SWT15_ARATH
ID SWT15_ARATH Reviewed; 292 AA.
AC Q9FY94; Q8LAG0; Q9XHG3;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Bidirectional sugar transporter SWEET15 {ECO:0000303|PubMed:21107422};
DE Short=AtSWEET15 {ECO:0000303|PubMed:21107422};
DE AltName: Full=Protein SUGARS WILL EVENTUALLY BE EXPORTED TRANSPORTERS 15 {ECO:0000303|PubMed:21107422};
DE AltName: Full=Senescence-associated protein 29 {ECO:0000303|PubMed:20963606};
GN Name=SWEET15 {ECO:0000303|PubMed:21107422};
GN Synonyms=SAG29 {ECO:0000303|PubMed:20963606}; OrderedLocusNames=At5g13170;
GN ORFNames=T19L5.130;
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=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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 51-135, TISSUE SPECIFICITY, AND INDUCTION BY
RP SALICYLIC ACID.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10412905; DOI=10.1023/a:1006199932265;
RA Quirino B.F., Normanly J., Amasino R.M.;
RT "Diverse range of gene activity during Arabidopsis thaliana leaf senescence
RT includes pathogen-independent induction of defense-related genes.";
RL Plant Mol. Biol. 40:267-278(1999).
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 FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY OSMOTIC STRESSES AND ABSCISIC
RP ACID, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=20963606; DOI=10.1007/s00425-010-1293-8;
RA Seo P.J., Park J.-M., Kang S.K., Kim S.-G., Park C.-M.;
RT "An Arabidopsis senescence-associated protein SAG29 regulates cell
RT viability under high salinity.";
RL Planta 233:189-200(2011).
RN [8]
RP FUNCTION.
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 INTERACTION WITH SWEET1; SWEET6; SWEET8; 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, TISSUE SPECIFICITY,
RP AND INDUCTION BY SENESCENCE.
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).
RN [12]
RP INDUCTION BY NAC072/RD26.
RC STRAIN=cv. Columbia;
RX PubMed=29659022; DOI=10.1111/nph.15127;
RA Kamranfar I., Xue G.-P., Tohge T., Sedaghatmehr M., Fernie A.R.,
RA Balazadeh S., Mueller-Roeber B.;
RT "Transcription factor RD26 is a key regulator of metabolic reprogramming
RT during dark-induced senescence.";
RL New Phytol. 218:1543-1557(2018).
CC -!- FUNCTION: Mediates both low-affinity uptake and efflux of sugar across
CC the plasma membrane. Regulates cell viability under high salinity.
CC Promotes senescence and sensitivity to salt stress (PubMed:20963606).
CC Contributes to seed filling by triggering sucrose efflux involved in
CC the transfer of sugars from seed coat to embryos (PubMed:25988582).
CC {ECO:0000269|PubMed:20963606, ECO:0000269|PubMed:22157085,
CC ECO:0000269|PubMed:25794936, ECO:0000303|PubMed:25988582}.
CC -!- SUBUNIT: Forms heterooligomers with SWEET1, SWEET6, SWEET8, SWEET11 and
CC SWEET17. {ECO:0000269|PubMed:24027245}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20963606};
CC Multi-pass membrane protein {ECO:0000269|PubMed:20963606}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:25794936}.
CC -!- TISSUE SPECIFICITY: Accumulates in leaves during senescence, in a SA-
CC independent manner. Expressed in the lateral roots and in flowers.
CC Expressed in developing seeds (PubMed:25794936).
CC {ECO:0000269|PubMed:10412905, ECO:0000269|PubMed:20963606,
CC ECO:0000269|PubMed:25794936}.
CC -!- DEVELOPMENTAL STAGE: In seedlings, expressed at low levels in the
CC petioles (at protein level) (PubMed:25794936). In young plants, mainly
CC expressed in the roots, particularly in the tips and primordia of
CC lateral roots. In flowering plants, first observed at high levels in
CC young buds of the inflorescence (at protein level), later detected in
CC reproductive tissues, such as pollen grains and ovules. In developing
CC seeds, accumulates specifically at different stages. At globular stage,
CC mostly present in outer integument, but also in endosperm and embryo.
CC At the heart stage, only observed in endosperm and embryo. From the
CC linear mature cotyledon stage until mature seed, accumulates in outer
CC integument and in micropylar endosperm. Detected at low levels in
CC senescent leaves (at protein level) despite a high transcription
CC induction during senescence (PubMed:25794936).
CC {ECO:0000269|PubMed:20963606, ECO:0000269|PubMed:25794936}.
