UPS1_ARATH
ID UPS1_ARATH Reviewed; 390 AA.
AC Q9ZPR7; Q058M8; Q0WP08;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Ureide permease 1 {ECO:0000303|PubMed:11971139};
DE Short=AtUPS1 {ECO:0000303|PubMed:11971139};
GN Name=UPS1 {ECO:0000303|PubMed:11971139};
GN OrderedLocusNames=At2g03590 {ECO:0000312|Araport:AT2G03590};
GN ORFNames=F19B11.4 {ECO:0000312|EMBL:AAD20067.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF Clone.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION,
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=11971139; DOI=10.1105/tpc.010458;
RA Desimone M., Catoni E., Ludewig U., Hilpert M., Schneider A., Kunze R.,
RA Tegeder M., Frommer W.B., Schumacher K.;
RT "A novel superfamily of transporters for allantoin and other oxo
RT derivatives of nitrogen heterocyclic compounds in Arabidopsis.";
RL Plant Cell 14:847-856(2002).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND DEVELOPMENTAL STAGE.
RX PubMed=15308648; DOI=10.1074/jbc.m405433200;
RA Schmidt A., Su Y.H., Kunze R., Warner S., Hewitt M., Slocum R.D.,
RA Ludewig U., Frommer W.B., Desimone M.;
RT "UPS1 and UPS2 from Arabidopsis mediate high affinity transport of uracil
RT and 5-fluorouracil.";
RL J. Biol. Chem. 279:44817-44824(2004).
RN [8]
RP FUNCTION.
RX PubMed=16897711; DOI=10.1002/biot.200500034;
RA Froissard M., Belgareh-Touze N., Buisson N., Desimone M., Frommer W.B.,
RA Haguenauer-Tsapis R.;
RT "Heterologous expression of a plant uracil transporter in yeast:
RT improvement of plasma membrane targeting in mutants of the Rsp5p ubiquitin
RT protein ligase.";
RL Biotechnol. J. 1:308-320(2006).
RN [9]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16738859; DOI=10.1007/s00425-006-0315-z;
RA Schmidt A., Baumann N., Schwarzkopf A., Frommer W.B., Desimone M.;
RT "Comparative studies on Ureide Permeases in Arabidopsis thaliana and
RT analysis of two alternative splice variants of AtUPS5.";
RL Planta 224:1329-1340(2006).
CC -!- FUNCTION: Proton-coupled transporter that transports a wide spectrum of
CC oxo derivatives of heterocyclic nitrogen compounds, including
CC allantoin, uric acid and xanthine, but not adenine (PubMed:11971139,
CC PubMed:15308648). Mediates high affinity transport of uracil and 5-
CC fluorouracil (a toxic uracil analog) (PubMed:15308648,
CC PubMed:16897711). Mediates transport of free pyrimidines and may
CC function during early seedling development in salvage pathways, by the
CC utilization of pyrimidines from seed storage tissue (PubMed:15308648).
CC {ECO:0000269|PubMed:11971139, ECO:0000269|PubMed:15308648,
CC ECO:0000269|PubMed:16897711}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=52 uM for allantoin {ECO:0000269|PubMed:11971139};
CC KM=75 uM for allantoin {ECO:0000269|PubMed:15308648};
CC KM=5.9 uM for uracil {ECO:0000269|PubMed:15308648};
CC KM=7.0 uM for xanthine {ECO:0000269|PubMed:16738859};
CC pH dependence:
CC Optimum pH is 4.75. {ECO:0000269|PubMed:11971139};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flowers, roots and stems.
CC {ECO:0000269|PubMed:11971139}.
CC -!- DEVELOPMENTAL STAGE: During seedling development, expression is high at
CC 1 day after imbibition and then declines continuously to reach steady
CC levels after 5 days. {ECO:0000269|PubMed:15308648}.
CC -!- INDUCTION: By nitrogen deficiency. {ECO:0000269|PubMed:11971139}.
