NCS1_ARATH
ID NCS1_ARATH Reviewed; 599 AA.
AC Q9LZD0; Q93Z26;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Purine-uracil permease NCS1 {ECO:0000305};
DE AltName: Full=Nucleobase cation symporter 1 {ECO:0000303|PubMed:22616996};
DE Short=AtNCS1 {ECO:0000303|PubMed:22616996};
DE AltName: Full=Plastidic nucleobase transporter {ECO:0000303|PubMed:22474184};
DE AltName: Full=Uracil/purine transport protein NCS1 {ECO:0000305};
GN Name=NCS1 {ECO:0000303|PubMed:22616996};
GN Synonyms=PLUTO {ECO:0000303|PubMed:22474184};
GN OrderedLocusNames=At5g03555 {ECO:0000312|Araport:AT5G03555};
GN ORFNames=F12E4.350 {ECO:0000312|EMBL:CAB83318.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-599.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-599.
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RX PubMed=22616996; DOI=10.1016/j.febslet.2012.03.058;
RA Mourad G.S., Tippmann-Crosby J., Hunt K.A., Gicheru Y., Bade K.,
RA Mansfield T.A., Schultes N.P.;
RT "Genetic and molecular characterization reveals a unique nucleobase cation
RT symporter 1 in Arabidopsis.";
RL FEBS Lett. 586:1370-1378(2012).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22474184; DOI=10.1105/tpc.112.096743;
RA Witz S., Jung B., Furst S., Mohlmann T.;
RT "De novo pyrimidine nucleotide synthesis mainly occurs outside of plastids,
RT but a previously undiscovered nucleobase importer provides substrates for
RT the essential salvage pathway in Arabidopsis.";
RL Plant Cell 24:1549-1559(2012).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF LEU-144; VAL-145; GLY-147; TRP-223; ILE-226;
RP GLU-227; PHE-341; TRP-342; THR-425; ASN-426 AND ASN-430.
RX PubMed=24621654; DOI=10.1371/journal.pone.0091343;
RA Witz S., Panwar P., Schober M., Deppe J., Pasha F.A., Lemieux M.J.,
RA Moehlmann T.;
RT "Structure-function relationship of a plant NCS1 member--homology modeling
RT and mutagenesis identified residues critical for substrate specificity of
RT PLUTO, a nucleobase transporter from Arabidopsis.";
RL PLoS ONE 9:E91343-E91343(2014).
CC -!- FUNCTION: Nucleobase-proton symporter that facilitates the uptake of
CC nucleobases in the cells. Can transport adenine, guanine and uracil
CC (PubMed:22616996, PubMed:22474184, PubMed:24621654). Contributes to
CC uracil import into plastids for plastidic uracil salvage which is
CC essential for plant growth and development (PubMed:22474184).
CC {ECO:0000269|PubMed:22474184, ECO:0000269|PubMed:22616996,
CC ECO:0000269|PubMed:24621654}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.0 uM for uracil {ECO:0000269|PubMed:22616996};
CC KM=16.4 uM for uracil {ECO:0000269|PubMed:22474184};
CC KM=7.9 uM for adenine {ECO:0000269|PubMed:22616996};
CC KM=0.4 uM for adenine {ECO:0000269|PubMed:22474184};
CC KM=6.3 uM for guanine {ECO:0000269|PubMed:22474184};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast envelope
CC {ECO:0000269|PubMed:22474184}. Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:22474184}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers,
CC siliques and seeds. {ECO:0000269|PubMed:22474184}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:22616996}.
CC -!- SIMILARITY: Belongs to the purine-cytosine permease (2.A.39) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL25608.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM67341.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL162751; CAB83318.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90625.1; -; Genomic_DNA.
DR EMBL; AY058195; AAL25608.1; ALT_INIT; mRNA.
DR EMBL; AY088516; AAM67341.1; ALT_INIT; mRNA.
DR PIR; T48383; T48383.
DR RefSeq; NP_568122.2; NM_120436.4.
DR AlphaFoldDB; Q9LZD0; -.
DR SMR; Q9LZD0; -.
DR STRING; 3702.AT5G03555.1; -.
DR TCDB; 2.A.39.3.11; the nucleobase:cation symporter-1 (ncs1) family.
DR PaxDb; Q9LZD0; -.
DR PRIDE; Q9LZD0; -.
DR ProteomicsDB; 250998; -.
DR EnsemblPlants; AT5G03555.1; AT5G03555.1; AT5G03555.
DR GeneID; 831791; -.
DR Gramene; AT5G03555.1; AT5G03555.1; AT5G03555.
DR KEGG; ath:AT5G03555; -.
DR Araport; AT5G03555; -.
DR TAIR; locus:505006580; AT5G03555.
DR eggNOG; KOG0568; Eukaryota.
DR eggNOG; KOG2466; Eukaryota.
DR HOGENOM; CLU_021555_0_1_1; -.
DR InParanoid; Q9LZD0; -.
DR OMA; GWNWRAV; -.
DR OrthoDB; 479382at2759; -.
DR PhylomeDB; Q9LZD0; -.
DR PRO; PR:Q9LZD0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZD0; baseline and differential.
