UTR5_ARATH
ID UTR5_ARATH Reviewed; 347 AA.
AC Q6NM25; C0Z2S8; Q0WTJ3; Q9LX77;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=UDP-galactose/UDP-glucose transporter 5 {ECO:0000303|PubMed:12042319};
DE Short=AtUTr5 {ECO:0000303|PubMed:12042319};
GN Name=UTR5 {ECO:0000303|PubMed:12042319};
GN OrderedLocusNames=At3g46180 {ECO:0000312|Araport:AT3G46180};
GN ORFNames=F12M12.150 {ECO:0000312|EMBL:CAB90945.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 2).
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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, AND NOMENCLATURE.
RX PubMed=12042319; DOI=10.1074/jbc.m204081200;
RA Norambuena L., Marchant L., Berninsone P., Hirschberg C.B., Silva H.,
RA Orellana A.;
RT "Transport of UDP-galactose in plants. Identification and functional
RT characterization of AtUTr1, an Arabidopsis thaliana UDP-galactose/UDP-
RT glucose transporter.";
RL J. Biol. Chem. 277:32923-32929(2002).
RN [7]
RP GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=15456736; DOI=10.1093/glycob/cwh159;
RA Bakker H., Routier F., Oelmann S., Jordi W., Lommen A., Gerardy-Schahn R.,
RA Bosch D.;
RT "Molecular cloning of two Arabidopsis UDP-galactose transporters by
RT complementation of a deficient Chinese hamster ovary cell line.";
RL Glycobiology 15:193-201(2005).
RN [8]
RP GENE FAMILY.
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).
CC -!- FUNCTION: Sugar transporter involved in the transport of nucleotide-
CC sugars from cytoplasm into the Golgi and/or the endoplasmic reticulum.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NM25-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NM25-2; Sequence=VSP_042443;
CC -!- SIMILARITY: Belongs to the nucleotide-sugar transporter family. UDP-
CC galactose:UMP antiporter (TC 2.A.7.11) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB90945.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL355775; CAB90945.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78125.1; -; Genomic_DNA.
DR EMBL; AK318892; BAH57007.1; -; mRNA.
DR EMBL; BT011224; AAR92260.1; -; mRNA.
DR EMBL; BT012152; AAS76247.1; -; mRNA.
DR EMBL; AK227561; BAE99555.1; -; mRNA.
DR PIR; T49259; T49259.
DR RefSeq; NP_190204.2; NM_114487.4. [Q6NM25-1]
DR AlphaFoldDB; Q6NM25; -.
DR SMR; Q6NM25; -.
DR STRING; 3702.AT3G46180.1; -.
DR TCDB; 2.A.7.11.7; the drug/metabolite transporter (dmt) superfamily.
DR PaxDb; Q6NM25; -.
DR PRIDE; Q6NM25; -.
DR ProteomicsDB; 228572; -. [Q6NM25-1]
DR EnsemblPlants; AT3G46180.1; AT3G46180.1; AT3G46180. [Q6NM25-1]
DR GeneID; 823761; -.
DR Gramene; AT3G46180.1; AT3G46180.1; AT3G46180. [Q6NM25-1]
DR KEGG; ath:AT3G46180; -.
DR Araport; AT3G46180; -.
DR TAIR; locus:2075311; AT3G46180.
DR eggNOG; KOG1581; Eukaryota.
DR HOGENOM; CLU_036019_3_0_1; -.
DR InParanoid; Q6NM25; -.
DR OMA; IMTTRQM; -.
DR PhylomeDB; Q6NM25; -.
DR PRO; PR:Q6NM25; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q6NM25; baseline and differential.
DR Genevisible; Q6NM25; AT.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0046964; F:3'-phosphoadenosine 5'-phosphosulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR InterPro; IPR013657; UAA.
DR PANTHER; PTHR10778; PTHR10778; 1.
DR Pfam; PF08449; UAA; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Antiport; Membrane; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..347
FT /note="UDP-galactose/UDP-glucose transporter 5"
FT /id="PRO_0000415964"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 325..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 186..347
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640, ECO:0000303|Ref.5"
FT /id="VSP_042443"
FT CONFLICT 13
FT /note="K -> E (in Ref. 3; BAH57007)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 38860 MW; 95111D176F00BD61 CRC64;
MAEPDSVNEA KEKKKKLWKA VFAISGIMLT LVIYGLLQEK IMRVPYGLKK EYFKHSLFLV
FCNRLTTSAV SAAALLASKK VLDPVAPVYK YCLISVTNIL TTTCQYEALK YVSFPVQTLA
KCAKMIPVMV WGTLIMQKKY RGFDYLVAFL VTLGCSVFIL FPAGDDISPY NKGRENTVWG
VSLMVGYLGF DGFTSTFQDK LFKGYNMEIH NQIFYTTICS SILSFTGLIL QGHLLPAVDF
VSRHRDCLFD IALLSTVATA SQFFISYTIR TFGALTFAAI MTTRQLASIM LSCIWFSHPL
SWEQCIGSVI VFGSLYAKTF VKKKSEKPPA AQELPRDEEA QPLKGNP
