SWT12_ARATH
ID SWT12_ARATH Reviewed; 285 AA.
AC O82587;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Bidirectional sugar transporter SWEET12 {ECO:0000303|PubMed:21107422};
DE Short=AtSWEET12 {ECO:0000303|PubMed:21107422};
DE AltName: Full=MtN3-like protein {ECO:0000303|Ref.1};
DE AltName: Full=Protein SUGARS WILL EVENTUALLY BE EXPORTED TRANSPORTERS 12 {ECO:0000303|PubMed:21107422};
GN Name=SWEET12 {ECO:0000303|PubMed:21107422};
GN Synonyms=MTN3 {ECO:0000303|Ref.1}; OrderedLocusNames=At5g23660;
GN ORFNames=MQM1.8;
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].
RA Cheong J.-J.;
RT "An Arabidopsis cDNA clone encoding a protein homologous to Medicago
RT truncatula MTN3.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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;
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 [5]
RP IDENTIFICATION BY 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, TISSUE SPECIFICITY,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
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 SUBUNIT, AND INTERACTION WITH SWEET5; SWEET11 AND SWEET17.
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, AND TISSUE
RP SPECIFICITY.
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:25988582). Contributes to seed filling by
CC triggering sucrose efflux involved in the transfer of sugars from seed
CC coat to embryos (PubMed:25988582). {ECO:0000269|PubMed:22157085,
CC ECO:0000269|PubMed:25794936, ECO:0000303|PubMed:25988582}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=70 mM for sucrose uptake {ECO:0000269|PubMed:22157085};
CC KM=10 mM for sucrose efflux {ECO:0000269|PubMed:22157085};
CC -!- SUBUNIT: Forms homooligomers and heterooligomers with SWEET5, SWEET11
CC and SWEET17. {ECO:0000269|PubMed:24027245}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22157085};
CC Multi-pass membrane protein {ECO:0000250}. Note=Present in the plasma
CC membrane of 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. At globular stage, present in micropylar end of seed
CC coat, in the endosperm and in the embryo suspensor. At the heart stage,
CC confined to the micropylar end of seed coat. From the linear mature
CC cotyledon stage until mature seed, present in the micropylar end of
CC seed coat as well as in the endosperm. {ECO:0000269|PubMed:25794936}.
CC -!- INDUCTION: Induced by the powdery mildew fungus G.cichoracearum and the
CC pathogenic bacteria P.syringae pv. tomato.
CC {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; AF095641; AAC64192.1; -; mRNA.
DR EMBL; AB025633; BAA97235.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93195.1; -; Genomic_DNA.
DR EMBL; AY057575; AAL09814.1; -; mRNA.
DR EMBL; AY059108; AAL15214.1; -; mRNA.
DR EMBL; AY116672; AAM47150.1; -; mRNA.
DR PIR; T51837; T51837.
DR RefSeq; NP_197755.1; NM_122271.3.
DR AlphaFoldDB; O82587; -.
DR SMR; O82587; -.
DR BioGRID; 17706; 5.
DR IntAct; O82587; 2.
DR STRING; 3702.AT5G23660.1; -.
DR iPTMnet; O82587; -.
DR PaxDb; O82587; -.
DR PRIDE; O82587; -.
DR ProteomicsDB; 226558; -.
DR EnsemblPlants; AT5G23660.1; AT5G23660.1; AT5G23660.
DR GeneID; 832431; -.
DR Gramene; AT5G23660.1; AT5G23660.1; AT5G23660.
DR KEGG; ath:AT5G23660; -.
DR Araport; AT5G23660; -.
DR TAIR; locus:2171721; AT5G23660.
DR eggNOG; KOG1623; Eukaryota.
DR HOGENOM; CLU_048643_4_0_1; -.
DR InParanoid; O82587; -.
DR OMA; IELNTHY; -.
DR OrthoDB; 1116261at2759; -.
DR PhylomeDB; O82587; -.
DR SABIO-RK; O82587; -.
DR PRO; PR:O82587; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O82587; baseline and differential.
DR Genevisible; O82587; 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:TAIR.
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; Reference proteome; Repeat;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..285
FT /note="Bidirectional sugar transporter SWEET12"
FT /id="PRO_0000404112"
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..285
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"
SQ SEQUENCE 285 AA; 31487 MW; E18CD08B1D247E03 CRC64;
MALFDTHNTW AFVFGLLGNL ISFAVFLSPV PTFYRICKKK TTEGFQSIPY VVALFSAMLW
LYYATQKKDV FLLVTINSFG CFIETIYISI FVAFASKKAR MLTVKLLLLM NFGGFCLILL
LCQFLAKGTT RAKIIGGICV GFSVCVFAAP LSIIRTVIKT KSVEYMPFSL SLTLTISAVI
WLLYGLALKD IYVAFPNVIG FVLGALQMIL YVVYKYCKTP SDLVEKELEA AKLPEVSIDM
VKLGTLTSPE PVAITVVRSV NTCNCNDRNA EIENGQGVRN SAATT