DR Genevisible; Q9LZD0; AT.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0009526; C:plastid envelope; IDA:TAIR.
DR GO; GO:0015205; F:nucleobase transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015851; P:nucleobase transport; IBA:GO_Central.
DR GO; GO:0043100; P:pyrimidine nucleobase salvage; IMP:TAIR.
DR InterPro; IPR001248; Pur-cyt_permease.
DR InterPro; IPR045225; Uracil/uridine/allantoin_perm.
DR PANTHER; PTHR30618; PTHR30618; 1.
DR Pfam; PF02133; Transp_cyt_pur; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Membrane; Plastid; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..599
FT /note="Purine-uracil permease NCS1"
FT /id="PRO_0000433155"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 144
FT /note="L->A: Slightly affects uracil, guanine and adenine
FT transport activity."
FT /evidence="ECO:0000269|PubMed:24621654"
FT MUTAGEN 145
FT /note="V->A: Reduces guanine and adenine transport activity
FT 2-fold."
FT /evidence="ECO:0000269|PubMed:24621654"
FT MUTAGEN 147
FT /note="G->K: Slightly affects uracil, guanine and adenine
FT transport activity."
FT /evidence="ECO:0000269|PubMed:24621654"
FT MUTAGEN 147
FT /note="G->Q: Reduces uracil, guanine and adenine transport
FT activity 2-fold."
FT /evidence="ECO:0000269|PubMed:24621654"
FT MUTAGEN 223
FT /note="W->A: Reduces uracil, guanine and adenine transport
FT activity 2-fold."
FT /evidence="ECO:0000269|PubMed:24621654"
FT MUTAGEN 226
FT /note="I->A: Reduces uracil and guanine transport activity
FT 2-fold."
FT /evidence="ECO:0000269|PubMed:24621654"
FT MUTAGEN 227
FT /note="E->A: Reduces uracil and guanine transport activity
FT 10-fold. Reduces adenine transport activity 5-fold."
FT /evidence="ECO:0000269|PubMed:24621654"
FT MUTAGEN 227
FT /note="E->D: Reduces uracil transport activity 10-fold.
FT Reduces guanine transport activity 5-fold. Reduces adenine
FT transport activity 2-fold."
FT /evidence="ECO:0000269|PubMed:24621654"
FT MUTAGEN 227
FT /note="E->K: Reduces uracil, guanine and adenine transport
FT activity 10-fold."
FT /evidence="ECO:0000269|PubMed:24621654"
FT MUTAGEN 227
FT /note="E->Q: Reduces uracil transport activity 10-fold.
FT Reduces adenine transport activity 5-fold."
FT /evidence="ECO:0000269|PubMed:24621654"
FT MUTAGEN 341
FT /note="F->A: Reduces adenine transport activity 2-fold."
FT /evidence="ECO:0000269|PubMed:24621654"
FT MUTAGEN 342
FT /note="W->A: Reduces adenine transport activity 5-fold."
FT /evidence="ECO:0000269|PubMed:24621654"
FT MUTAGEN 425
FT /note="T->A: Slightly affects uracil, guanine and adenine
FT transport activity."
FT /evidence="ECO:0000269|PubMed:24621654"
FT MUTAGEN 426
FT /note="N->A: Reduces uracil, guanine and adenine transport
FT activity 2-fold."
FT /evidence="ECO:0000269|PubMed:24621654"
FT MUTAGEN 430
FT /note="N->A: Reduces uracil, guanine and adenine transport
FT activity 2-fold."
FT /evidence="ECO:0000269|PubMed:24621654"
SQ SEQUENCE 599 AA; 65356 MW; 881F9F31939D79BD CRC64;
MVSNCLSLSL HLNLHPHKHN RHSLSSLRSR TKAKLYQHVS FTDSSHKSSY TSCVSTFDIQ
RKSSKHYELG KHSFSPILPG DNLVLSRSGV IRPRLSAMTG SEINDHGYDE SQFDPSLTND
DLKPTTPSQR TFSWLDMSSL WIGLVVGVPT YYLAGSLVDL GMAWWQGIAT VVTANLILLV
PLVLTAQPGT LYGISFPVLA RSSFGIRGAH IPTLLRALVG CGWYGIETWI GGEAIFLLLP
GHIKKSALSH TLPWLGTSPL EFSCFIVFWL AQLCIVWRGM DGIRKLEKYS APILISLTSC
LLAWSYLKAG GFGHMLSLSS KLTSAQFWTL FFPSLTANIS FWATLALNIP DFSRFAKSQT
DQIIGQVGLP VFMGLFTFVG VAVTSSTSII FGRVISNPIE LLGQIGGLAT TLLAIVGISL
ATLTTNIAAN VVAPANALVN LNPKFFTFGR GAFLTAVLGI VFQPWRLLKS SESFVYTWLI
GYSALLGPIG GIILVDYYLI KKMKLNIGDL YSLSPSGEYY FSKGYNVAAV VALVAGIIPV
VPGFLHKISA LSKISNGFVV VYDNALFFSF IIAGFVYWII MSRLGRKQSS LSSSSHPLL
