STP10_ARATH
ID STP10_ARATH Reviewed; 514 AA.
AC Q9LT15; O81707;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Sugar transport protein 10 {ECO:0000303|PubMed:16923188};
DE Short=AtSTP10 {ECO:0000303|PubMed:26893494};
DE AltName: Full=D-glucose-H(+) symport protein STP10 {ECO:0000305};
DE AltName: Full=D-glucose-proton symporter STP10 {ECO:0000305};
DE AltName: Full=Hexose transporter 10 {ECO:0000305};
GN Name=STP10 {ECO:0000303|PubMed:16923188};
GN OrderedLocusNames=At3g19940 {ECO:0000312|Araport:AT3G19940};
GN ORFNames=MPN9.19 {ECO:0000312|EMBL:BAB01309.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 407-474.
RC STRAIN=cv. C24;
RA Baier K., Truernit E., Sauer N.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=26893494; DOI=10.1093/jxb/erw048;
RA Rottmann T., Zierer W., Subert C., Sauer N., Stadler R.;
RT "STP10 encodes a high-affinity monosaccharide transporter and is induced
RT under low-glucose conditions in pollen tubes of Arabidopsis.";
RL J. Exp. Bot. 67:2387-2399(2016).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-514 IN COMPLEX WITH
RP BETA-D-GLUCOSE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, DISULFIDE BONDS,
RP AND MUTAGENESIS OF LEU-43; CYS-77 AND CYS-449.
RX PubMed=30679446; DOI=10.1038/s41467-018-08176-9;
RA Paulsen P.A., Custodio T.F., Pedersen B.P.;
RT "Crystal structure of the plant symporter STP10 illuminates sugar uptake
RT mechanism in monosaccharide transporter superfamily.";
RL Nat. Commun. 10:407-407(2019).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) IN COMPLEX WITH BETA-D-GLUCOSE,
RP FUNCTION, DISULFIDE BONDS, AND MUTAGENESIS OF PHE-39; GLU-162; GLN-177;
RP ILE-184 AND ASP-344.
RX PubMed=34556835; DOI=10.1038/s41477-021-00992-0;
RA Bavnhoj L., Paulsen P.A., Flores-Canales J.C., Schiott B., Pedersen B.P.;
RT "Molecular mechanism of sugar transport in plants unveiled by structures of
RT glucose/H+ symporter STP10.";
RL Nat. Plants 7:1409-1419(2021).
CC -!- FUNCTION: Hexose-H(+) symporter that catalyzes the high-affinity uptake
CC of glucose, galactose and mannose (PubMed:26893494). Proton-coupled
CC symporter responsible for the uptake of glucose from the apoplast into
CC the cells (Probable). {ECO:0000269|PubMed:26893494,
CC ECO:0000305|PubMed:30679446, ECO:0000305|PubMed:34556835}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) + H(+)(out) = D-glucose(in) + H(+)(in);
CC Xref=Rhea:RHEA:69556, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000269|PubMed:26893494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69557;
CC Evidence={ECO:0000269|PubMed:26893494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannose(out) + H(+)(out) = D-mannose(in) + H(+)(in);
CC Xref=Rhea:RHEA:69560, ChEBI:CHEBI:4208, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000269|PubMed:26893494};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69561;
CC Evidence={ECO:0000269|PubMed:26893494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose(in) + H(+)(in) = D-galactose(out) + H(+)(out);
CC Xref=Rhea:RHEA:29019, ChEBI:CHEBI:4139, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000269|PubMed:26893494};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29021;
CC Evidence={ECO:0000269|PubMed:26893494};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 uM for beta-D-glucose {ECO:0000269|PubMed:30679446};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:26893494}; Multi-
CC pass membrane protein {ECO:0000255}. Note=Localizes to the plasma
CC membrane. {ECO:0000269|PubMed:26893494}.
CC -!- TISSUE SPECIFICITY: Expressed in primordia of lateral roots, pollinated
CC stigmata, and pollen tubes. {ECO:0000269|PubMed:26893494}.
