ESL1_ARATH
ID ESL1_ARATH Reviewed; 470 AA.
AC Q94KE0; A0A178WFZ8; B1GXJ7; O04037; Q9SCW9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Sugar transporter ESL1 {ECO:0000303|PubMed:19901034};
DE AltName: Full=Protein EARLY-RESPONSIVE TO DEHYDRATION 6-LIKE 1 {ECO:0000303|PubMed:19901034};
DE Short=ERD six-like 1 {ECO:0000303|PubMed:19901034};
DE AltName: Full=Sugar transporter ERD6-like 3;
DE AltName: Full=Sugar transporter-like protein 2 {ECO:0000303|Ref.1};
GN Name=ESL1 {ECO:0000303|PubMed:19901034};
GN Synonyms=SUGTL2 {ECO:0000303|Ref.1};
GN OrderedLocusNames=At1g08920 {ECO:0000312|Araport:AT1G08920};
GN ORFNames=F7G19.20 {ECO:0000312|EMBL:AAB70413.1};
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 2).
RA Gy I., Kreis M., Lecharny A.;
RT "A novel multigene family in Arabidopsis thaliana coding for putative sugar
RT transporters.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Sauer N., Wirsching P.;
RT "An Arabidopsis hexose transporter-like protein.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP GENE FAMILY.
RX PubMed=16923188; DOI=10.1186/1471-2148-6-64;
RA Johnson D.A., Hill J.P., Thomas M.A.;
RT "The monosaccharide transporter gene family in land plants is ancient and
RT shows differential subfamily expression and expansion across lineages.";
RL BMC Evol. Biol. 6:64-64(2006).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, DOMAIN,
RP DISRUPTION PHENOTYPE, MOTIF, AND MUTAGENESIS OF LEU-10; LEU-14; LEU-15 AND
RP LEU-16.
RX PubMed=19901034; DOI=10.1074/jbc.m109.054288;
RA Yamada K., Osakabe Y., Mizoi J., Nakashima K., Fujita Y., Shinozaki K.,
RA Yamaguchi-Shinozaki K.;
RT "Functional analysis of an Arabidopsis thaliana abiotic stress-inducible
RT facilitated diffusion transporter for monosaccharides.";
RL J. Biol. Chem. 285:1138-1146(2010).
CC -!- FUNCTION: Sugar transporter. Transports monosaccharides across the
CC vacuolar membrane independently from a proton gradient. May function
CC coordinately with the vacuolar invertase to regulate osmotic pressure
CC by affecting the accumulation of sugar in the cells under abiotic
CC stress conditions. {ECO:0000269|PubMed:19901034}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:19901034};
CC Multi-pass membrane protein {ECO:0000255}. Vesicle
CC {ECO:0000269|PubMed:19901034}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94KE0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94KE0-2; Sequence=VSP_021545;
CC -!- TISSUE SPECIFICITY: Expressed in both shoots and roots. In roots,
CC strongly expressed in pericycle and xylem parenchyma cells, and to a
CC lesser extent in the root endodermis. In flowers, expressed in sepals.
CC {ECO:0000269|PubMed:19901034}.
CC -!- INDUCTION: By drought and high salinity conditions, and with exogenous
CC application of abscisic acid (ABA), with high expression after 5 hour
CC exposure to these conditions. Expression in roots is higher than that
CC in leaves upon the high salinity and ABA treatment likewise as it is
CC under normal conditions. {ECO:0000269|PubMed:19901034}.
CC -!- DOMAIN: The N-terminal sequence motif LXXXLL is necessary for
CC localization to the vacuole membrane (tonoplast).
CC {ECO:0000269|PubMed:19901034}.
CC -!- DISRUPTION PHENOTYPE: No effect on the root lengths compared to those
CC of wild-type plant under high salinity conditions.
CC {ECO:0000269|PubMed:19901034}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB70413.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ249968; CAB64733.1; -; mRNA.
DR EMBL; AM944529; CAQ16329.1; -; mRNA.
DR EMBL; AC000106; AAB70413.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28367.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28368.1; -; Genomic_DNA.
DR EMBL; AF367260; AAK56249.1; -; mRNA.
DR EMBL; AY133547; AAM91377.1; -; mRNA.
