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Protein

Sulfate transporter 1.1

Gene

SULTR1;1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

High-affinity H+/sulfate cotransporter that mediates the uptake of the environmental sulfate by plant roots under low-sulfur conditions. Plays a central role in the regulation of sulfate assimilation.3 Publications

GO - Molecular functioni

GO - Biological processi

  • sulfate transport Source: TAIR
Complete GO annotation...

Keywords - Biological processi

Sulfate transport, Symport, Transport

Protein family/group databases

TCDBi2.A.53.1.7. the sulfate permease (sulp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfate transporter 1.1
Alternative name(s):
AST101
High-affinity sulfate transporter 1
Hst1At
Gene namesi
Name:SULTR1;1
Synonyms:HST1
Ordered Locus Names:At4g08620
ORF Names:T3F12.7
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G08620.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8686CytoplasmicSequence analysisAdd
BLAST
Transmembranei87 – 10721HelicalSequence analysisAdd
BLAST
Topological domaini108 – 1114ExtracellularSequence analysis
Transmembranei112 – 13221HelicalSequence analysisAdd
BLAST
Topological domaini133 – 1364CytoplasmicSequence analysis
Transmembranei137 – 15721HelicalSequence analysisAdd
BLAST
Topological domaini158 – 16811ExtracellularSequence analysisAdd
BLAST
Transmembranei169 – 18921HelicalSequence analysisAdd
BLAST
Transmembranei190 – 21021HelicalSequence analysisAdd
BLAST
Topological domaini211 – 24838ExtracellularSequence analysisAdd
BLAST
Transmembranei249 – 26921HelicalSequence analysisAdd
BLAST
Topological domaini270 – 2756CytoplasmicSequence analysis
Transmembranei276 – 29621HelicalSequence analysisAdd
BLAST
Topological domaini297 – 33438ExtracellularSequence analysisAdd
BLAST
Transmembranei335 – 35521HelicalSequence analysisAdd
BLAST
Topological domaini356 – 36712CytoplasmicSequence analysisAdd
BLAST
Transmembranei368 – 38821HelicalSequence analysisAdd
BLAST
Topological domaini389 – 40416ExtracellularSequence analysisAdd
BLAST
Transmembranei405 – 42521HelicalSequence analysisAdd
BLAST
Topological domaini426 – 4316CytoplasmicSequence analysis
Transmembranei432 – 45221HelicalSequence analysisAdd
BLAST
Topological domaini453 – 46513ExtracellularSequence analysisAdd
BLAST
Transmembranei466 – 48621HelicalSequence analysisAdd
BLAST
Topological domaini487 – 649163CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 649649Sulfate transporter 1.1PRO_0000080172Add
BLAST

Proteomic databases

PaxDbiQ9SAY1.
PRIDEiQ9SAY1.

Expressioni

Tissue specificityi

Expressed in lateral root cap, root hairs, epidermal and cortical cells of roots.3 Publications

Inductioni

In roots by sulfate starvation or after selenate treatment.3 Publications

Gene expression databases

GenevisibleiQ9SAY1. AT.

Interactioni

Subunit structurei

Interacts with OASA1 through its STAS domain.1 Publication

Protein-protein interaction databases

IntActiQ9SAY1. 1 interaction.
STRINGi3702.AT4G08620.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SAY1.
SMRiQ9SAY1. Positions 86-637.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini517 – 640124STASPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 STAS domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0236. Eukaryota.
COG0659. LUCA.
HOGENOMiHOG000199842.
InParanoidiQ9SAY1.
KOiK17470.
OMAiILIWRID.
PhylomeDBiQ9SAY1.

Family and domain databases

Gene3Di3.30.750.24. 1 hit.
InterProiIPR030314. High_sul_transp.
IPR018045. S04_transporter_CS.
IPR011547. SLC26A/SulP_dom.
IPR001902. SLC26A/SulP_fam.
IPR002645. STAS_dom.
[Graphical view]
PANTHERiPTHR11814. PTHR11814. 1 hit.
PTHR11814:SF65. PTHR11814:SF65. 1 hit.
PfamiPF01740. STAS. 1 hit.
PF00916. Sulfate_transp. 1 hit.
[Graphical view]
SUPFAMiSSF52091. SSF52091. 1 hit.
TIGRFAMsiTIGR00815. sulP. 1 hit.
PROSITEiPS01130. SLC26A. 1 hit.
PS50801. STAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9SAY1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGTINPPDG GGSGARNPPV VRQRVLAPPK AGLLKDIKSV VEETFFHDAP
60 70 80 90 100
LRDFKGQTPA KKALLGIQAV FPIIGWAREY TLRKFRGDLI AGLTIASLCI
110 120 130 140 150
PQDIGYAKLA NVDPKYGLYS SFVPPLIYAG MGSSRDIAIG PVAVVSLLVG
160 170 180 190 200
TLCQAVIDPK KNPEDYLRLV FTATFFAGIF QAGLGFLRLG FLIDFLSHAA
210 220 230 240 250
VVGFMGGAAI TIALQQLKGF LGIKTFTKKT DIVSVMHSVF KNAEHGWNWQ
260 270 280 290 300
TIVIGASFLT FLLVTKFIGK RNRKLFWVPA IAPLISVIIS TFFVFIFRAD
310 320 330 340 350
KQGVQIVKHI DQGINPISVH KIFFSGKYFT EGIRIGGIAG MVALTEAVAI
360 370 380 390 400
ARTFAAMKDY QIDGNKEMIA LGTMNVVGSM TSCYIATGSF SRSAVNFMAG
410 420 430 440 450
VETAVSNIVM AIVVALTLEF ITPLFKYTPN AILAAIIISA VLGLIDIDAA
460 470 480 490 500
ILIWRIDKLD FLACMGAFLG VIFISVEIGL LIAVVISFAK ILLQVTRPRT
510 520 530 540 550
TVLGKLPNSN VYRNTLQYPD AAQIPGILII RVDSAIYFSN SNYVRERASR
560 570 580 590 600
WVREEQENAK EYGMPAIRFV IIEMSPVTDI DTSGIHSIEE LLKSLEKQEI
610 620 630 640
QLILANPGPV VIEKLYASKF VEEIGEKNIF LTVGDAVAVC STEVAEQQT
Length:649
Mass (Da):70,657
Last modified:September 26, 2003 - v2
Checksum:i248521A19E1B7AB4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171N → S in BAA33932 (PubMed:10929111).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018695 mRNA. Translation: BAA33932.1.
AC002983 Genomic DNA. Translation: AAB81876.1.
AL161512 Genomic DNA. Translation: CAB77987.1.
CP002687 Genomic DNA. Translation: AEE82664.1.
PIRiT00946.
T51839.
RefSeqiNP_192602.1. NM_116931.2.
UniGeneiAt.4168.