CC -!- INDUCTION: Induced under low-glucose conditions in pollen tubes
CC (PubMed:26893494). Down-regulated by glucose (PubMed:26893494).
CC {ECO:0000269|PubMed:26893494}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:26893494}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR EMBL; AB025631; BAB01309.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76310.1; -; Genomic_DNA.
DR EMBL; DQ056599; AAY78747.1; -; mRNA.
DR EMBL; AJ001663; CAA04908.1; -; Genomic_DNA.
DR RefSeq; NP_188628.1; NM_112884.1.
DR PDB; 6H7D; X-ray; 2.40 A; A=2-514.
DR PDB; 7AAQ; X-ray; 1.81 A; A=1-514.
DR PDB; 7AAR; X-ray; 2.64 A; A=1-514.
DR PDBsum; 6H7D; -.
DR PDBsum; 7AAQ; -.
DR PDBsum; 7AAR; -.
DR AlphaFoldDB; Q9LT15; -.
DR SMR; Q9LT15; -.
DR STRING; 3702.AT3G19940.1; -.
DR TCDB; 2.A.1.1.124; the major facilitator superfamily (mfs).
DR PaxDb; Q9LT15; -.
DR PRIDE; Q9LT15; -.
DR ProteomicsDB; 228425; -.
DR EnsemblPlants; AT3G19940.1; AT3G19940.1; AT3G19940.
DR GeneID; 821532; -.
DR Gramene; AT3G19940.1; AT3G19940.1; AT3G19940.
DR KEGG; ath:AT3G19940; -.
DR Araport; AT3G19940; -.
DR TAIR; locus:2092221; AT3G19940.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; Q9LT15; -.
DR OMA; WFGRRIT; -.
DR OrthoDB; 430696at2759; -.
DR PhylomeDB; Q9LT15; -.
DR PRO; PR:Q9LT15; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LT15; baseline and differential.
DR Genevisible; Q9LT15; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0055055; F:D-glucose:proton symporter activity; IDA:TAIR.
DR GO; GO:0005354; F:galactose transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0009679; F:hexose:proton symporter activity; IDA:TAIR.
DR GO; GO:0015578; F:mannose transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:TAIR.
DR GO; GO:0008645; P:hexose transmembrane transport; IDA: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 3D-structure; Disulfide bond; Membrane; Reference proteome;
KW Sugar transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..514
FT /note="Sugar transport protein 10"
FT /id="PRO_0000050440"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..514
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 177
FT /ligand="beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:15903"
FT /evidence="ECO:0000269|PubMed:30679446,
FT ECO:0000269|PubMed:34556835, ECO:0007744|PDB:6H7D,
FT ECO:0007744|PDB:7AAQ"
FT BINDING 295
FT /ligand="beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:15903"
FT /evidence="ECO:0000269|PubMed:30679446,
FT ECO:0000269|PubMed:34556835, ECO:0007744|PDB:6H7D,
FT ECO:0007744|PDB:7AAQ"
FT BINDING 296
FT /ligand="beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:15903"
FT /evidence="ECO:0000269|PubMed:34556835,
FT ECO:0007744|PDB:7AAQ"
FT BINDING 301
FT /ligand="beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:15903"
FT /evidence="ECO:0000269|PubMed:30679446,
FT ECO:0000269|PubMed:34556835, ECO:0007744|PDB:6H7D,
FT ECO:0007744|PDB:7AAQ"
FT BINDING 332
FT /ligand="beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:15903"
FT /evidence="ECO:0000269|PubMed:30679446,
FT ECO:0000269|PubMed:34556835, ECO:0007744|PDB:6H7D,
FT ECO:0007744|PDB:7AAQ"
FT BINDING 410
FT /ligand="beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:15903"
FT /evidence="ECO:0000269|PubMed:30679446,
FT ECO:0000269|PubMed:34556835, ECO:0007744|PDB:6H7D,
FT ECO:0007744|PDB:7AAQ"
FT DISULFID 77..449
FT /evidence="ECO:0000269|PubMed:30679446,
FT ECO:0000269|PubMed:34556835, ECO:0007744|PDB:6H7D,
FT ECO:0007744|PDB:7AAQ"
FT MUTAGEN 39
FT /note="F->A: Reduces affinity for glucose 8-fold."
