STP1_ARATH
ID STP1_ARATH Reviewed; 522 AA.
AC P23586; Q56Z12; Q8H775; Q8LBC8; Q9SXB1;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 171.
DE RecName: Full=Sugar transport protein 1;
DE AltName: Full=Glucose transporter;
DE AltName: Full=Hexose transporter 1;
GN Name=STP1; OrderedLocusNames=At1g11260; ORFNames=T28P6.9;
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], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=2209537; DOI=10.1002/j.1460-2075.1990.tb07500.x;
RA Sauer N., Friedlaender K., Graeml-Wicke U.;
RT "Primary structure, genomic organization and heterologous expression of a
RT glucose transporter from Arabidopsis thaliana.";
RL EMBO J. 9:3045-3050(1990).
RN [2]
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 [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 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-194.
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 429-522.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION.
RX PubMed=1633849; DOI=10.1016/0014-5793(92)80431-f;
RA Boorer K.J., Forde B.G., Leigh R.A., Miller A.J.;
RT "Functional expression of a plant plasma membrane transporter in Xenopus
RT oocytes.";
RL FEBS Lett. 302:166-168(1992).
RN [9]
RP FUNCTION.
RX PubMed=8051137; DOI=10.1016/s0021-9258(17)32008-2;
RA Boorer K.J., Loo D.D.F., Wright E.M.;
RT "Steady-state and presteady-state kinetics of the H(+)/hexose cotransporter
RT (STP1) from Arabidopsis thaliana expressed in Xenopus oocytes.";
RL J. Biol. Chem. 269:20417-20424(1994).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7920712; DOI=10.1046/j.1365-313x.1994.6020225.x;
RA Stolz J., Stadler R., Opekarova M., Sauer N.;
RT "Functional reconstitution of the solubilized Arabidopsis thaliana STP1
RT monosaccharide-H(+) symporter in lipid vesicles and purification of the
RT histidine tagged protein from transgenic Saccharomyces cerevisiae.";
RL Plant J. 6:225-233(1994).
RN [11]
RP FUNCTION.
RX PubMed=11135118; DOI=10.1046/j.1365-313x.2000.00935.x;
RA Sherson S.M., Hemmann G., Wallace G., Forbes S.M., Germain V., Stadler R.,
RA Bechtold N., Sauer N., Smith S.M.;
RT "Monosaccharide/proton symporter AtSTP1 plays a major role in uptake and
RT response of Arabidopsis seeds and seedlings to sugars.";
RL Plant J. 24:849-857(2000).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=12508063; DOI=10.1093/jxb/erg055;
RA Sherson S.M., Alford H.L., Forbes S.M., Wallace G., Smith S.M.;
RT "Roles of cell-wall invertases and monosaccharide transporters in the
RT growth and development of Arabidopsis.";
RL J. Exp. Bot. 54:525-531(2003).
RN [13]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12972665; DOI=10.1104/pp.103.024240;
RA Stadler R., Buettner M., Ache P., Hedrich R., Ivashikina N., Melzer M.,
RA Shearson S.M., Smith S.M., Sauer N.;
RT "Diurnal and light-regulated expression of AtSTP1 in guard cells of
RT Arabidopsis.";
RL Plant Physiol. 133:528-537(2003).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT proteome.";
RL Mol. Cell. Proteomics 3:675-691(2004).
RN [15]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17869214; DOI=10.1016/j.bbrc.2007.08.177;
RA Hem S., Rofidal V., Sommerer N., Rossignol M.;
RT "Novel subsets of the Arabidopsis plasmalemma phosphoproteome identify
RT phosphorylation sites in secondary active transporters.";
RL Biochem. Biophys. Res. Commun. 363:375-380(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
CC -!- FUNCTION: Major hexose transporter. Mediates an active uptake of
CC hexoses, by sugar/hydrogen symport. Can transport glucose, 3-O-
CC methylglucose, fructose, xylose, mannose, galactose, fucose, 2-
CC deoxyglucose and arabinose. Confers sensitivity to galactose in
CC seedlings. {ECO:0000269|PubMed:11135118, ECO:0000269|PubMed:1633849,
CC ECO:0000269|PubMed:2209537, ECO:0000269|PubMed:7920712,
CC ECO:0000269|PubMed:8051137}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for glucose (at pH 6.0 and 32 degrees Celsius)
CC {ECO:0000269|PubMed:2209537};
CC KM=100 uM for 3-O-methylglucose (at pH 6.0 and 32 degrees Celsius)
CC {ECO:0000269|PubMed:2209537};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130,
CC ECO:0000305|PubMed:15308754, ECO:0000305|PubMed:7920712}; Multi-pass
CC membrane protein {ECO:0000305|PubMed:15308754,
CC ECO:0000305|PubMed:7920712}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in young leaves, especially in
CC guard cells (at protein level). Also present in roots.
