SWT11_ARATH
ID SWT11_ARATH Reviewed; 289 AA.
AC Q9SMM5;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Bidirectional sugar transporter SWEET11 {ECO:0000303|PubMed:21107422};
DE Short=AtSWEET11 {ECO:0000303|PubMed:21107422};
DE AltName: Full=Protein SUGARS WILL EVENTUALLY BE EXPORTED TRANSPORTERS 11 {ECO:0000303|PubMed:21107422};
GN Name=SWEET11 {ECO:0000303|PubMed:21107422}; OrderedLocusNames=At3g48740;
GN ORFNames=T21J18.1, T8P19.250;
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].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Seedling;
RX PubMed=17586839; DOI=10.1074/mcp.m700164-mcp200;
RA Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.;
RT "Temporal analysis of sucrose-induced phosphorylation changes in plasma
RT membrane proteins of Arabidopsis.";
RL Mol. Cell. Proteomics 6:1711-1726(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-276, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP INDUCTION BY PATHOGENS, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=21107422; DOI=10.1038/nature09606;
RA Chen L.-Q., Hou B.-H., Lalonde S., Takanaga H., Hartung M.L., Qu X.-Q.,
RA Guo W.-J., Kim J.-G., Underwood W., Chaudhuri B., Chermak D., Antony G.,
RA White F.F., Somerville S.C., Mudgett M.B., Frommer W.B.;
RT "Sugar transporters for intercellular exchange and nutrition of
RT pathogens.";
RL Nature 468:527-532(2010).
RN [7]
RP REVIEW.
RX PubMed=22815540; DOI=10.1093/mp/sss054;
RA Baker R.F., Leach K.A., Braun D.M.;
RT "SWEET as sugar: new sucrose effluxers in plants.";
RL Mol. Plant 5:766-768(2012).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=22157085; DOI=10.1126/science.1213351;
RA Chen L.-Q., Qu X.-Q., Hou B.-H., Sosso D., Osorio S., Fernie A.R.,
RA Frommer W.B.;
RT "Sucrose efflux mediated by SWEET proteins as a key step for phloem
RT transport.";
RL Science 335:207-211(2012).
RN [9]
RP FUNCTION, SUBUNIT, INTERACTION WITH SWEET1; SWEET3; SWEET5; SWEET6; SWEET7;
RP SWEET8; SWEET9; SWEET12; SWEET13; SWEET15 AND SWEET17, AND SUBCELLULAR
RP LOCATION.
RX PubMed=24027245; DOI=10.1073/pnas.1311244110;
RA Xuan Y.H., Hu Y.B., Chen L.-Q., Sosso D., Ducat D.C., Hou B.-H.,
RA Frommer W.B.;
RT "Functional role of oligomerization for bacterial and plant SWEET sugar
RT transporter family.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E3685-E3685(2013).
RN [10]
RP REVIEW.
RC STRAIN=cv. Columbia;
RX PubMed=25988582; DOI=10.1016/j.pbi.2015.04.005;
RA Eom J.-S., Chen L.-Q., Sosso D., Julius B.T., Lin I.W., Qu X.-Q.,
RA Braun D.M., Frommer W.B.;
RT "SWEETs, transporters for intracellular and intercellular sugar
RT translocation.";
RL Curr. Opin. Plant Biol. 25:53-62(2015).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25794936; DOI=10.1105/tpc.114.134585;
RA Chen L.Q., Lin I.W., Qu X.Q., Sosso D., McFarlane H.E., Londono A.,
RA Samuels A.L., Frommer W.B.;
RT "A cascade of sequentially expressed sucrose transporters in the seed coat
RT and endosperm provides nutrition for the Arabidopsis embryo.";
RL Plant Cell 27:607-619(2015).
CC -!- FUNCTION: Mediates both low-affinity uptake and efflux of sugar across
CC the plasma membrane. Involved in phloem loading by mediating export
CC from parenchyma cells feeding H(+)-coupled import into the sieve
CC element/companion cell complex, thus contributing to the sucrose
CC migration from sites of synthesis in the mesophyll to the phloem
CC (PubMed:22157085, PubMed:24027245, PubMed:25988582). Contributes to
CC seed filling by triggering sucrose efflux involved in the transfer of
CC sugars from seed coat to embryos (PubMed:25988582).
CC {ECO:0000269|PubMed:22157085, ECO:0000269|PubMed:24027245,
CC ECO:0000269|PubMed:25794936, ECO:0000303|PubMed:25988582}.
CC -!- SUBUNIT: Forms homooligomers and heterooligomers with SWEET1, SWEET3,
CC SWEET5, SWEET6, SWEET7, SWEET8, SWEET9, SWEET12, SWEET13, SWEET15 and
CC SWEET17. {ECO:0000269|PubMed:24027245}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22157085,
CC ECO:0000269|PubMed:24027245, ECO:0000269|PubMed:25794936}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Present in the plasma membrane of
CC the phloem. {ECO:0000269|PubMed:22157085}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, especially in phloem
CC (PubMed:22157085). Expressed in developing seeds (PubMed:25794936).
