SUT11_ARATH
ID SUT11_ARATH Reviewed; 649 AA.
AC Q9SAY1; O22277;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Sulfate transporter 1.1;
DE AltName: Full=AST101;
DE AltName: Full=High-affinity sulfate transporter 1;
DE AltName: Full=Hst1At;
GN Name=SULTR1;1; Synonyms=HST1; OrderedLocusNames=At4g08620;
GN ORFNames=T3F12.7;
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, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10929111; DOI=10.1046/j.1365-313x.2000.00768.x;
RA Takahashi H., Watanabe-Takahashi A., Smith F.W., Blake-Kalff M.,
RA Hawkesford M.J., Saito K.;
RT "The roles of three functional sulphate transporters involved in uptake and
RT translocation of sulphate in Arabidopsis thaliana.";
RL Plant J. 23:171-182(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10854860; DOI=10.1016/s0014-5793(00)01615-x;
RA Vidmar J.J., Tagmount A., Cathala N., Touraine B., Davidian J.-C.E.;
RT "Cloning and characterization of a root specific high-affinity sulfate
RT transporter from Arabidopsis thaliana.";
RL FEBS Lett. 475:65-69(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11846879; DOI=10.1046/j.0960-7412.2001.01231.x;
RA Yoshimoto N., Takahashi H., Smith F.W., Yamaya T., Saito K.;
RT "Two distinct high-affinity sulfate transporters with different
RT inducibilities mediate uptake of sulfate in Arabidopsis roots.";
RL Plant J. 29:465-473(2002).
RN [6]
RP INTERACTION WITH OASA1.
RX PubMed=20529854; DOI=10.1074/jbc.m110.126888;
RA Shibagaki N., Grossman A.R.;
RT "Binding of cysteine synthase to the STAS domain of sulfate transporter and
RT its regulatory consequences.";
RL J. Biol. Chem. 285:25094-25102(2010).
CC -!- FUNCTION: High-affinity H(+)/sulfate cotransporter that mediates the
CC uptake of the environmental sulfate by plant roots under low-sulfur
CC conditions. Plays a central role in the regulation of sulfate
CC assimilation. {ECO:0000269|PubMed:10854860,
CC ECO:0000269|PubMed:10929111, ECO:0000269|PubMed:11846879}.
CC -!- SUBUNIT: Interacts with OASA1 through its STAS domain.
CC {ECO:0000269|PubMed:20529854}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in lateral root cap, root hairs,
CC epidermal and cortical cells of roots. {ECO:0000269|PubMed:10854860,
CC ECO:0000269|PubMed:10929111, ECO:0000269|PubMed:11846879}.
CC -!- INDUCTION: In roots by sulfate starvation or after selenate treatment.
CC {ECO:0000269|PubMed:10854860, ECO:0000269|PubMed:10929111,
CC ECO:0000269|PubMed:11846879}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000305}.
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DR EMBL; AB018695; BAA33932.1; -; mRNA.
DR EMBL; AC002983; AAB81876.1; -; Genomic_DNA.
DR EMBL; AL161512; CAB77987.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82664.1; -; Genomic_DNA.
DR PIR; T00946; T00946.
DR PIR; T51839; T51839.
DR RefSeq; NP_192602.1; NM_116931.3.
DR AlphaFoldDB; Q9SAY1; -.
DR SMR; Q9SAY1; -.
DR IntAct; Q9SAY1; 1.
DR STRING; 3702.AT4G08620.1; -.
DR TCDB; 2.A.53.1.7; the sulfate permease (sulp) family.
DR PaxDb; Q9SAY1; -.
DR PRIDE; Q9SAY1; -.
DR ProteomicsDB; 226752; -.
DR EnsemblPlants; AT4G08620.1; AT4G08620.1; AT4G08620.
DR GeneID; 826426; -.
DR Gramene; AT4G08620.1; AT4G08620.1; AT4G08620.
DR KEGG; ath:AT4G08620; -.
DR Araport; AT4G08620; -.
DR TAIR; locus:2138561; AT4G08620.
DR eggNOG; KOG0236; Eukaryota.
DR HOGENOM; CLU_003182_13_2_1; -.
DR InParanoid; Q9SAY1; -.
DR OMA; EWLPRYS; -.
DR OrthoDB; 289441at2759; -.
DR PhylomeDB; Q9SAY1; -.
DR PRO; PR:Q9SAY1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SAY1; baseline and differential.
DR Genevisible; Q9SAY1; AT.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015301; F:anion:anion antiporter activity; IBA:GO_Central.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IGI:TAIR.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:1902358; P:sulfate transmembrane transport; IGI:TAIR.
DR GO; GO:0008272; P:sulfate transport; IEP:TAIR.
DR Gene3D; 3.30.750.24; -; 1.
DR InterPro; IPR030314; High_sul_transp.
DR InterPro; IPR018045; S04_transporter_CS.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR PANTHER; PTHR11814; PTHR11814; 1.
DR PANTHER; PTHR11814:SF210; PTHR11814:SF210; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF52091; SSF52091; 1.
DR TIGRFAMs; TIGR00815; sulP; 1.
DR PROSITE; PS01130; SLC26A; 1.
DR PROSITE; PS50801; STAS; 1.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Sulfate transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..649
FT /note="Sulfate transporter 1.1"
FT /id="PRO_0000080172"
FT TOPO_DOM 1..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..111
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..168
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..334
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..404
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..465
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..649
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 517..640
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 17
FT /note="N -> S (in Ref. 1; BAA33932)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 649 AA; 70657 MW; 248521A19E1B7AB4 CRC64;
MSGTINPPDG GGSGARNPPV VRQRVLAPPK AGLLKDIKSV VEETFFHDAP LRDFKGQTPA
KKALLGIQAV FPIIGWAREY TLRKFRGDLI AGLTIASLCI PQDIGYAKLA NVDPKYGLYS
SFVPPLIYAG MGSSRDIAIG PVAVVSLLVG TLCQAVIDPK KNPEDYLRLV FTATFFAGIF
QAGLGFLRLG FLIDFLSHAA VVGFMGGAAI TIALQQLKGF LGIKTFTKKT DIVSVMHSVF
KNAEHGWNWQ TIVIGASFLT FLLVTKFIGK RNRKLFWVPA IAPLISVIIS TFFVFIFRAD
KQGVQIVKHI DQGINPISVH KIFFSGKYFT EGIRIGGIAG MVALTEAVAI ARTFAAMKDY
QIDGNKEMIA LGTMNVVGSM TSCYIATGSF SRSAVNFMAG VETAVSNIVM AIVVALTLEF
ITPLFKYTPN AILAAIIISA VLGLIDIDAA ILIWRIDKLD FLACMGAFLG VIFISVEIGL
LIAVVISFAK ILLQVTRPRT TVLGKLPNSN VYRNTLQYPD AAQIPGILII RVDSAIYFSN
SNYVRERASR WVREEQENAK EYGMPAIRFV IIEMSPVTDI DTSGIHSIEE LLKSLEKQEI
QLILANPGPV VIEKLYASKF VEEIGEKNIF LTVGDAVAVC STEVAEQQT
