CRNA_EMENI
ID CRNA_EMENI Reviewed; 507 AA.
AC P22152; C8VU57; Q5BEM2;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Nitrate transporter;
DE AltName: Full=Nitrate permease;
GN Name=crnA; ORFNames=AN1008;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1986367; DOI=10.1073/pnas.88.1.204;
RA Unkles S.E., Hawker K.L., Grieve C., Campbell E.I., Montague P.,
RA Kinghorn J.R.;
RT "crnA encodes a nitrate transporter in Aspergillus nidulans.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:204-208(1991).
RN [2]
RP ERRATUM OF PUBMED:1986367.
RA Unkles S.E., Hawker K.L., Grieve C., Campbell E.I., Montague P.,
RA Kinghorn J.R.;
RL Proc. Natl. Acad. Sci. U.S.A. 88:4564-4564(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Trueman L.J., Onyeocha I., Forde B.G.;
RT "Molecular biology of a family of nitrate and nitrite transporters found in
RT bacteria, fungi and plants.";
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Permease for nitrate uptake.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Subject to nitrate and nitrite induction, and nitrogen
CC metabolite repression. CrnA expression is mediated by the products of
CC nirA, areA, and niaD.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Nitrate/nitrite porter (TC 2.A.1.8) family. {ECO:0000305}.
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DR EMBL; M61125; AAA62125.1; -; Genomic_DNA.
DR EMBL; U34382; AAA76713.1; -; mRNA.
DR EMBL; AACD01000015; EAA65576.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF88345.1; -; Genomic_DNA.
DR PIR; A38560; A38560.
DR RefSeq; XP_658612.1; XM_653520.1.
DR AlphaFoldDB; P22152; -.
DR STRING; 162425.CADANIAP00001640; -.
DR TCDB; 2.A.1.8.5; the major facilitator superfamily (mfs).
DR EnsemblFungi; CBF88345; CBF88345; ANIA_01008.
DR EnsemblFungi; EAA65576; EAA65576; AN1008.2.
DR GeneID; 2876788; -.
DR KEGG; ani:AN1008.2; -.
DR VEuPathDB; FungiDB:AN1008; -.
DR eggNOG; ENOG502QPIC; Eukaryota.
DR HOGENOM; CLU_024204_1_1_1; -.
DR InParanoid; P22152; -.
DR OMA; IPCFMFA; -.
DR OrthoDB; 542533at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015513; F:high-affinity secondary active nitrite transmembrane transporter activity; IMP:AspGD.
DR GO; GO:0015112; F:nitrate transmembrane transporter activity; IDA:AspGD.
DR GO; GO:0015113; F:nitrite transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0022832; F:voltage-gated channel activity; IDA:AspGD.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0015706; P:nitrate transmembrane transport; IDA:AspGD.
DR GO; GO:0015707; P:nitrite transport; IMP:AspGD.
DR CDD; cd17341; MFS_NRT2_like; 1.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR044772; NO3_transporter.
DR InterPro; IPR004737; NO3_transporter_NarK/NarU-like.
DR PANTHER; PTHR23515; PTHR23515; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00886; 2A0108; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Membrane; Nitrate assimilation; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..507
FT /note="Nitrate transporter"
FT /id="PRO_0000084837"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..71
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..130
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..198
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..357
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411..417
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..507
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 507 AA; 54925 MW; 4A3D3FA643F16952 CRC64;
MDFAKLLVAS PEVNPNNRKA LTIPVLNPFN TYGRVFFFSW FGFMLAFLSW YAFPPLLTVT
IRDDLDMSQT QIANSNIIAL LATLLVRLIC GPLCDRFGPR LVFIGLLLVG SIPTAMAGLV
TSPQGLIALR FFIGILGGTF VPCQVWCTGF FDKSIVGTAN SLAAGLGNAG GGITYFVMPA
IFDSLIRDQG LPAHKAWRVA YIVPFILIVA AALGMLFTCD DTPTGKWSER HIWMKEDTQT
ASKGNIVDLS SGAQSSRPSG PPSIIAYAIP DVEKKGTETP LEPQSQAIGQ FDAFRANAVA
SPSRKEAFNV IFSLATMAVA VPYACSFGSE LAINSILGDY YDKNFPYMGQ TQTGKWAAMF
GFLNIVCRPA GGFLADFLYR KTNTPWAKKL LLSFLGVVMG AFMIAMGFSD PKSEATMFGL
TAGLAFFLES CNGAIFSLVP HVHPYANGIV SGMVGGFGNL GGIIFAIIFR YSHHDYARGI
WILGVISMAV FISVSWVRPV PKSQMRE