CC -!- SIMILARITY: Belongs to the plant ureide permease (TC 2.A.7.19) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC006836; AAD20067.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05718.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62801.1; -; Genomic_DNA.
DR EMBL; AK229277; BAF01141.1; -; mRNA.
DR EMBL; BT029190; ABJ17125.1; -; mRNA.
DR EMBL; AY085962; AAM63172.1; -; mRNA.
DR PIR; C84450; C84450.
DR RefSeq; NP_001324930.1; NM_001335192.1.
DR RefSeq; NP_565303.1; NM_126409.4.
DR AlphaFoldDB; Q9ZPR7; -.
DR BioGRID; 289; 7.
DR IntAct; Q9ZPR7; 7.
DR STRING; 3702.AT2G03590.1; -.
DR TCDB; 2.A.7.19.2; the drug/metabolite transporter (dmt) superfamily.
DR MetOSite; Q9ZPR7; -.
DR PaxDb; Q9ZPR7; -.
DR PRIDE; Q9ZPR7; -.
DR EnsemblPlants; AT2G03590.1; AT2G03590.1; AT2G03590.
DR EnsemblPlants; AT2G03590.2; AT2G03590.2; AT2G03590.
DR GeneID; 814888; -.
DR Gramene; AT2G03590.1; AT2G03590.1; AT2G03590.
DR Gramene; AT2G03590.2; AT2G03590.2; AT2G03590.
DR KEGG; ath:AT2G03590; -.
DR Araport; AT2G03590; -.
DR TAIR; locus:2044214; AT2G03590.
DR eggNOG; ENOG502QUAA; Eukaryota.
DR HOGENOM; CLU_051261_0_0_1; -.
DR InParanoid; Q9ZPR7; -.
DR OMA; LFYWDYV; -.
DR OrthoDB; 706541at2759; -.
DR PhylomeDB; Q9ZPR7; -.
DR PRO; PR:Q9ZPR7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZPR7; baseline and differential.
DR Genevisible; Q9ZPR7; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005274; F:allantoin:proton symporter activity; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015210; F:uracil transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015505; F:uracil:cation symporter activity; IBA:GO_Central.
DR GO; GO:0015720; P:allantoin transport; IDA:TAIR.
DR GO; GO:0043100; P:pyrimidine nucleobase salvage; TAS:UniProtKB.
DR GO; GO:0015857; P:uracil transport; IDA:UniProtKB.
DR InterPro; IPR030189; UPS_plant.
DR InterPro; IPR009834; Ureide_permease.
DR PANTHER; PTHR31081; PTHR31081; 1.
DR Pfam; PF07168; Ureide_permease; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Membrane; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..390
FT /note="Ureide permease 1"
FT /id="PRO_0000221645"
FT TOPO_DOM 1..9
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..78
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..136
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..261
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..333
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..390
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT BINDING 213..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 321
FT /note="N -> D (in Ref. 3; BAF01141)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 42734 MW; 5B5C2144125F7D3A CRC64;
MYMIESKGGA IACMLLALLF LGTWPAIMTL TERRGRLPQH TYLDYTLTNL LAAVIIALTL
GEIGPSRPNF FTQLSQDNWQ SVMFAMAGGI VLSLGNLATQ YAWAYVGLSV TEVITASITV
VIGTTLNYFL DDRINRAEVL FPGVACFLIA VCFGSAVHKS NAADNKTKLQ NFKSLETTSS
FEMETISASN GLTKGKAKEG TAAFLIELEK QRAIKVFGKS TIIGLVITFF AGICFSLFSP
AFNLATNDQW HTLKHGVPKL NVYTAFFYFS ISAFVVALIL NIRFLYWPIL GLPRSSFKAY
LNDWNGRGWS FLAGFLCGFG NGLQFMGGQA AGYAAADAVQ ALPLVSTFWG ILLFGEYRRS
SRKTYTLLIS MLLMFIVAVA VLMASSGHRK