CC {ECO:0000269|PubMed:22157085, ECO:0000269|PubMed:25794936}.
CC -!- DEVELOPMENTAL STAGE: In developing seeds, accumulates specifically at
CC different stages. First observed at the linear mature cotyledon stage
CC until mature seed, mostly in micropylar endosperm and the seed coat.
CC {ECO:0000269|PubMed:25794936}.
CC -!- INDUCTION: Slightly induced by the pathogenic bacteria P.syringae pv.
CC tomato, the powdery mildew fungus G.cichoracearum, and the fungal
CC pathogen B.cinerea. {ECO:0000269|PubMed:21107422}.
CC -!- DISRUPTION PHENOTYPE: Under high-light conditions, plants lacking both
CC SWEET11 and SWEET12 are defective in phloem loading and display slower
CC growth, mild chlorosis, and high levels of starch and sugar
CC accumulation in leaves (PubMed:22157085). In plants lacking SWEET11,
CC SWEET12 and SWEET15, severe seed defects, which include retarded embryo
CC development, reduced seed weight, and reduced starch and lipid content,
CC causing a wrinkled seed phenotype. Altered sucrose efflux involved in
CC the transfer of sugars from seed coat to embryos thus leading to starch
CC accumulation in the seed coat but not in the embryo (PubMed:25794936).
CC {ECO:0000269|PubMed:22157085, ECO:0000269|PubMed:25794936}.
CC -!- SIMILARITY: Belongs to the SWEET sugar transporter family.
CC {ECO:0000305}.
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DR EMBL; AL133315; CAB62363.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78451.1; -; Genomic_DNA.
DR EMBL; AF361825; AAK32837.1; -; mRNA.
DR EMBL; AF419559; AAL31891.1; -; mRNA.
DR EMBL; AY070412; AAL49908.1; -; mRNA.
DR EMBL; AY078041; AAL77742.1; -; mRNA.
DR EMBL; AY096594; AAM20244.1; -; mRNA.
DR PIR; T46218; T46218.
DR RefSeq; NP_190443.1; NM_114733.4.
DR AlphaFoldDB; Q9SMM5; -.
DR SMR; Q9SMM5; -.
DR BioGRID; 9353; 11.
DR IntAct; Q9SMM5; 1.
DR STRING; 3702.AT3G48740.1; -.
DR TCDB; 2.A.123.1.13; the sweet, pq-loop, saliva, mtn3 (sweet) family.
DR iPTMnet; Q9SMM5; -.
DR PaxDb; Q9SMM5; -.
DR PRIDE; Q9SMM5; -.
DR ProteomicsDB; 226800; -.
DR EnsemblPlants; AT3G48740.1; AT3G48740.1; AT3G48740.
DR GeneID; 824035; -.
DR Gramene; AT3G48740.1; AT3G48740.1; AT3G48740.
DR KEGG; ath:AT3G48740; -.
DR Araport; AT3G48740; -.
DR TAIR; locus:2114540; AT3G48740.
DR eggNOG; KOG1623; Eukaryota.
DR HOGENOM; CLU_048643_4_0_1; -.
DR InParanoid; Q9SMM5; -.
DR OMA; KEHVVNI; -.
DR OrthoDB; 1116261at2759; -.
DR PhylomeDB; Q9SMM5; -.
DR PRO; PR:Q9SMM5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SMM5; baseline and differential.
DR Genevisible; Q9SMM5; AT.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008515; F:sucrose transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0051119; F:sugar transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0008643; P:carbohydrate transport; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0010431; P:seed maturation; IMP:UniProtKB.
DR GO; GO:0015770; P:sucrose transport; IDA:TAIR.
DR InterPro; IPR004316; SWEET_sugar_transpr.
DR Pfam; PF03083; MtN3_slv; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Sugar transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..289
FT /note="Bidirectional sugar transporter SWEET11"
FT /id="PRO_0000404111"
FT TOPO_DOM 1..9
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..70
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..133
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 12..98
FT /note="MtN3/slv 1"
FT DOMAIN 134..218
FT /note="MtN3/slv 2"
FT REGION 266..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 276
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 289 AA; 31921 MW; BCFB4931EC7FF761 CRC64;
MSLFNTENTW AFVFGLLGNL ISFAVFLSPV PTFYRIWKKK TTEGFQSIPY VVALFSATLW
LYYATQKKDV FLLVTINAFG CFIETIYISM FLAYAPKPAR MLTVKMLLLM NFGGFCAILL
LCQFLVKGAT RAKIIGGICV GFSVCVFAAP LSIIRTVIKT RSVEYMPFSL SLTLTISAVI
WLLYGLALKD IYVAFPNVLG FALGALQMIL YVVYKYCKTS PHLGEKEVEA AKLPEVSLDM
LKLGTVSSPE PISVVRQANK CTCGNDRRAE IEDGQTPKHG KQSSSAAAT
