CEX1_ASPNG
ID CEX1_ASPNG Reviewed; 524 AA.
AC A0A254TZW7;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 1.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=Citrate exporter 1 {ECO:0000303|PubMed:31062025};
GN Name=cex1 {ECO:0000305}; Synonyms=cexA {ECO:0000303|PubMed:31062025};
GN ORFNames=ATCC64974_65440 {ECO:0000312|EMBL:SPB48923.1},
GN CAN33_0036340 {ECO:0000312|EMBL:TPR10838.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000312|Proteomes:UP000236662};
RN [1] {ECO:0000312|Proteomes:UP000236662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64974 / FGSC A733 / N402 {ECO:0000312|Proteomes:UP000236662};
RX PubMed=30319579; DOI=10.3389/fmicb.2018.02269;
RA Laothanachareon T., Tamayo-Ramos J.A., Nijsse B., Schaap P.J.;
RT "Forward genetics by genome sequencing uncovers the central role of the
RT Aspergillus niger goxB locus in hydrogen peroxide induced glucose oxidase
RT expression.";
RL Front. Microbiol. 9:2269-2269(2018).
RN [2] {ECO:0000312|Proteomes:UP000197666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_311 {ECO:0000312|Proteomes:UP000197666};
RA Kerrigan L., Tallon L., Sadzewicz L., Sengamalay N., Ott S., Godinez A.,
RA Nagaraj S., Vavikolanu K., Nadendla S., George J., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 64974 / FGSC A733 / N402 {ECO:0000303|PubMed:31062025};
RX PubMed=31062025; DOI=10.1093/femsle/fnz071;
RA Odoni D.I., Vazquez-Vilar M., van Gaal M.P., Schonewille T.,
RA Martins Dos Santos V.A.P., Tamayo-Ramos J.A., Suarez-Diez M., Schaap P.J.;
RT "Aspergillus niger citrate exporter revealed by comparison of two
RT alternative citrate producing conditions.";
RL FEMS Microbiol. Lett. 366:0-0(2019).
CC -!- FUNCTION: Transmembrane transporter that exports citrate across the
CC cell membrane. {ECO:0000269|PubMed:31062025}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate(in) = citrate(out); Xref=Rhea:RHEA:33183,
CC ChEBI:CHEBI:16947; Evidence={ECO:0000305|PubMed:31062025};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:31062025};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; OGUI01000010; SPB48923.1; -; Genomic_DNA.
DR EMBL; NKJJ02000012; TPR10838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A254TZW7; -.
DR VEuPathDB; FungiDB:An17g01710; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1165828; -.
DR VEuPathDB; FungiDB:ATCC64974_65440; -.
DR VEuPathDB; FungiDB:M747DRAFT_295654; -.
DR eggNOG; KOG0255; Eukaryota.
DR OrthoDB; 552415at2759; -.
DR Proteomes; UP000197666; Unassembled WGS sequence.
DR Proteomes; UP000236662; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IC:UniProtKB.
DR GO; GO:0015137; F:citrate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015746; P:citrate transport; IDA:UniProtKB.
DR GO; GO:0140115; P:export across plasma membrane; IDA:UniProtKB.
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 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..524
FT /note="Citrate exporter 1"
FT /id="PRO_0000452023"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 524 AA; 56776 MW; 26618A9C4220C61D CRC64;
MSSTTSSSRS DLEKVPVPQV TPRDSDSDKG SLSPEPSTLE AQSSEKPPHH IFTRSRKLQM
VCIVSLAAIF SPLSSNIYFP ALDDVSKSLN ISMSLATLTI TVYMIVQGLA PSFWGSMSDA
TGRRPVFIGT FIVYLVANIA LAESKNYGEL MAFRALQAAG SAATISIGAG VIGDITNSEE
RGSLVGIFGG VRMLGQGIGP VFGGIFTQYL GYRSIFWFLT IAGGVSLLSI LVLLPETLRP
IAGNGTVKLN GIHKPFIYTI TGQTGVVEGA QPEAKKTKTS WKSVFAPLTF LVEKDVFITL
FFGSIVYTVW SMVTSSTTDL FSEVYGLSSL DIGLTFLGNG FGCMSGSYLV GYLMDYNHRL
TEREYCEKHG YPAGTRVNLK SHPDFPIEVA RMRNTWWVIA IFIVTVALYG VSLRTHLAVP
IILQYFIAFC STGLFTINSA LVIDLYPGAS ASATAVNNLM RCLLGAGGVA IVQPILDALK
PDYTFLLLAG ITLVMTPLLY VEDRWGPGWR HARERRLKAK ANGN
