UPS2_ARATH
ID UPS2_ARATH Reviewed; 398 AA.
AC Q9ZQ89;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Ureide permease 2 {ECO:0000303|PubMed:11971139};
DE Short=AtUPS2 {ECO:0000303|PubMed:11971139};
GN Name=UPS2 {ECO:0000303|PubMed:11971139};
GN OrderedLocusNames=At2g03530 {ECO:0000312|Araport:AT2G03530};
GN ORFNames=T4M8.3 {ECO:0000312|EMBL:AAD17424.1};
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 GENE FAMILY, AND NOMENCLATURE.
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 [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND
RP 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 [5]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
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. Mediates high
CC affinity transport of uracil and 5-fluorouracil (a toxic uracil
CC analog). Mediates transport of free pyrimidines and may function during
CC early seedling development in salvage pathways, by the utilization of
CC pyrimidines from seed storage tissue. {ECO:0000269|PubMed:15308648}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=26 uM for allantoin {ECO:0000269|PubMed:15308648};
CC KM=6.2 uM for uracil {ECO:0000269|PubMed:15308648};
CC KM=24 uM for xanthine {ECO:0000269|PubMed:16738859};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in root xylem, cotyledons and leaves
CC (PubMed:15308648). Expressed in leaf blades, petioles, trichomes,
CC stems, flower stigma, the upper part of pedicels, sepals, and the top
CC and bottom parts of carpels in siliques (PubMed:16738859).
CC {ECO:0000269|PubMed:15308648, ECO:0000269|PubMed:16738859}.
CC -!- DEVELOPMENTAL STAGE: During seedling development, expression is hardly
CC detected during the first 2 days after imbibition, and then increases
CC to reach a peak after 9 days. {ECO:0000269|PubMed:15308648}.
CC -!- SIMILARITY: Belongs to the plant ureide permease (TC 2.A.7.19) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD17424.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AC006284; AAD17424.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC05711.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05712.1; -; Genomic_DNA.
DR PIR; E84449; E84449.
DR RefSeq; NP_001077874.1; NM_001084405.2.
DR RefSeq; NP_178451.2; NM_126403.4.
DR AlphaFoldDB; Q9ZQ89; -.
DR STRING; 3702.AT2G03530.2; -.
DR TCDB; 2.A.7.19.4; the drug/metabolite transporter (dmt) superfamily.
DR iPTMnet; Q9ZQ89; -.
DR PaxDb; Q9ZQ89; -.
DR PRIDE; Q9ZQ89; -.
DR ProteomicsDB; 242327; -.
DR EnsemblPlants; AT2G03530.1; AT2G03530.1; AT2G03530.
DR EnsemblPlants; AT2G03530.2; AT2G03530.2; AT2G03530.
DR GeneID; 814882; -.
DR Gramene; AT2G03530.1; AT2G03530.1; AT2G03530.
DR Gramene; AT2G03530.2; AT2G03530.2; AT2G03530.
DR KEGG; ath:AT2G03530; -.
DR Araport; AT2G03530; -.
DR TAIR; locus:2063814; AT2G03530.
DR eggNOG; ENOG502QUAA; Eukaryota.
DR HOGENOM; CLU_051261_0_0_1; -.
DR InParanoid; Q9ZQ89; -.
DR OMA; GESKQNM; -.
DR PhylomeDB; Q9ZQ89; -.
DR PRO; PR:Q9ZQ89; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQ89; baseline and differential.
DR Genevisible; Q9ZQ89; 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:UniProtKB.
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:UniProtKB.
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..398
FT /note="Ureide permease 2"
FT /id="PRO_0000221646"
FT TOPO_DOM 1..10
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..81
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..139
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..272
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..341
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..398
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 176..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 221..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 398 AA; 43542 MW; 32CD4B1436BDCCA7 CRC64;
MYLVESKGGA IACMLLALLS LGTWPAVLTL LERRGRLPQH TYLDYSITNL LAAIIIAFTF
GQIGSTKPDS PNFITQLAQD NWPSVMFAMA GGIVLSLGNL STQYAWALVG LSVTEVITSS
ITVVIGSTLN YFLDDKINKA EILFPGVACF LIAVCLGSAV HRSNADDNKA KLRDFETAKQ
EASGPSTEIG TNSSKDLETN VTTKPKEGTA RFLIELENTR AIKVFGKRKI IGLAITFFAG
LCFSLFSPAF NLATNDQWNR LKQGVPKLVV YTAFFYFSVS CFIIALILNV VFLYYPVLGL
PKSSFKAYLN DWNGRYWAFL AGFLCGFGNG LQFMGGQAAG YAAADSVQAL PLVSTFWGVV
LFGEYRRSSR KTYLLLFCML FMFISAVAVL MASSGHRK