CC {ECO:0000269|PubMed:12508063, ECO:0000269|PubMed:12972665,
CC ECO:0000269|PubMed:2209537}.
CC -!- INDUCTION: Strong increase at the onset of the dark period followed by
CC a progressive decrease. Transient increase at midday.
CC {ECO:0000269|PubMed:12972665}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD95185.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X55350; CAA39037.1; -; mRNA.
DR EMBL; AC007259; AAD49995.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28705.1; -; Genomic_DNA.
DR EMBL; AY059781; AAL24129.1; -; mRNA.
DR EMBL; AY054249; AAL06908.1; -; mRNA.
DR EMBL; AY133845; AAM91779.1; -; mRNA.
DR EMBL; AY087292; AAM67326.1; -; mRNA.
DR EMBL; AF083803; AAN60361.1; -; mRNA.
DR EMBL; AK221157; BAD95185.1; ALT_INIT; mRNA.
DR PIR; E86246; E86246.
DR PIR; S12042; S12042.
DR RefSeq; NP_172592.1; NM_100998.4.
DR AlphaFoldDB; P23586; -.
DR SMR; P23586; -.
DR BioGRID; 22907; 7.
DR IntAct; P23586; 1.
DR STRING; 3702.AT1G11260.1; -.
DR TCDB; 2.A.1.1.60; the major facilitator superfamily (mfs).
DR iPTMnet; P23586; -.
DR PaxDb; P23586; -.
DR PRIDE; P23586; -.
DR ProteomicsDB; 228428; -.
DR EnsemblPlants; AT1G11260.1; AT1G11260.1; AT1G11260.
DR GeneID; 837667; -.
DR Gramene; AT1G11260.1; AT1G11260.1; AT1G11260.
DR KEGG; ath:AT1G11260; -.
DR Araport; AT1G11260; -.
DR TAIR; locus:2202044; AT1G11260.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; P23586; -.
DR OMA; VWILYMS; -.
DR OrthoDB; 430696at2759; -.
DR PhylomeDB; P23586; -.
DR PRO; PR:P23586; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P23586; baseline and differential.
DR Genevisible; P23586; AT.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0015145; F:monosaccharide transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015749; P:monosaccharide transmembrane transport; IMP:TAIR.
DR CDD; cd17361; MFS_STP; 1.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR044778; MFS_STP/MST-like_plant.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR045262; STP/PLT_plant.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR PANTHER; PTHR23500; PTHR23500; 1.
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; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Reference proteome;
KW Sugar transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..522
FT /note="Sugar transport protein 1"
FT /id="PRO_0000050431"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..79
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..140
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..321
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..384
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..452
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15308754,
FT ECO:0007744|PubMed:17869214, ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862"
FT CONFLICT 333
FT /note="A -> G (in Ref. 1; CAA39037)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="S -> F (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="V -> E (in Ref. 5; AAM67326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 57611 MW; 813AFC8AFA7AA583 CRC64;
MPAGGFVVGD GQKAYPGKLT PFVLFTCVVA AMGGLIFGYD IGISGGVTSM PSFLKRFFPS
VYRKQQEDAS TNQYCQYDSP TLTMFTSSLY LAALISSLVA STVTRKFGRR LSMLFGGILF
CAGALINGFA KHVWMLIVGR ILLGFGIGFA NQAVPLYLSE MAPYKYRGAL NIGFQLSITI
GILVAEVLNY FFAKIKGGWG WRLSLGGAVV PALIITIGSL VLPDTPNSMI ERGQHEEAKT
KLRRIRGVDD VSQEFDDLVA ASKESQSIEH PWRNLLRRKY RPHLTMAVMI PFFQQLTGIN
VIMFYAPVLF NTIGFTTDAS LMSAVVTGSV NVAATLVSIY GVDRWGRRFL FLEGGTQMLI
CQAVVAACIG AKFGVDGTPG ELPKWYAIVV VTFICIYVAG FAWSWGPLGW LVPSEIFPLE
IRSAAQSITV SVNMIFTFII AQIFLTMLCH LKFGLFLVFA FFVVVMSIFV YIFLPETKGI
PIEEMGQVWR SHWYWSRFVE DGEYGNALEM GKNSNQAGTK HV
