URGT5_ARATH
ID URGT5_ARATH Reviewed; 335 AA.
AC Q9SZ96; Q0WV68;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=UDP-rhamnose/UDP-galactose transporter 5 {ECO:0000312|EMBL:AKA88218.1};
DE Short=UDP-Rha/UDP-Gal transporter 5 {ECO:0000303|PubMed:25053812};
DE AltName: Full=Bi-functional UDP-rhamnose/UDP-galactose transporter {ECO:0000312|EMBL:AIJ01999.1};
GN Name=URGT5 {ECO:0000312|EMBL:AIJ01999.1, ECO:0000312|EMBL:AKA88218.1};
GN OrderedLocusNames=At4g09810 {ECO:0000312|Araport:AT4G09810};
GN ORFNames=F17A8.160 {ECO:0000312|EMBL:CAB39648.1};
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 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 [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:25053812}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 uM for UDP-Rhamnose {ECO:0000269|PubMed:25053812};
CC KM=177 uM for UDP-Galactose {ECO:0000269|PubMed:25053812};
CC Vmax=4 nmol/sec/mg enzyme toward UDP-Rhamnose
CC {ECO:0000269|PubMed:25053812};
CC Vmax=4 nmol/sec/mg enzyme toward UDP-Galactose
CC {ECO:0000269|PubMed:25053812};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:25053812}; Multi-pass membrane protein
CC {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=Q9SZ96-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the TPT transporter family. TPT (TC 2.A.7.9)
CC subfamily. {ECO:0000305}.
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DR EMBL; KJ667161; AIJ01999.1; -; mRNA.
DR EMBL; KP872772; AKA88218.1; -; mRNA.
DR EMBL; AL049482; CAB39648.1; -; Genomic_DNA.
DR EMBL; AL161515; CAB78104.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82801.1; -; Genomic_DNA.
DR EMBL; BT010950; AAR24728.1; -; mRNA.
DR EMBL; AK226903; BAE98980.1; -; mRNA.
DR PIR; T04029; T04029.
DR RefSeq; NP_192719.1; NM_117049.5. [Q9SZ96-1]
DR AlphaFoldDB; Q9SZ96; -.
DR SMR; Q9SZ96; -.
DR STRING; 3702.AT4G09810.1; -.
DR iPTMnet; Q9SZ96; -.
DR PaxDb; Q9SZ96; -.
DR PRIDE; Q9SZ96; -.
DR EnsemblPlants; AT4G09810.1; AT4G09810.1; AT4G09810. [Q9SZ96-1]
DR GeneID; 826570; -.
DR Gramene; AT4G09810.1; AT4G09810.1; AT4G09810. [Q9SZ96-1]
DR KEGG; ath:AT4G09810; -.
DR Araport; AT4G09810; -.
DR TAIR; locus:2118514; AT4G09810.
DR eggNOG; KOG1441; Eukaryota.
DR HOGENOM; CLU_048347_2_1_1; -.
DR InParanoid; Q9SZ96; -.
DR OMA; KERWSHA; -.
DR PhylomeDB; Q9SZ96; -.
DR PRO; PR:Q9SZ96; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZ96; baseline and differential.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0015297; F:antiporter activity; IDA:UniProtKB.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0005338; F:nucleotide-sugar transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0005459; F:UDP-galactose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1904659; P:glucose transmembrane transport; IDA:TAIR.
DR InterPro; IPR031089; NST-KT_B.
DR InterPro; IPR004853; Sugar_P_trans_dom.
DR PANTHER; PTHR11132:SF326; PTHR11132:SF326; 1.
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..335
FT /note="UDP-rhamnose/UDP-galactose transporter 5"
FT /id="PRO_0000439523"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 303..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FDZ5"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FDZ5"
FT CONFLICT 264
FT /note="I -> T (in Ref. 5; BAE98980)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 37030 MW; 7B9D554B0DD23C15 CRC64;
MAPVKKSDKK ATLDAAAWMF NVVTSVGIII VNKALMATYG FSFATTLTGL HFATTTLMTL
VLRCLGYIQP SHLPFTELLK FILFANFSIV GMNVSLMWNS VGFYQIAKLS MIPVSCLLEV
VFDKIRYSRD TKLSIGLVLV GVGVCTVTDV SVNTKGFVAA FVAVWSTALQ QYYVHYLQRK
YSLSSFNLLG HTAPAQAATL LIVGPFLDYW LTDKRVDMYD YNSVSVMFIT LSCTIAIGTN
LSQFICIGRF TAVSFQVLGH MKTILVLVMG FFFFDRDGLN LHVILGMIIA VLGMIWYGNA
SSKPGGKEKK NYSLPTTRQQ KLGATSDSDE HRDKA
