CEX1_YARLI
ID CEX1_YARLI Reviewed; 673 AA.
AC Q6C8F0;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Citrate exporter 1 {ECO:0000303|PubMed:32990722};
GN Name=CEX1 {ECO:0000303|PubMed:32990722};
GN ORFNames=YALI0_D20196g {ECO:0000312|EMBL:CAG81254.1};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591 {ECO:0000312|Proteomes:UP000001300};
RN [1] {ECO:0000312|Proteomes:UP000001300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150 {ECO:0000312|Proteomes:UP000001300};
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 3286;
RX PubMed=32990722; DOI=10.1093/femsyr/foaa055;
RA Erian A.M., Egermeier M., Rassinger A., Marx H., Sauer M.;
RT "Identification of the citrate exporter Cex1 of Yarrowia lipolytica.";
RL FEMS Yeast Res. 0:0-0(2020).
CC -!- FUNCTION: Transmembrane transporter that exports citrate across the
CC cell membrane. {ECO:0000269|PubMed:32990722}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate(in) = citrate(out); Xref=Rhea:RHEA:33183,
CC ChEBI:CHEBI:16947; Evidence={ECO:0000305|PubMed:32990722};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32990722};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Abolishes citrate export.
CC {ECO:0000269|PubMed:32990722}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; CR382130; CAG81254.1; -; Genomic_DNA.
DR RefSeq; XP_503062.1; XM_503062.1.
DR AlphaFoldDB; Q6C8F0; -.
DR SMR; Q6C8F0; -.
DR STRING; 284591.Q6C8F0; -.
DR EnsemblFungi; CAG81254; CAG81254; YALI0_D20196g.
DR GeneID; 2911201; -.
DR KEGG; yli:YALI0D20196g; -.
DR VEuPathDB; FungiDB:YALI0_D20196g; -.
DR HOGENOM; CLU_000960_22_0_1; -.
DR InParanoid; Q6C8F0; -.
DR OMA; QNFFFGM; -.
DR Proteomes; UP000001300; Chromosome D.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0015137; F:citrate transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015746; P:citrate transport; IMP:UniProtKB.
DR GO; GO:0140115; P:export across plasma membrane; IMP:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
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 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..673
FT /note="Citrate exporter 1"
FT /id="PRO_0000452024"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 673 AA; 73132 MW; 71E2552C062A2032 CRC64;
MFNLNTKSSK EPEVTEVAVD STPSSPVTRE SSPESSPDNS AVDLEKGKKS KFEMHDQTNL
LPRSQLFLVF GAMAFCMLVS FMDQNGISVA LPDIAKDLNA TDTISWAGTS GLIANTVFQV
LYGRLSDIFG RKLVFMIVVC TLVCADIGCA CAQTSTQLYI FRAFSGIANG GMSCLTMIVV
SDIVTLKERG KYQGILGACV GLGNTIGPFL GAAFTENVSW RAIFYLLAPM GGLCAVVIFF
ILPSKKPQGS AIQKAKAIDY PGLFCSSVAL VFLLVPIAGG GSYYEWDSPM VISMLCIGGV
FFIAFFVIEG FFAKLPMMPL RIFGTKALFA LMMHSVLLGI AYYGDLYYLP MYMRNIRGWS
SMKAAGMSCA LVTTQAVTTV ISGQYLSRMG RYLEVIYFGF GIWTVGAIMK CFWKRDSNMA
LLIFSLLFEG AGVGCCFQPT LVAAQALSRK EDRSVVISSR NFLRSFGGAV GLAVCSAILA
NSLKADLKTK NLPSELYELI VKAPFSLPDL SHYPEYRDQV LDAYMNGSHT VFVFLCPIVG
ACLLVTVFVK DHGLQTHEKK AAEAKTVEDK DKDESGTDCE DMTKGEVLVS EKEGKLSRNS
SSQSMHFGDH TAVNTPAPTG YNTPVVGTLC HNSPNFPPMD HNDVITPLED FDESPLPPHS
PNSSGKRVTI QEE
