URGT4_ARATH
ID URGT4_ARATH Reviewed; 337 AA.
AC Q8RWW7; Q9SVB8;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=UDP-rhamnose/UDP-galactose transporter 4 {ECO:0000312|EMBL:AKA88217.1};
DE Short=UDP-Rha/UDP-Gal transporter 4 {ECO:0000303|PubMed:25053812};
DE AltName: Full=Bi-functional UDP-rhamnose/UDP-galactose transporter {ECO:0000312|EMBL:AIJ01998.1};
DE AltName: Full=Nucleotide sugar transporter-KT 1 {ECO:0000303|PubMed:16831428};
DE Short=AtNST-KT1 {ECO:0000303|PubMed:16831428};
GN Name=URGT4 {ECO:0000312|EMBL:AIJ01998.1, ECO:0000312|EMBL:AKA88217.1};
GN Synonyms=NST-KT1 {ECO:0000303|PubMed:16831428};
GN OrderedLocusNames=At4g39390 {ECO:0000312|Araport:AT4G39390};
GN ORFNames=F23K16.20 {ECO:0000312|EMBL:CAB44674.1};
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 [MRNA], GENE FAMILY, NOMENCLATURE, SUBCELLULAR
RP LOCATION, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=25053812; DOI=10.1073/pnas.1406073111;
RA Rautengarten C., Ebert B., Moreno I., Temple H., Herter T., Link B.,
RA Donas-Cofre D., Moreno A., Saez-Aguayo S., Blanco F., Mortimer J.C.,
RA Schultink A., Reiter W.D., Dupree P., Pauly M., Heazlewood J.L.,
RA Scheller H.V., Orellana A.;
RT "The Golgi localized bifunctional UDP-rhamnose/UDP-galactose transporter
RT family of Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:11563-11568(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16831428; DOI=10.1016/j.febslet.2006.06.082;
RA Rollwitz I., Santaella M., Hille D., Fluegge U.I., Fischer K.;
RT "Characterization of AtNST-KT1, a novel UDP-galactose transporter from
RT Arabidopsis thaliana.";
RL FEBS Lett. 580:4246-4251(2006).
RN [6]
RP GENE FAMILY.
RX PubMed=25804536; DOI=10.1105/tpc.114.133827;
RA Ebert B., Rautengarten C., Guo X., Xiong G., Stonebloom S.,
RA Smith-Moritz A.M., Herter T., Chan L.J., Adams P.D., Petzold C.J.,
RA Pauly M., Willats W.G., Heazlewood J.L., Scheller H.V.;
RT "Identification and characterization of a Golgi-localized UDP-xylose
RT transporter family from Arabidopsis.";
RL Plant Cell 27:1218-1227(2015).
CC -!- FUNCTION: Nucleotide-sugar transporter that transports UDP-rhamnose or
CC UDP-galactose and UMP in a strict counter-exchange mode.
CC {ECO:0000269|PubMed:16831428, ECO:0000269|PubMed:25053812}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=37 uM for UDP-Rhamnose {ECO:0000269|PubMed:25053812};
CC KM=77 uM for UDP-Galactose {ECO:0000269|PubMed:25053812};
CC Vmax=12 nmol/sec/mg enzyme toward UDP-Rhamnose
CC {ECO:0000269|PubMed:25053812};
CC Vmax=8 nmol/sec/mg enzyme toward UDP-Galactose
CC {ECO:0000269|PubMed:25053812};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:16831428, ECO:0000269|PubMed:25053812}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8RWW7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16831428}.
CC -!- SIMILARITY: Belongs to the TPT transporter family. TPT (TC 2.A.7.9)
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB44674.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80602.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KJ667160; AIJ01998.1; -; mRNA.
DR EMBL; KP872771; AKA88217.1; -; mRNA.
DR EMBL; AL078620; CAB44674.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161595; CAB80602.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE87066.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87067.1; -; Genomic_DNA.
DR EMBL; AY091057; AAM13878.1; -; mRNA.
DR EMBL; AY142535; AAN13117.1; -; mRNA.
DR PIR; T09355; T09355.
DR RefSeq; NP_568059.1; NM_120099.4. [Q8RWW7-1]
DR RefSeq; NP_849527.1; NM_179196.2. [Q8RWW7-1]
DR AlphaFoldDB; Q8RWW7; -.
DR SMR; Q8RWW7; -.
DR STRING; 3702.AT4G39390.1; -.
DR iPTMnet; Q8RWW7; -.
DR PaxDb; Q8RWW7; -.
DR PRIDE; Q8RWW7; -.
DR ProteomicsDB; 228632; -. [Q8RWW7-1]
DR EnsemblPlants; AT4G39390.1; AT4G39390.1; AT4G39390. [Q8RWW7-1]
DR EnsemblPlants; AT4G39390.2; AT4G39390.2; AT4G39390. [Q8RWW7-1]
DR GeneID; 830094; -.
DR Gramene; AT4G39390.1; AT4G39390.1; AT4G39390. [Q8RWW7-1]
DR Gramene; AT4G39390.2; AT4G39390.2; AT4G39390. [Q8RWW7-1]
DR KEGG; ath:AT4G39390; -.
DR Araport; AT4G39390; -.
DR TAIR; locus:2122467; AT4G39390.
DR eggNOG; KOG1441; Eukaryota.
DR InParanoid; Q8RWW7; -.
DR OMA; ERHNGGS; -.
DR OrthoDB; 938634at2759; -.
DR PhylomeDB; Q8RWW7; -.
DR PRO; PR:Q8RWW7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8RWW7; baseline and differential.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015297; F:antiporter activity; IDA:UniProtKB.
DR GO; GO:0005338; F:nucleotide-sugar transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0022857; F:transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0005459; F:UDP-galactose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0015780; P:nucleotide-sugar transmembrane transport; IDA:TAIR.
DR GO; GO:0072334; P:UDP-galactose transmembrane transport; IDA:UniProtKB.
DR InterPro; IPR004853; Sugar_P_trans_dom.
DR Pfam; PF03151; TPT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiport; Golgi apparatus; Membrane; Phosphoprotein;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..337
FT /note="UDP-rhamnose/UDP-galactose transporter 4"
FT /id="PRO_0000439522"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 307..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FDZ5"
SQ SEQUENCE 337 AA; 37125 MW; 46CCC13CB883F9A3 CRC64;
MFKKMSATTS KTDQKAALDI ASWLFNVVTS VGIILVNKAL MATYGFSFAT TLTGLHFGTT
TLLTTFLTWL GYIQPSQLPW PDLLKFVLFA NFSIVGMNVS LMWNSVGFYQ IAKLSMIPVS
CLLEVMLDNV RYSRDTKLSI LLVLAGVAVC TVTDVSVNLN GFLAAAIAVW STALQQYYVH
YLQRKYSLGS FNLLAHTAPV QAASLLLVGP FLDYWLTNQR VDAYNFSFVS LFFLILSCSI
AVGTNLSQFI CIGRFTAVSF QVLGHMKTIL VLVLGFTFFG KEGLNLQVVL GMLIAILGMI
WYGNASSKPG GKERRSLSIP ITKSQKLSET NESDEKV
