GONS1_ARATH
ID GONS1_ARATH Reviewed; 333 AA.
AC Q941R4; Q3EC15; Q9SIT2;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=GDP-mannose transporter GONST1 {ECO:0000303|PubMed:11595802};
DE AltName: Full=Protein GOLGI NUCLEOTIDE SUGAR TRANSPORTER 1 {ECO:0000303|PubMed:11595802};
GN Name=GONST1 {ECO:0000312|EMBL:CAC69066.1};
GN OrderedLocusNames=At2g13650 {ECO:0000312|Araport:AT2G13650};
GN ORFNames=T10F5.19 {ECO:0000312|EMBL:AAD22687.2};
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] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11595802; DOI=10.2307/3871508;
RA Baldwin T.C., Handford M.G., Yuseff M.I., Orellana A., Dupree P.;
RT "Identification and characterization of GONST1, a Golgi-localized GDP-
RT mannose transporter in Arabidopsis.";
RL Plant Cell 13:2283-2295(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=20576760; DOI=10.1093/molbev/msq158;
RA Colleoni C., Linka M., Deschamps P., Handford M.G., Dupree P., Weber A.P.,
RA Ball S.G.;
RT "Phylogenetic and biochemical evidence supports the recruitment of an ADP-
RT glucose translocator for the export of photosynthate during plastid
RT endosymbiosis.";
RL Mol. Biol. Evol. 27:2691-2701(2010).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23695979; DOI=10.1105/tpc.113.111500;
RA Mortimer J.C., Yu X., Albrecht S., Sicilia F., Huichalaf M., Ampuero D.,
RA Michaelson L.V., Murphy A.M., Matsunaga T., Kurz S., Stephens E.,
RA Baldwin T.C., Ishii T., Napier J.A., Weber A.P., Handford M.G., Dupree P.;
RT "Abnormal glycosphingolipid mannosylation triggers salicylic acid-mediated
RT responses in Arabidopsis.";
RL Plant Cell 25:1881-1894(2013).
RN [7]
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 [8]
RP SUBCELLULAR LOCATION, FUNCTION, AND BIOPHYSICOCHEMICAL 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: Involved in the import of GDP-mannose from the cytoplasm into
CC the Golgi lumen (PubMed:11595802, PubMed:20576760, PubMed:27381418).
CC Required for the luminal synthesis of a variety of plant cell surface
CC components (PubMed:11595802). Is required for the correct mannosylation
CC of the glycosylinositol phosphoceramides (GIPC). Can indifferently
CC transport GDP-mannose, GDP-Glucose, GDP-Fucose or GDP-Galactose in
CC vitro (PubMed:23695979, PubMed:27381418). {ECO:0000269|PubMed:11595802,
CC ECO:0000269|PubMed:20576760, ECO:0000269|PubMed:23695979,
CC ECO:0000269|PubMed:27381418}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=76 uM for UDP-Fucose {ECO:0000269|PubMed:27381418};
CC KM=17 uM for UDP-Mannose {ECO:0000269|PubMed:27381418};
CC Vmax=14 nmol/sec/mg enzyme toward UDP-Fucose
CC {ECO:0000269|PubMed:27381418};
CC Vmax=24 nmol/sec/mg enzyme toward UDP-Mannose
CC {ECO:0000269|PubMed:27381418};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:11595802, ECO:0000269|PubMed:27381418}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q941R4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q941R4-2; Sequence=VSP_026061, VSP_026062;
CC -!- DISRUPTION PHENOTYPE: Dwarf phenotype, necrotic lesions and a
CC constitutive hypersensitive response to salicylic acid induction.
CC {ECO:0000269|PubMed:23695979}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nucleotide-sugar transporter family. GDP-
CC Mannose:GMP antiporter (GMA) (TC 2.A.7.13) subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ314836; CAC69066.1; -; mRNA.
DR EMBL; AC007063; AAD22687.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC06250.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06251.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06252.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62847.1; -; Genomic_DNA.
DR EMBL; BT030001; ABN04739.1; -; mRNA.
DR PIR; E84509; E84509.