FT /evidence="ECO:0000269|PubMed:34556835"
FT MUTAGEN 43
FT /note="L->A: Reduces affinity for glucose 150-fold and
FT turns STP10 into a low affinity transporter."
FT /evidence="ECO:0000269|PubMed:30679446"
FT MUTAGEN 77
FT /note="C->A: Increases sensitivity to alkaline pH and can
FT only function fully at acidic pH (pH < 5)."
FT /evidence="ECO:0000269|PubMed:30679446"
FT MUTAGEN 162
FT /note="E->Q: Abolishes glucose transport activity; when
FT associated with N-344."
FT /evidence="ECO:0000269|PubMed:34556835"
FT MUTAGEN 177
FT /note="Q->A: Reduces affinity for glucose 37-fold."
FT /evidence="ECO:0000269|PubMed:34556835"
FT MUTAGEN 184
FT /note="I->A: Reduces affinity for glucose 3-fold."
FT /evidence="ECO:0000269|PubMed:34556835"
FT MUTAGEN 344
FT /note="D->N: Abolishes glucose transport activity; when
FT associated with Q-162."
FT /evidence="ECO:0000269|PubMed:34556835"
FT MUTAGEN 449
FT /note="C->A: Increases sensitivity to alkaline pH and can
FT only function fully at acidic pH (pH < 5)."
FT /evidence="ECO:0000269|PubMed:30679446"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 36..50
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 61..67
FT /evidence="ECO:0007829|PDB:7AAQ"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:6H7D"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:6H7D"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 82..109
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 111..130
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 135..163
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 169..194
FT /evidence="ECO:0007829|PDB:7AAQ"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 210..222
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 236..247
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 253..266
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:7AAQ"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 282..297
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 306..313
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 317..342
FT /evidence="ECO:0007829|PDB:7AAQ"
FT TURN 343..346
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 348..376
FT /evidence="ECO:0007829|PDB:7AAQ"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 384..402
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 405..415
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 422..443
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 445..449
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 454..473
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 482..485
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 486..490
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 495..498
FT /evidence="ECO:0007829|PDB:7AAQ"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:7AAQ"
SQ SEQUENCE 514 AA; 56200 MW; 0A994C50794F4252 CRC64;
MAGGAFVSEG GGGGRSYEGG VTAFVIMTCI VAAMGGLLFG YDLGISGGVT SMEEFLTKFF
PQVESQMKKA KHDTAYCKFD NQMLQLFTSS LYLAALVASF MASVITRKHG RKVSMFIGGL
AFLIGALFNA FAVNVSMLII GRLLLGVGVG FANQSTPVYL SEMAPAKIRG ALNIGFQMAI
TIGILVANLI NYGTSKMAQH GWRVSLGLAA VPAVVMVIGS FILPDTPNSM LERGKNEEAK
QMLKKIRGAD NVDHEFQDLI DAVEAAKKVE NPWKNIMESK YRPALIFCSA IPFFQQITGI
NVIMFYAPVL FKTLGFGDDA ALMSAVITGV VNMLSTFVSI YAVDRYGRRL LFLEGGIQMF
ICQLLVGSFI GARFGTSGTG TLTPATADWI LAFICVYVAG FAWSWGPLGW LVPSEICPLE
IRPAGQAINV SVNMFFTFLI GQFFLTMLCH MKFGLFYFFA SMVAIMTVFI YFLLPETKGV
PIEEMGRVWK QHWFWKKYIP EDAIIGGHDD NNTN
