GFT1_ARATH
ID GFT1_ARATH Reviewed; 341 AA.
AC Q84L08;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=GDP-fucose transporter 1 {ECO:0000303|PubMed:27381418};
DE AltName: Full=GDP-mannose transporter GONST4 {ECO:0000303|PubMed:15480787};
DE AltName: Full=Protein GOLGI NUCLEOTIDE SUGAR TRANSPORTER 4 {ECO:0000303|PubMed:15480787};
GN Name=GFT1 {ECO:0000303|PubMed:27381418};
GN Synonyms=GONST4 {ECO:0000312|EMBL:CAD83088.1};
GN OrderedLocusNames=At5g19980 {ECO:0000312|Araport:AT5G19980};
GN ORFNames=F28I16.130 {ECO:0000312|EMBL:AF296836};
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=15480787; DOI=10.1007/s00438-004-1071-z;
RA Handford M.G., Sicilia F., Brandizzi F., Chung J.H., Dupree P.;
RT "Arabidopsis thaliana expresses multiple Golgi-localised nucleotide-sugar
RT transporters related to GONST1.";
RL Mol. Genet. Genomics 272:397-410(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=27381418; DOI=10.1038/ncomms12119;
RA Rautengarten C., Ebert B., Liu L., Stonebloom S., Smith-Moritz A.M.,
RA Pauly M., Orellana A., Scheller H.V., Heazlewood J.L.;
RT "The Arabidopsis Golgi-localized GDP-L-fucose transporter is required for
RT plant development.";
RL Nat. Commun. 7:12119-12119(2016).
CC -!- FUNCTION: Acts as the major nucleotide-sugar transporter for the import
CC of GDP-Fucose into the Golgi lumen. Transports GDP-Fucose in a strict
CC counter-exchange mode. Is required for proper plant growth and
CC development (PubMed:27381418). Acts also as a GDP-mannose transporter
CC that may be involved in the import of GDP-mannose from the cytoplasm
CC into the Golgi lumen (PubMed:15480787). {ECO:0000269|PubMed:15480787,
CC ECO:0000269|PubMed:27381418}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7 uM for UDP-Fucose {ECO:0000269|PubMed:27381418};
CC Vmax=54 nmol/sec/mg enzyme toward UDP-Fucose
CC {ECO:0000269|PubMed:27381418};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:15480787, ECO:0000269|PubMed:27381418}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:15480787}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15480787,
CC ECO:0000269|PubMed:27381418}.
CC -!- MISCELLANEOUS: RNAi plants display dwarfed phenotype with severe
CC developmental growth defects. Cell wall composition of the RNAi plants
CC shows a considerable reduction of the fucose content. GFT1 down-
CC regulation has also an impact on the levels of protein fucosylation.
CC {ECO:0000269|PubMed:27381418}.
CC -!- SIMILARITY: Belongs to the nucleotide-sugar transporter family. GDP-
CC Mannose:GMP antiporter (GMA) (TC 2.A.7.13) subfamily. {ECO:0000305}.
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DR EMBL; AJ551327; CAD83088.1; -; mRNA.
DR EMBL; AF296836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92776.1; -; Genomic_DNA.
DR EMBL; BT024734; ABD59072.1; -; mRNA.
DR RefSeq; NP_197498.1; NM_122005.4.
DR AlphaFoldDB; Q84L08; -.
DR SMR; Q84L08; -.
DR STRING; 3702.AT5G19980.1; -.
DR iPTMnet; Q84L08; -.
DR PaxDb; Q84L08; -.
DR PRIDE; Q84L08; -.
DR ProteomicsDB; 221830; -.
DR EnsemblPlants; AT5G19980.1; AT5G19980.1; AT5G19980.
DR GeneID; 832120; -.
DR Gramene; AT5G19980.1; AT5G19980.1; AT5G19980.
DR KEGG; ath:AT5G19980; -.
DR Araport; AT5G19980; -.
DR TAIR; locus:2147655; AT5G19980.
DR eggNOG; KOG1444; Eukaryota.
DR HOGENOM; CLU_045047_1_0_1; -.
DR InParanoid; Q84L08; -.
DR OMA; MSYFAWM; -.
DR OrthoDB; 1093260at2759; -.
DR PhylomeDB; Q84L08; -.
DR PRO; PR:Q84L08; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84L08; baseline and differential.
DR Genevisible; Q84L08; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA: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:0005457; F:GDP-fucose transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0015780; P:nucleotide-sugar transmembrane transport; IGI:TAIR.
DR InterPro; IPR029663; GONST4.
DR InterPro; IPR004853; Sugar_P_trans_dom.
DR PANTHER; PTHR11132:SF386; PTHR11132:SF386; 1.
DR Pfam; PF03151; TPT; 1.
PE 1: Evidence at protein level;
KW Antiport; Golgi apparatus; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..341
FT /note="GDP-fucose transporter 1"
FT /id="PRO_0000406123"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
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 316..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 341 AA; 37386 MW; 6952E8F43E57B916 CRC64;
MSSSRFDSNK QLTTSSLVIG YALCSSLLAV INKLAITYFN YPGLLTALQY LTCTVAVYLL
GKSGLINHDP FTWDTAKKFL PAAIVFYLAI FTNTNLLRHA NVDTFIVFRS LTPLLVAIAD
TVFRSQPLPS RLTFLSLVVI LAGAVGYVAT DSSFTLTAYS WALAYLVTIT TEMVYIKHMV
SNIKLNIWGL VLYNNLLSLM IAPVFWFLTG EFTEVFAALS ENRGNLFEPY AFSSVAASCV
FGFLISYFGF AARNAISATA FTVTGVVNKF LTVVINVLIW DKHATPVGLV CLLFTICGGV
GYQQSVKLDK PIEKVSEKDS EKGEEDEELT QLVPGKLASV V