Genome annotation databases

EnsemblPlantsiAT4G08620.1; AT4G08620.1; AT4G08620.
GeneIDi826426.
GrameneiAT4G08620.1; AT4G08620.1; AT4G08620.
KEGGiath:AT4G08620.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018695 mRNA. Translation: BAA33932.1.
AC002983 Genomic DNA. Translation: AAB81876.1.
AL161512 Genomic DNA. Translation: CAB77987.1.
CP002687 Genomic DNA. Translation: AEE82664.1.
PIRiT00946.
T51839.
RefSeqiNP_192602.1. NM_116931.2.
UniGeneiAt.4168.

3D structure databases

ProteinModelPortaliQ9SAY1.
SMRiQ9SAY1. Positions 86-637.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9SAY1. 1 interaction.
STRINGi3702.AT4G08620.1.

Protein family/group databases

TCDBi2.A.53.1.7. the sulfate permease (sulp) family.

Proteomic databases

PaxDbiQ9SAY1.
PRIDEiQ9SAY1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G08620.1; AT4G08620.1; AT4G08620.
GeneIDi826426.
GrameneiAT4G08620.1; AT4G08620.1; AT4G08620.
KEGGiath:AT4G08620.

Organism-specific databases

TAIRiAT4G08620.

Phylogenomic databases

eggNOGiKOG0236. Eukaryota.
COG0659. LUCA.
HOGENOMiHOG000199842.
InParanoidiQ9SAY1.
KOiK17470.
OMAiILIWRID.
PhylomeDBiQ9SAY1.

Miscellaneous databases

PROiQ9SAY1.

Gene expression databases

GenevisibleiQ9SAY1. AT.

Family and domain databases

Gene3Di3.30.750.24. 1 hit.
InterProiIPR030314. High_sul_transp.
IPR018045. S04_transporter_CS.
IPR011547. SLC26A/SulP_dom.
IPR001902. SLC26A/SulP_fam.
IPR002645. STAS_dom.
[Graphical view]
PANTHERiPTHR11814. PTHR11814. 1 hit.
PTHR11814:SF65. PTHR11814:SF65. 1 hit.
PfamiPF01740. STAS. 1 hit.
PF00916. Sulfate_transp. 1 hit.
[Graphical view]
SUPFAMiSSF52091. SSF52091. 1 hit.
TIGRFAMsiTIGR00815. sulP. 1 hit.
PROSITEiPS01130. SLC26A. 1 hit.
PS50801. STAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The roles of three functional sulphate transporters involved in uptake and translocation of sulphate in Arabidopsis thaliana."
    Takahashi H., Watanabe-Takahashi A., Smith F.W., Blake-Kalff M., Hawkesford M.J., Saito K.
    Plant J. 23:171-182(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION.
    Strain: cv. Columbia.
  2. "Cloning and characterization of a root specific high-affinity sulfate transporter from Arabidopsis thaliana."
    Vidmar J.J., Tagmount A., Cathala N., Touraine B., Davidian J.-C.E.
    FEBS Lett. 475:65-69(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION.
    Strain: cv. Columbia.
  3. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Two distinct high-affinity sulfate transporters with different inducibilities mediate uptake of sulfate in Arabidopsis roots."
    Yoshimoto N., Takahashi H., Smith F.W., Yamaya T., Saito K.
    Plant J. 29:465-473(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
    Strain: cv. Columbia.
  6. "Binding of cysteine synthase to the STAS domain of sulfate transporter and its regulatory consequences."
    Shibagaki N., Grossman A.R.
    J. Biol. Chem. 285:25094-25102(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OASA1.

Entry informationi

Entry nameiSUT11_ARATH
AccessioniPrimary (citable) accession number: Q9SAY1
Secondary accession number(s): O22277
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: September 26, 2003
Last modified: July 6, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.