CC -!- INDUCTION: Induced by the pathogenic bacteria P.syringae pv. tomato and
CC the fungal pathogen B.cinerea, as well as by salicylic acid (SA) and
CC abscisic acid (ABA). Induced by osmotic stresses (e.g. cold, high
CC salinity, drought, mannitol, and sorbitol) via an abscisic acid-
CC dependent pathway. Highly induced during senescence (PubMed:25794936).
CC Triggered by NAC072/RD26 during senescence (PubMed:29659022).
CC {ECO:0000269|PubMed:10412905, ECO:0000269|PubMed:20963606,
CC ECO:0000269|PubMed:21107422, ECO:0000269|PubMed:25794936,
CC ECO:0000269|PubMed:29659022}.
CC -!- DISRUPTION PHENOTYPE: Reduced sensitivity to high salinity. In plants
CC lacking SWEET11, SWEET12 and SWEET15, severe seed defects, which
CC include retarded embryo development, reduced seed weight, and reduced
CC starch and lipid content, causing a wrinkled seed phenotype. Altered
CC sucrose efflux involved in the transfer of sugars from seed coat to
CC embryos thus leading to starch accumulation in the seed coat but not in
CC the embryo (PubMed:25794936). {ECO:0000269|PubMed:20963606,
CC ECO:0000269|PubMed:25794936}.
CC -!- SIMILARITY: Belongs to the SWEET sugar transporter family.
CC {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; AL391711; CAC05445.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91859.1; -; Genomic_DNA.
DR EMBL; AY045949; AAK76623.1; -; mRNA.
DR EMBL; AY113934; AAM44982.1; -; mRNA.
DR EMBL; AY087836; AAM65389.1; -; mRNA.
DR EMBL; AF118824; AAD20614.1; -; mRNA.
DR RefSeq; NP_196821.1; NM_121320.3.
DR AlphaFoldDB; Q9FY94; -.
DR SMR; Q9FY94; -.
DR BioGRID; 16434; 19.
DR IntAct; Q9FY94; 18.
DR STRING; 3702.AT5G13170.1; -.
DR TCDB; 2.A.123.1.3; the sweet, pq-loop, saliva, mtn3 (sweet) family.
DR PaxDb; Q9FY94; -.
DR PRIDE; Q9FY94; -.
DR ProteomicsDB; 226801; -.
DR EnsemblPlants; AT5G13170.1; AT5G13170.1; AT5G13170.
DR GeneID; 831156; -.
DR Gramene; AT5G13170.1; AT5G13170.1; AT5G13170.
DR KEGG; ath:AT5G13170; -.
DR Araport; AT5G13170; -.
DR TAIR; locus:2179867; AT5G13170.
DR eggNOG; KOG1623; Eukaryota.
DR HOGENOM; CLU_048643_4_0_1; -.
DR InParanoid; Q9FY94; -.
DR OMA; ERSTWAF; -.
DR OrthoDB; 1116261at2759; -.
DR PhylomeDB; Q9FY94; -.
DR PRO; PR:Q9FY94; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FY94; baseline and differential.
DR Genevisible; Q9FY94; AT.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of 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:0071215; P:cellular response to abscisic acid stimulus; IEP:UniProtKB.
DR GO; GO:0071470; P:cellular response to osmotic stress; IMP:UniProtKB.
DR GO; GO:0071446; P:cellular response to salicylic acid stimulus; IEP:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
DR GO; GO:0010150; P:leaf senescence; IMP: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; Golgi apparatus; Membrane;
KW Reference proteome; Repeat; Sugar transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..292
FT /note="Bidirectional sugar transporter SWEET15"
FT /id="PRO_0000404115"
FT TOPO_DOM 1..8
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..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..134
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 12..99
FT /note="MtN3/slv 1"
FT DOMAIN 135..219
FT /note="MtN3/slv 2"
FT CONFLICT 4
FT /note="M -> I (in Ref. 4; AAM65389)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="S -> P (in Ref. 5; AAD20614)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="Q -> E (in Ref. 4; AAM65389)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 292 AA; 32936 MW; 4C3826F6D3A845D5 CRC64;
MGVMINHHFL AFIFGILGNV ISFLVFLAPV PTFYRIYKRK STESFQSLPY QVSLFSCMLW
LYYALIKKDA FLLITINSFG CVVETLYIAM FFAYATREKR ISAMKLFIAM NVAFFSLILM
VTHFVVKTPP LQVSVLGWIC VAISVSVFAA PLMIVARVIK TKSVEYMPFT LSFFLTISAV
MWFAYGLFLN DICIAIPNVV GFVLGLLQMV LYLVYRNSNE KPEKINSSEQ QLKSIVVMSP
LGVSEVHPVV TESVDPLSEA VHHEDLSKVT KVEEPSIENG KCYVEATRPE TV
