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CEX1_ASPNA
ID   CEX1_ASPNA              Reviewed;         524 AA.
AC   G3Y4N5;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2021, sequence version 2.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Citrate exporter 1 {ECO:0000303|PubMed:30553933};
GN   Name=cex1 {ECO:0000305}; Synonyms=cexA {ECO:0000303|PubMed:30553933};
GN   ORFNames=ASPNIDRAFT2_1165828 {ECO:0000305},
GN   ASPNIDRAFT_57285 {ECO:0000312|EMBL:EHA22412.1};
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS   NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=380704 {ECO:0000312|Proteomes:UP000009038};
RN   [1] {ECO:0000312|Proteomes:UP000009038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL
RC   328 / USDA 3528.7 {ECO:0000312|Proteomes:UP000009038};
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.I.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA   Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA   van Dijck P.W.M., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA   Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.J.,
RA   Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA   Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA   Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA   Martinez D., van Peij N.N.M.E., Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT   versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(2011).
RN   [2] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL
RC   328 / USDA 3528.7 {ECO:0000303|PubMed:30553933};
RX   PubMed=30553933; DOI=10.1016/j.ymben.2018.12.004;
RA   Steiger M.G., Rassinger A., Mattanovich D., Sauer M.;
RT   "Engineering of the citrate exporter protein enables high citric acid
RT   production in Aspergillus niger.";
RL   Metab. Eng. 52:224-231(2019).
RN   [3] {ECO:0000305}
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL
RC   328 / USDA 3528.7 {ECO:0000303|PubMed:32990722};
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:30553933,
CC       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:30553933,
CC         ECO:0000305|PubMed:32990722};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:30553933,
CC       ECO:0000305|PubMed:32990722}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Decreases concentration of citric acid and
CC       increases concentration of oxalic acid in growth medium.
CC       {ECO:0000269|PubMed:30553933}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EHA22412.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; ACJE01000012; EHA22412.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; G3Y4N5; -.
DR   STRING; 380704.G3Y4N5; -.
DR   EnsemblFungi; EHA22412; EHA22412; ASPNIDRAFT_57285.
DR   HOGENOM; CLU_008455_8_4_1; -.
DR   Proteomes; UP000009038; 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; IMP:UniProtKB.
DR   GO; GO:0015746; P:citrate transport; IMP:UniProtKB.
DR   GO; GO:0140115; P:export across plasma membrane; IMP: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; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..524
FT                   /note="Citrate exporter 1"
FT                   /id="PRO_0000452022"
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
 
 
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