SNQ2_CANGA
ID SNQ2_CANGA Reviewed; 1507 AA.
AC Q6FQN3;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=ABC multidrug transporter SNQ2 {ECO:0000303|PubMed:11257032};
GN Name=SNQ2 {ECO:0000303|PubMed:11257032}; OrderedLocusNames=CAGL0I04862g;
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 IDENTIFICATION.
RX PubMed=11257032; DOI=10.1128/aac.45.4.1174-1183.2001;
RA Sanglard D., Ischer F., Bille J.;
RT "Role of ATP-binding-cassette transporter genes in high-frequency
RT acquisition of resistance to azole antifungals in Candida glabrata.";
RL Antimicrob. Agents Chemother. 45:1174-1183(2001).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=15673750; DOI=10.1128/aac.49.2.668-679.2005;
RA Sanguinetti M., Posteraro B., Fiori B., Ranno S., Torelli R., Fadda G.;
RT "Mechanisms of azole resistance in clinical isolates of Candida glabrata
RT collected during a hospital survey of antifungal resistance.";
RL Antimicrob. Agents Chemother. 49:668-679(2005).
RN [4]
RP INDUCTION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18312269; DOI=10.1111/j.1365-2958.2008.06143.x;
RA Torelli R., Posteraro B., Ferrari S., La Sorda M., Fadda G., Sanglard D.,
RA Sanguinetti M.;
RT "The ATP-binding cassette transporter-encoding gene CgSNQ2 is contributing
RT to the CgPDR1-dependent azole resistance of Candida glabrata.";
RL Mol. Microbiol. 68:186-201(2008).
RN [5]
RP INDUCTION, AND FUNCTION.
RX PubMed=24645630; DOI=10.1080/08927014.2014.886108;
RA Fonseca E., Silva S., Rodrigues C.F., Alves C.T., Azeredo J., Henriques M.;
RT "Effects of fluconazole on Candida glabrata biofilms and its relationship
RT with ABC transporter gene expression.";
RL Biofouling 30:447-457(2014).
RN [6]
RP INDUCTION.
RX PubMed=25355935; DOI=10.1099/jmm.0.081760-0;
RA Li H., Chen Z., Zhang C., Gao Y., Zhang X., Sun S.;
RT "Resistance reversal induced by a combination of fluconazole and tacrolimus
RT (FK506) in Candida glabrata.";
RL J. Med. Microbiol. 64:44-52(2015).
RN [7]
RP INDUCTION.
RX PubMed=29464833; DOI=10.1111/myc.12756;
RA Ni Q., Wang C., Tian Y., Dong D., Jiang C., Mao E., Peng Y.;
RT "CgPDR1 gain-of-function mutations lead to azole-resistance and increased
RT adhesion in clinical Candida glabrata strains.";
RL Mycoses 61:430-440(2018).
CC -!- FUNCTION: ABC multidrug transporter involved in the response to azoles
CC such as fluconazole, itraconazole, ketoconazole and voriconazole and
CC contributes to the development of PDR1-dependent azole resistance
CC (PubMed:15673750, PubMed:18312269). Plays a role in biofilm tolerance
CC to fluconazole (PubMed:24645630). Confers also resistance to 4-
CC nitroquinoline-N-oxide (4-NQO) (PubMed:18312269).
CC {ECO:0000269|PubMed:15673750, ECO:0000269|PubMed:18312269,
CC ECO:0000269|PubMed:24645630}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is increased in clinical azole-resistant
CC isolates, displaying amounts of transcript increasing from 3.3- to
CC 44.3-fold (PubMed:15673750, PubMed:18312269, PubMed:29464833).
CC Expression is controlled by the pleiotropic drug resistance
CC transcription factor PDR1 (PubMed:18312269, PubMed:29464833).
CC Expression is increased during biofilm growth (PubMed:24645630). The
CC expression levels are significantly down-regulated after exposure to
CC the combination of fluconazole and tacrolimus (FK506)
CC (PubMed:25355935). {ECO:0000269|PubMed:15673750,
CC ECO:0000269|PubMed:18312269, ECO:0000269|PubMed:24645630,
CC ECO:0000269|PubMed:25355935, ECO:0000269|PubMed:29464833}.
CC -!- DISRUPTION PHENOTYPE: Leads to increased susceptibility to fluconazole
CC (PubMed:18312269). Leads also to increased susceptibility to 4-
CC nitroquinoline-N-oxide (4-NQO) (PubMed:18312269).
CC {ECO:0000269|PubMed:18312269}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR380955; CAG60398.1; -; Genomic_DNA.
DR RefSeq; XP_447461.1; XM_447461.1.
DR AlphaFoldDB; Q6FQN3; -.
DR SMR; Q6FQN3; -.
