UPS5_ARATH
ID UPS5_ARATH Reviewed; 413 AA.
AC Q93Z75; Q8LBT6; Q9FZC9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Ureide permease 5 {ECO:0000303|PubMed:11971139};
DE Short=AtUPS5 {ECO:0000303|PubMed:11971139};
GN Name=UPS5 {ECO:0000303|PubMed:11971139};
GN OrderedLocusNames=At1g26440 {ECO:0000312|Araport:AT1G26440};
GN ORFNames=T1K7.19 {ECO:0000312|EMBL:AAF98583.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 1).
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] (ISOFORM 2).
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 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 [6]
RP FUNCTION, ALTERNATIVE SPLICING, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP 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 transport
CC of uracil and 5-fluorouracil (a toxic uracil analog).
CC {ECO:0000269|PubMed:16738859}.
CC -!- FUNCTION: Proton-coupled transporter that transports a wide spectrum of
CC oxo derivatives of heterocyclic nitrogen compounds, including
CC allantoin, xanthine and uracil. {ECO:0000269|PubMed:16738859}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=35 uM for allantoin {ECO:0000269|PubMed:16738859};
CC KM=38 uM for uracil {ECO:0000269|PubMed:16738859};
CC KM=6.8 uM for xanthine {ECO:0000269|PubMed:16738859};
CC pH dependence:
CC Optimum pH is 4.7. {ECO:0000269|PubMed:16738859};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=AtUPS5l {ECO:0000303|PubMed:16738859};
CC IsoId=Q93Z75-1; Sequence=Displayed;
CC Name=2; Synonyms=AtUPS5s {ECO:0000303|PubMed:16738859};
CC IsoId=Q93Z75-2; Sequence=VSP_014327;
CC -!- TISSUE SPECIFICITY: Expressed in lateral roots, rosette leaves, stems,
CC stipules, flower stigma, pedicels and the connective tissue between
CC pollen sacks. {ECO:0000269|PubMed:16738859}.
CC -!- SIMILARITY: Belongs to the plant ureide permease (TC 2.A.7.19) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF98583.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC013427; AAF98583.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE30689.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30690.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59222.1; -; Genomic_DNA.
DR EMBL; AY058066; AAL24174.1; -; mRNA.
DR EMBL; BT003016; AAO23581.1; -; mRNA.
DR EMBL; AY087003; AAM64564.1; -; mRNA.
DR PIR; B86391; B86391.
DR RefSeq; NP_001321599.1; NM_001332712.1. [Q93Z75-2]
DR RefSeq; NP_849708.1; NM_179377.2. [Q93Z75-1]
DR RefSeq; NP_973915.1; NM_202186.3. [Q93Z75-1]
DR AlphaFoldDB; Q93Z75; -.
DR STRING; 3702.AT1G26440.2; -.
DR TCDB; 2.A.7.19.3; the drug/metabolite transporter (dmt) superfamily.
DR PaxDb; Q93Z75; -.
DR ProteomicsDB; 243192; -. [Q93Z75-1]
DR EnsemblPlants; AT1G26440.2; AT1G26440.2; AT1G26440. [Q93Z75-1]
DR EnsemblPlants; AT1G26440.3; AT1G26440.3; AT1G26440. [Q93Z75-1]
DR EnsemblPlants; AT1G26440.6; AT1G26440.6; AT1G26440. [Q93Z75-2]
DR GeneID; 839185; -.
DR Gramene; AT1G26440.2; AT1G26440.2; AT1G26440. [Q93Z75-1]
DR Gramene; AT1G26440.3; AT1G26440.3; AT1G26440. [Q93Z75-1]
DR Gramene; AT1G26440.6; AT1G26440.6; AT1G26440. [Q93Z75-2]
DR KEGG; ath:AT1G26440; -.
DR Araport; AT1G26440; -.
DR TAIR; locus:2197995; AT1G26440.
DR eggNOG; ENOG502QUAA; Eukaryota.
DR HOGENOM; CLU_051261_0_0_1; -.
DR InParanoid; Q93Z75; -.
DR OMA; VSQEEYC; -.
DR OrthoDB; 706541at2759; -.
DR PhylomeDB; Q93Z75; -.
DR PRO; PR:Q93Z75; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93Z75; baseline and differential.
DR Genevisible; Q93Z75; AT.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; IDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0005274; F:allantoin:proton symporter activity; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140318; F:protein transporter activity; IMP:TAIR.
DR GO; GO:0015210; F:uracil transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015505; F:uracil:cation symporter activity; IBA:GO_Central.
DR GO; GO:0042907; F:xanthine transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0071705; P:nitrogen compound transport; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
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 Alternative splicing; ATP-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..413
FT /note="Ureide permease 5"
FT /id="PRO_0000221649"
FT TOPO_DOM 1..18
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..149
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..278
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..352
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..413
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT BINDING 232..239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 101..135
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_014327"
FT CONFLICT 161
FT /note="M -> L (in Ref. 4; AAM64564)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="Missing (in Ref. 4; AAM64564)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 44621 MW; 74B884267A86D0F4 CRC64;
MMIAQELGIY VVESKGGAIL CLLLSLLCLG TWPALMALLE RRGRLPQHTY LDYSITNFLA
AIFIAFVFGG IGESTHEAPS FITQLTQIQD NWPSVLFAMA GGVGLSIGNL ATQYSLAFVG
LSVTEVTAAS ITVVVGTTVN YFLDNGLNRA DILFSGVGCF MVAVCLGSAV HSSNSADIKA
KLGKLSGDCE TVTPEECQRL FGVEEEEEEE KEMENVKEGS AAFLIALENK RAIKVLGKSM
VVGLGITFFA GLSFSLFSPL FNLATNDQWH TLKQGVPKLI VYTAFFYFSL SCFVIAVALN
ISFLYKPVLD SPRSSFREYL SDWNGRGWAL AAGLLCGFGN GLQFMGGQAA GYAASDAVQA
LPLVSTFWGI YLFGEYRRSS TRTYALLVGM LVMFTVAVGL LMASAGERET RFT