DR RefSeq; NP_001189524.1; NM_001202595.1. [Q941R4-1]
DR RefSeq; NP_001318219.1; NM_001335395.1. [Q941R4-2]
DR RefSeq; NP_565357.1; NM_126944.5. [Q941R4-1]
DR RefSeq; NP_849952.1; NM_179621.3. [Q941R4-2]
DR AlphaFoldDB; Q941R4; -.
DR SMR; Q941R4; -.
DR BioGRID; 1211; 29.
DR IntAct; Q941R4; 1.
DR STRING; 3702.AT2G13650.1; -.
DR TCDB; 2.A.7.13.3; the drug/metabolite transporter (dmt) superfamily.
DR PaxDb; Q941R4; -.
DR PRIDE; Q941R4; -.
DR ProteomicsDB; 248444; -. [Q941R4-1]
DR EnsemblPlants; AT2G13650.1; AT2G13650.1; AT2G13650. [Q941R4-1]
DR EnsemblPlants; AT2G13650.2; AT2G13650.2; AT2G13650. [Q941R4-2]
DR EnsemblPlants; AT2G13650.3; AT2G13650.3; AT2G13650. [Q941R4-1]
DR EnsemblPlants; AT2G13650.7; AT2G13650.7; AT2G13650. [Q941R4-2]
DR GeneID; 815850; -.
DR Gramene; AT2G13650.1; AT2G13650.1; AT2G13650. [Q941R4-1]
DR Gramene; AT2G13650.2; AT2G13650.2; AT2G13650. [Q941R4-2]
DR Gramene; AT2G13650.3; AT2G13650.3; AT2G13650. [Q941R4-1]
DR Gramene; AT2G13650.7; AT2G13650.7; AT2G13650. [Q941R4-2]
DR KEGG; ath:AT2G13650; -.
DR Araport; AT2G13650; -.
DR TAIR; locus:2054090; AT2G13650.
DR eggNOG; KOG1444; Eukaryota.
DR HOGENOM; CLU_025360_0_1_1; -.
DR InParanoid; Q941R4; -.
DR OMA; WCIRKTS; -.
DR PhylomeDB; Q941R4; -.
DR PRO; PR:Q941R4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q941R4; baseline and differential.
DR Genevisible; Q941R4; AT.
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:0015297; F:antiporter activity; IBA:GO_Central.
DR GO; GO:0005457; F:GDP-fucose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005458; F:GDP-mannose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005338; F:nucleotide-sugar transmembrane transporter activity; ISS:TAIR.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEP:TAIR.
DR GO; GO:0015783; P:GDP-fucose transmembrane transport; IDA:UniProtKB.
DR GO; GO:1990570; P:GDP-mannose transmembrane transport; IDA:UniProtKB.
DR InterPro; IPR004853; Sugar_P_trans_dom.
DR InterPro; IPR038736; Vrg4-like.
DR PANTHER; PTHR11132:SF251; PTHR11132:SF251; 1.
DR Pfam; PF03151; TPT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiport; Golgi apparatus; Membrane;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..333
FT /note="GDP-mannose transporter GONST1"
FT /id="PRO_0000213397"
FT TRANSMEM 33..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 284
FT /note="S -> R (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_026061"
FT VAR_SEQ 285..333
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_026062"
FT CONFLICT 17
FT /note="V -> L (in Ref. 1; CAC69066)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 36840 MW; 87340BA073B9276B CRC64;
MKLYEHDGVD LEDGKTVKSG GDKPIPRKIH NRALLSGLAY CISSCSMILV NKFVLSSYNF
NAGIFLMLYQ NFVSVIIVVG LSLMGLITTE PLTLRLMKVW FPVNVIFVGM LITSMFSLKY
INVAMVTVLK NVTNVITAVG EMYLFNKQHD NRVWAALFLM IISAVSGGIT DLSFNAVGYA
WQIANCFLTA SYSLTLRKTM DTAKQVTQSG NLNEFSMVLL NNTLSLPLGL LLSYFFNEMD
YLYQTPLLRL PSFWMVMTLS GLLGLAISFT SMWFLHQTGA TTYSLVGSLN KIPLSIAGIV
LFNVPTSLQN SASILFGLVA GVVFARAKMR EKS
