ID QAY_NEUCR Reviewed; 537 AA.
AC P11636; Q7RVA0;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 27-MAR-2024, entry version 157.
DE RecName: Full=MFS-type transporter qa-x {ECO:0000303|PubMed:2525625};
DE AltName: Full=Quinate permease {ECO:0000303|PubMed:2525625};
DE AltName: Full=Quinate transporter {ECO:0000303|PubMed:2525625};
DE AltName: Full=Quinic acid degradation cluster protein y {ECO:0000303|PubMed:2525625};
GN Name=qa-y {ECO:0000303|PubMed:2525625}; ORFNames=NCU06026;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=2525625; DOI=10.1016/0022-2836(89)90438-5;
RA Geever R.F., Huiet L., Baum J.A., Tyler B.M., Patel V.B., Rutledge B.J.,
RA Case M.E., Giles N.H.;
RT "DNA sequence, organization and regulation of the qa gene cluster of
RT Neurospora crassa.";
RL J. Mol. Biol. 207:15-34(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=6458044; DOI=10.1073/pnas.78.9.5783;
RA Patel V.B., Schweizer M., Dykstra C.C., Kushner S.R., Giles N.H.;
RT "Genetic organization and transcriptional regulation in the qa gene cluster
RT of Neurospora crassa.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:5783-5787(1981).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=1533844; DOI=10.1093/genetics/130.4.729;
RA Case M.E., Geever R.F., Asch D.K.;
RT "Use of gene replacement transformation to elucidate gene function in the
RT qa gene cluster of Neurospora crassa.";
RL Genetics 130:729-736(1992).
RN [5]
RP INDUCTION.
RX PubMed=12477937; DOI=10.1073/pnas.262658899;
RA Battogtokh D., Asch D.K., Case M.E., Arnold J., Schuttler H.B.;
RT "An ensemble method for identifying regulatory circuits with special
RT reference to the qa gene cluster of Neurospora crassa.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16904-16909(2002).
RN [6]
RP INDUCTION.
RX PubMed=17597928; DOI=10.6026/97320630001390;
RA Logan D.A., Koch A.L., Dong W., Griffith J., Nilsen R., Case M.E.,
RA Schuettler H.B., Arnold J.;
RT "Genome-wide expression analysis of genetic networks in Neurospora
RT crassa.";
RL Bioinformation 1:390-395(2007).
RN [7]
RP INDUCTION.
RX PubMed=19236936; DOI=10.1016/j.fgb.2009.02.003;
RA Arnett D.R., Lorimer H.E., Asch D.K.;
RT "Catabolite repression directly affects transcription of the qa-y gene of
RT Neurospora crassa.";
RL Fungal Genet. Biol. 46:377-380(2009).
CC -!- FUNCTION: MFS-type transporter; part of the qa gene cluster that
CC mediates the catabolism of quinic acid (QA) and as such, allows the use
CC of QA as a sole carbon source (PubMed:2525625, PubMed:6458044).
CC Involved in the upatke of QA (PubMed:1533844). The qa cluster encodes 3
CC inducible enymes (qa-2, qa-3 and qa-4) catalyzing the first three
CC reactions in the catabolism of quinic acid to protocatechuic acid (also
CC known as 3,4-Dihydroxybenzoic acid) (Probable).
CC {ECO:0000269|PubMed:1533844, ECO:0000269|PubMed:2525625,
CC ECO:0000269|PubMed:6458044, ECO:0000305|PubMed:2525625}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is induced in the presence of quinic acid
CC (PubMed:6458044). The quinic acid (qa) gene cluster is subject to two
CC levels of gene control: a primary system which responds to the presence
CC of quinic acid via the qa-1S repressor protein that blocks the qa-1F
CC activator, and a secondary system which represses transcription of qa
CC genes in the presence of a preferred carbon source such as glucose
CC (PubMed:6458044, PubMed:12477937, PubMed:17597928, PubMed:19236936).
CC {ECO:0000269|PubMed:12477937, ECO:0000269|PubMed:17597928,
CC ECO:0000269|PubMed:19236936, ECO:0000269|PubMed:6458044}.
CC -!- DISRUPTION PHENOTYPE: Impairs growth on quinic acid as a sole carbon
CC source and leads to very low inducible levels of qa-2 and qa-3 enzyme
CC activities. {ECO:0000269|PubMed:1533844}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR EMBL; X14603; CAA32752.1; -; Genomic_DNA.
DR EMBL; CM002242; EAA30380.1; -; Genomic_DNA.
DR PIR; S04254; G31277.
DR RefSeq; XP_959616.1; XM_954523.2.
DR AlphaFoldDB; P11636; -.
DR SMR; P11636; -.
DR STRING; 367110.P11636; -.
DR TCDB; 2.A.1.1.7; the major facilitator superfamily (mfs).
DR GlyCosmos; P11636; 1 site, No reported glycans.
DR PaxDb; 5141-EFNCRP00000005335; -.
DR EnsemblFungi; EAA30380; EAA30380; NCU06026.
DR GeneID; 3875775; -.
DR KEGG; ncr:NCU06026; -.
DR VEuPathDB; FungiDB:NCU06026; -.
DR HOGENOM; CLU_001265_30_12_1; -.
DR InParanoid; P11636; -.
DR OMA; PADHIYM; -.
DR OrthoDB; 1354898at2759; -.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IBA:GO_Central.
DR GO; GO:0008643; P:carbohydrate transport; IBA:GO_Central.
DR GO; GO:0019630; P:quinate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd17356; MFS_HXT; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR NCBIfam; TIGR00879; SP; 1.
DR PANTHER; PTHR48022:SF34; MAJOR FACILITATOR SUPERFAMILY (MFS) PROFILE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR48022; PLASTIDIC GLUCOSE TRANSPORTER 4; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Quinate metabolism; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..537
FT /note="MFS-type transporter qa-x"
FT /id="PRO_0000050449"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..74
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..131
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..195
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..327
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..349
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..389
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..458
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 514..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 481
FT /note="E -> V (in Ref. 1; CAA32752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 60134 MW; 89D53413EFC164F3 CRC64;
MTLLALKEDR PTPKAVYNWR VYTCAAIASF ASCMIGYDSA FIGTTLALPS FTKEFDFASY
TPGALALLQS NIVSVYQAGA FFGCLFAYAT SYFLGRRKSL IAFSVVFIIG AAIMLAADGQ
GRGIDPIIAG RVLAGIGVGG ASNMVPIYIS ELAPPAVRGR LVGIYELGWQ IGGLVGFWIN
YGVNTTMAPT RSQWLIPFAV QLIPAGLLFL GSFWIPESPR WLYANGKREE AMKVLCWIRN
LEPTDRYIVQ EVSFIDADLE RYTRQVGNGF WKPFLSLKQR KVQWRFFLGG MLFFWQNGSG
INAINYYSPT VFRSIGITGT DTGFLTTGIF GVVKMVLTII WLLWLVDLVG RRRILFIGAA
GGSLCMWFIG AYIKIADPGS NKAEDAKLTS GGIAAIFFFY LWTAFYTPSW NGTPWVINSE
MFDQNTRSLG QASAAANNWF WNFIISRFTP QMFIKMEYGV YFFFASLMLL SIVFIYFFLP
ETKSIPLEAM DRLFEIKPVQ NANKNLMAEL NFDRNPEREE SSSLDDKDRV TQTENAV
//