DR STRING; 5478.XP_447461.1; -.
DR EnsemblFungi; CAG60398; CAG60398; CAGL0I04862g.
DR GeneID; 2889250; -.
DR KEGG; cgr:CAGL0I04862g; -.
DR CGD; CAL0132132; SNQ2.
DR VEuPathDB; FungiDB:CAGL0I04862g; -.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; Q6FQN3; -.
DR OMA; MIKHHRG; -.
DR Proteomes; UP000002428; Chromosome I.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IGI:CGD.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IGI:CGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR005285; Drug-R_PDR/CDR.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010929; PDR_CDR_ABC.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
DR Pfam; PF06422; PDR_CDR; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00956; 3a01205; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1507
FT /note="ABC multidrug transporter SNQ2"
FT /id="PRO_0000445244"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 556..576
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 605..625
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 635..655
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 665..685
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1193..1213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1220..1240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1270..1290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1314..1334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1339..1359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1459..1479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 157..412
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 857..1099
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 893..900
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 659
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 878
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1507 AA; 170187 MW; AA7D82B795C4A786 CRC64;
MSSSSEISVA GSDVSFEGRL TQHGRHEETP ADQLTKILSG RSHEDADGDD AHSDNRSILS
RSRRSSTAEL SPEMVGRVQS LADVLSRHTS RSGGNIDLSQ LSESDRFDAE RIIGSFVRDA
DEQGIHLRKA GVTLEHVSAR GADSTAMEGA TFGNVLCLPY TIYKAIRDKS GSKMRTILND
VSGLARAGEM VLVLGRPGAG CSSMLKVTAG EIDQFAGGVE GEIMYDGIPQ KEMMKRYKPD
VIYNGEQDVH FPHLTVQQTL DFAIACKTPS KRVNDVSREE YIASTRDLHA TIFGLRHTYH
TKVGNDFVRG VSGGERKRVS IAEALVTKGS IYCWDNATRG LDASTALEYA KAIRITTNLL
GSTAFVTIYQ ASENIYETFD KVTVLYTGRQ IYFGPIDEAK DYFYRMGYEC PPRQVTAEFL
TALTDVNGYH KIRPGYENKV PRTAEEFERY WQESPEYRQL LIDIDQYKKE IDTEKTKEIY
DQSMQQEKSK HARKKSYYTV SFWEQIRLCT KRGFQRIYGD KAYTVITICS AIIQSLVSGS
LYYNTPSSTS GAFSRGGVLY FCLLYYSLMG LANLSFEHRP ILQKHKIYSL YHPAAEALGS
TIANFPFRMI GMTCFLIIIY FLSGLNRTAS SFFRVYLFLT MCSESINALF ELIAAGCDNI
SQANSISGIV MMSISLYSTY MIQLPSMRPW FKWISYILPI RYAFESMLLA EFHGRHMGCG
GTLVPSGPGY ENIASENQVC AFVGSKPGQS WVLGDDYLRL QFEYEYKHEW RNFGIMWCFL
LGYIALKALI TEIKRPVKGG GDALIFKKGT RKYHMKLDEE DGELHEIDTK EKFSSRSGSS
TTSEDEIFEE LESKGIFIWR NVCYTIPYDG GMRQLLDNVS GFCKPGTLTA LMGESGAGKT
TLLNTLAQRN VGIITGDMLV NGKPIDISFE RRTGYVQQQD IHISELTVRE SLQFSARMRR
AQNVPEEEKM EHVERIIKVL DMEEYADALV GDVGRGLNVE QRKKLSIGVE LVAKPDLLLF
LDEPTSGLDS QSSWAIVQLL KKLAKAGQSI LCTIHQPSAT LFEEFDRLLL LKKGGQTVYF
GDIGDNSKTL LSYFERNGAR KCSPSENPAE YILEAIGAGA TASVTEDWHQ IWKNSDEFIS
TEKEVDHLID QLSNQKTESE FGDAPTKYAT SYAYQFKWVL IRTSMSLWRN LDYIMSKMML
MTVGGLYIGF TFYDPGDSYT GLQNTLFAAF ISIILSAPAM NQIQARAIAA RELFEVRESK
SNMFHWSLLL ITQYLSEIPY HFLFSAIFFV SSYFPLRTHF QASASAVYYL NYSIMFQLYY
IGFGLCVLYM APNLQSANVI LGLCLSFLIA FCGVVQPVSL MPGFWTFMWK TSPYTYFVQN
MVGILLHNKP VICRKKELSI FDPPAGQTCQ EFTQAFLDKR GGYIANPNAT TACEYCIYEV
GDDYLKHISA SYSYLWRNFG LYWAYIGFNI CAMVAIYYIF HVRGVSFKFD RVFKLFSRIT
RRGKKSN
