down-regulated upon exposure to acetic acid
CC (PubMed:29184852). {ECO:0000269|PubMed:29184852}.
CC -!- DISRUPTION PHENOTYPE: Leads to intracellular accumulation of acetate
CC and decreases the ability to kill Galleria mellonella larvae by
CC decreasing proliferation in the host hemolymph after infection
CC (PubMed:29184852). {ECO:0000269|PubMed:29184852}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family.
CC {ECO:0000305}.
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DR EMBL; CR380959; CAG62596.1; -; Genomic_DNA.
DR RefSeq; XP_449620.1; XM_449620.1.
DR AlphaFoldDB; Q6FJH4; -.
DR STRING; 5478.XP_449620.1; -.
DR EnsemblFungi; CAG62596; CAG62596; CAGL0M06281g.
DR GeneID; 2891668; -.
DR KEGG; cgr:CAGL0M06281g; -.
DR CGD; CAL0137077; DTR1.
DR VEuPathDB; FungiDB:CAGL0M06281g; -.
DR eggNOG; KOG0255; Eukaryota.
DR HOGENOM; CLU_008455_8_7_1; -.
DR InParanoid; Q6FJH4; -.
DR OMA; GMTWCSN; -.
DR Proteomes; UP000002428; Chromosome M.
DR GO; GO:0071944; C:cell periphery; IDA:CGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005628; C:prospore membrane; IEA:EnsemblFungi.
DR GO; GO:0005275; F:amine transmembrane transporter activity; IEA:EnsemblFungi.
DR GO; GO:0030476; P:ascospore wall assembly; IEA:EnsemblFungi.
DR GO; GO:0006847; P:plasma membrane acetate transport; 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 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..542
FT /note="Multidrug transporter DTR1"
FT /id="PRO_0000443410"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 542 AA; 59751 MW; 6A163E008EEE55A0 CRC64;
MSTSSNTSGE CSPFSITDSI VVQATDDNAD KILQEVDLSD PNIDKNDTFE LRQQVSIKES
PLYYLRDIPY SAYTSFQVSL IFLIVIYNGF LGPLAGNVFI PALPLLQKEF NVSETTINAT
VSVFMATFSI SPLFWGALAD KGGRKILYII SISLMVIINI LLASVPKKIG SLIFLRIIQA
FASSSVISLG AGTVADLTPP KDRGKAMAYF MLGPNLGPIL APIIAGLILL DNNNWRWLFG
FLCIVSGLGL IMVILLLPET LRCIVGNGDR QWENWSQNEN DMSTQPVDFS SPISRWSFVS
DIGFLNPITQ DSIFKGLYPH PPKFSVWTYL RIMTFPPVIL TSIANALLFC TYYSISVTLS
HFLATEYSYS NLKIGACYVC PGVCMLLGSQ IGGHLSDSMR KSWKKENYNT EYPLEFRLIL
TVCGVLLAIG GSIGYGWCIQ FHYHISAVLV FAGLMAFGLT WCNNTIMTYL SELLSLRVSS
AIAVSSFFRN IAAAISSALI AKLCQKMGIG FCFLGLGLIN LVSLFSILVL INNRNKWVKD
SF