DR PIR; A86221; A86221.
DR RefSeq; NP_563829.1; NM_100764.4. [Q94KE0-1]
DR RefSeq; NP_849618.1; NM_179287.2. [Q94KE0-2]
DR AlphaFoldDB; Q94KE0; -.
DR SMR; Q94KE0; -.
DR BioGRID; 22654; 14.
DR IntAct; Q94KE0; 11.
DR STRING; 3702.AT1G08920.2; -.
DR PaxDb; Q94KE0; -.
DR ProteomicsDB; 222289; -. [Q94KE0-1]
DR EnsemblPlants; AT1G08920.1; AT1G08920.1; AT1G08920. [Q94KE0-1]
DR EnsemblPlants; AT1G08920.2; AT1G08920.2; AT1G08920. [Q94KE0-2]
DR GeneID; 837413; -.
DR Gramene; AT1G08920.1; AT1G08920.1; AT1G08920. [Q94KE0-1]
DR Gramene; AT1G08920.2; AT1G08920.2; AT1G08920. [Q94KE0-2]
DR KEGG; ath:AT1G08920; -.
DR Araport; AT1G08920; -.
DR TAIR; locus:2035984; AT1G08920.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; Q94KE0; -.
DR OMA; WNSFQYL; -.
DR OrthoDB; 430696at2759; -.
DR PhylomeDB; Q94KE0; -.
DR PRO; PR:Q94KE0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94KE0; baseline and differential.
DR Genevisible; Q94KE0; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0015145; F:monosaccharide transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015749; P:monosaccharide transmembrane transport; IDA:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd17358; MFS_GLUT6_8_Class3_like; 1.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR044775; MFS_ERD6/Tret1-like.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Reference proteome; Stress response;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..470
FT /note="Sugar transporter ESL1"
FT /id="PRO_0000259852"
FT TRANSMEM 28..48
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT MOTIF 10..16
FT /note="Essential for the localization to the vacuole
FT membrane"
FT /evidence="ECO:0000269|PubMed:19901034"
FT VAR_SEQ 333
FT /note="L -> LMNDLYLQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_021545"
FT MUTAGEN 10
FT /note="L->A: Localizes mainly to the endoplasmic
FT reticulum."
FT /evidence="ECO:0000269|PubMed:19901034"
FT MUTAGEN 14
FT /note="L->A: Localizes to the plasma membrane. Loss of
FT localization to the vacuole membrane; when associated with
FT A-15 and A-16."
FT /evidence="ECO:0000269|PubMed:19901034"
FT MUTAGEN 15
FT /note="L->A: Localizes to the plasma membrane. Loss of
FT localization to the vacuole membrane; when associated with
FT A-14 and A-16."
FT /evidence="ECO:0000269|PubMed:19901034"
FT MUTAGEN 16
FT /note="L->A: Loss of localization to the vacuole membrane;
FT when associated with A-14 and A-15."
FT /evidence="ECO:0000269|PubMed:19901034"
FT CONFLICT 405
FT /note="V -> G (in Ref. 3; CAB64733)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 51299 MW; B251FCEA8419A772 CRC64;
MTMSENSRNL EAGLLLRKNQ NDINECRITA VVLFSTFVSV CGSFCFGCAA GYSSVAQTGI
INDLGLSVAQ YSMFGSIMTF GGMIGAIFSG KVADLMGRKG TMWFAQIFCI FGWVAVALAK
DSMWLDIGRL STGFAVGLLS YVIPVYIAEI TPKHVRGAFV FANQLMQSCG LSLFYVIGNF
VHWRNLALIG LIPCALQVVT LFFIPESPRL LGKWGHEKEC RASLQSLRGD DADISEEANT
IKETMILFDE GPKSRVMDLF QRRYAPSVVI GVGLMLLQQL SGSSGLMYYV GSVFDKGGFP
SSIGSMILAV IMIPKALLGL ILVEKMGRRP LLLASTGGMC FFSLLLSFSF CFRSYGMLDE
LTPIFTCIGV VGFISSFAVG MGGLPWIIMS EIFPMNVKVS AGTLVTLANW SFGWIVAFAY
NFMLEWNASG TFLIFFTICG AGIVFIYAMV PETKGRTLED IQASLTDFLQ
