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UGNT1_ARATH
ID   UGNT1_ARATH             Reviewed;         344 AA.
AC   A8MRY9; O49364;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=UDP-N-acetylglucosamine transporter UGNT1 {ECO:0000305};
DE            Short=UDP-GlcNAc transporter 1 {ECO:0000303|PubMed:30224661};
DE   AltName: Full=Nucleotide-sugar uncharacterized transporter 3 {ECO:0000305};
GN   Name=UGNT1 {ECO:0000303|PubMed:30224661};
GN   OrderedLocusNames=At4g32272 {ECO:0000312|Araport:AT4G32272};
GN   ORFNames=F10M6.90 {ECO:0000312|EMBL:CAA16963.1};
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=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   [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].
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   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).
RN   [5]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=30224661; DOI=10.1038/s41477-018-0235-5;
RA   Ebert B., Rautengarten C., McFarlane H.E., Rupasinghe T., Zeng W., Ford K.,
RA   Scheller H.V., Bacic A., Roessner U., Persson S., Heazlewood J.L.;
RT   "A Golgi UDP-GlcNAc transporter delivers substrates for N-linked glycans
RT   and sphingolipids.";
RL   Nat. Plants 4:792-801(2018).
CC   -!- FUNCTION: Mediates the transport of UDP-N-acetylglucosamine (UDP-
CC       GlcNAc) across the Golgi apparatus membrane (PubMed:30224661). Delivers
CC       an essential substrate for the maturation of N-glycans and the GlcNAc-
CC       containing glycosyl inositol phosphorylceramide (GIPC) class of
CC       sphingolipids in the Golgi apparatus (PubMed:30224661).
CC       {ECO:0000269|PubMed:30224661}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=9 uM for UDP-N-acetyl-D-glucosamine {ECO:0000269|PubMed:30224661};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:30224661}; 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=A8MRY9-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC       siliques. {ECO:0000269|PubMed:30224661}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but mutant plants have increased levels of high mannose N-
CC       glycans, decreased levels of complex N-glycans, and are insensitive to
CC       root growth inhibition by salt stress. {ECO:0000269|PubMed:30224661}.
CC   -!- SIMILARITY: Belongs to the TPT transporter family. UGnT (TC 2.A.7.15)
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AY075601; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA16963.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79945.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL021811; CAA16963.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161580; CAB79945.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86030.1; -; Genomic_DNA.
DR   EMBL; AY075601; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; T05401; T05401.
DR   RefSeq; NP_001078479.1; NM_001085010.2. [A8MRY9-1]
DR   AlphaFoldDB; A8MRY9; -.
DR   SMR; A8MRY9; -.
DR   STRING; 3702.AT4G32272.2; -.
DR   PRIDE; A8MRY9; -.
DR   ProteomicsDB; 249076; -. [A8MRY9-1]
DR   EnsemblPlants; AT4G32272.1; AT4G32272.1; AT4G32272. [A8MRY9-1]
DR   GeneID; 5008177; -.
DR   Gramene; AT4G32272.1; AT4G32272.1; AT4G32272. [A8MRY9-1]
DR   KEGG; ath:AT4G32272; -.
DR   Araport; AT4G32272; -.
DR   eggNOG; KOG1444; Eukaryota.
DR   HOGENOM; CLU_040726_0_0_1; -.
DR   OMA; TVKFPDF; -.
DR   PhylomeDB; A8MRY9; -.
DR   PRO; PR:A8MRY9; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; A8MRY9; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015297; F:antiporter activity; IBA:GO_Central.
DR   GO; GO:0005338; F:nucleotide-sugar transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0005461; F:UDP-glucuronic acid transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005463; F:UDP-N-acetylgalactosamine transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005462; F:UDP-N-acetylglucosamine transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   GO; GO:1990569; P:UDP-N-acetylglucosamine 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; Golgi apparatus; Membrane; Reference proteome;
KW   Stress response; Sugar transport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..344
FT                   /note="UDP-N-acetylglucosamine transporter UGNT1"
FT                   /id="PRO_0000439530"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   344 AA;  37640 MW;  FCB6A5B286EA2241 CRC64;
     MRNNPVLPVS DPPLAGENDS DGKGVDDRLF KGSAMTKRGA YAALSYMACA VMLVLFNKAA
     LSSYDFPCVN VITLFQMVSS SLFLYALRRR KIISFTAADS FSIDSASTFV PVKTLFHTLP
     LAIAYLLYML ASMASVRGVN VPMYTTLRRT TVAFTMVIEY MLTGQRYTRS IIGSVGIILL
     GAFFAGARDL SFDFYGYGVV FLANISTAVY LATIARTGKS SGLNSFGLMW SNGIICGPIL
     MIWTFICGDL EKTINFPHLL TPGFMVVLLC SCVLAFVLNY CIFLNTTLNS ALTQTICGNM
     KDLFTVGLGW MLFGGLPFDL MNVIGQLFGF FGSGLYAYYK IIGR
 
 
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