SUT12_ARATH
ID SUT12_ARATH Reviewed; 653 AA.
AC Q9MAX3; Q0WTN0; Q9SH00;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Sulfate transporter 1.2;
GN Name=SULTR1;2; OrderedLocusNames=At1g78000; ORFNames=F28K19.22;
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=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 [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;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND MUTANTS SEL1.
RX PubMed=11846880; DOI=10.1046/j.0960-7412.2001.01232.x;
RA Shibagaki N., Rose A., McDermott J.P., Fujiwara T., Hayashi H.,
RA Yoneyama T., Davies J.P.;
RT "Selenate-resistant mutants of Arabidopsis thaliana identify Sultr1;2, a
RT sulfate transporter required for efficient transport of sulfate into
RT roots.";
RL Plant J. 29:475-486(2002).
RN [6]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=18003916; DOI=10.1073/pnas.0706373104;
RA Tomatsu H., Takano J., Takahashi H., Watanabe-Takahashi A., Shibagaki N.,
RA Fujiwara T.;
RT "An Arabidopsis thaliana high-affinity molybdate transporter required for
RT efficient uptake of molybdate from soil.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18807-18812(2007).
RN [7]
RP HOMODIMERIZATION, INTERACTION WITH OASA1, AND ACTIVITY REGULATION.
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. Plays a central
CC role in the regulation of sulfate assimilation. Unable to transport
CC molybdate. {ECO:0000269|PubMed:11846879, ECO:0000269|PubMed:11846880,
CC ECO:0000269|PubMed:18003916}.
CC -!- ACTIVITY REGULATION: Interaction with OASA1 negatively impacts the
CC transporter activity. {ECO:0000269|PubMed:20529854}.
CC -!- SUBUNIT: Homodimer. Interacts with OASA1 through its STAS domain.
CC {ECO:0000269|PubMed:20529854}.
CC -!- INTERACTION:
CC Q9MAX3; P47998: OASA1; NbExp=5; IntAct=EBI-8772960, EBI-1633418;
CC -!- SUBCELLULAR LOCATION: Cell 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:11846879}.
CC -!- INDUCTION: In roots by sulfate starvation.
CC {ECO:0000269|PubMed:11846879}.
CC -!- MISCELLANEOUS: Sel1 mutations in the gene lead to the resistance of the
CC plant to selenate, a toxic analog of sulfate.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53.1)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF17685.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB042322; BAA95484.1; -; mRNA.
DR EMBL; AC009243; AAF17685.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36055.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36056.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58967.1; -; Genomic_DNA.
DR EMBL; AK227518; BAE99518.1; -; mRNA.
DR PIR; D96809; D96809.
DR RefSeq; NP_001321366.1; NM_001334809.1.
DR RefSeq; NP_565166.1; NM_106449.3.
DR RefSeq; NP_849899.1; NM_179568.2.
DR AlphaFoldDB; Q9MAX3; -.
DR SMR; Q9MAX3; -.
DR BioGRID; 29354; 7.
DR IntAct; Q9MAX3; 4.
DR STRING; 3702.AT1G78000.1; -.
DR TCDB; 2.A.53.1.6; the sulfate permease (sulp) family.
DR iPTMnet; Q9MAX3; -.
DR PaxDb; Q9MAX3; -.
DR PRIDE; Q9MAX3; -.
DR ProteomicsDB; 226753; -.
DR EnsemblPlants; AT1G78000.1; AT1G78000.1; AT1G78000.
DR EnsemblPlants; AT1G78000.2; AT1G78000.2; AT1G78000.
DR EnsemblPlants; AT1G78000.3; AT1G78000.3; AT1G78000.
DR GeneID; 844135; -.
DR Gramene; AT1G78000.1; AT1G78000.1; AT1G78000.
DR Gramene; AT1G78000.2; AT1G78000.2; AT1G78000.
DR Gramene; AT1G78000.3; AT1G78000.3; AT1G78000.
DR KEGG; ath:AT1G78000; -.
DR Araport; AT1G78000; -.
DR TAIR; locus:2029396; AT1G78000.
DR eggNOG; KOG0236; Eukaryota.
DR HOGENOM; CLU_003182_13_2_1; -.
DR InParanoid; Q9MAX3; -.
DR OMA; EMFARNH; -.
DR OrthoDB; 690428at2759; -.
DR PhylomeDB; Q9MAX3; -.
DR PRO; PR:Q9MAX3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MAX3; baseline and differential.
DR Genevisible; Q9MAX3; AT.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0009970; P:cellular response to sulfate starvation; 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:SF207; PTHR11814:SF207; 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 Cell membrane; Membrane; Reference proteome; Sulfate transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..653
FT /note="Sulfate transporter 1.2"
FT /id="PRO_0000080173"
FT TOPO_DOM 1..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..173
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..253
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..339
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..409
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..466
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 522..645
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 511
FT /note="I->T: In sel1-8; reduces drastically sulfate
FT transport activity."
SQ SEQUENCE 653 AA; 71707 MW; B019CADDD9ADED46 CRC64;
MSSRAHPVDG SPATDGGHVP MKPSPTRHKV GIPPKQNMFK DFMYTFKETF FHDDPLRDFK
DQPKSKQFML GLQSVFPVFD WGRNYTFKKF RGDLISGLTI ASLCIPQDIG YAKLANLDPK
YGLYSSFVPP LVYACMGSSR DIAIGPVAVV SLLLGTLLRA EIDPNTSPDE YLRLAFTATF
FAGITEAALG FFRLGFLIDF LSHAAVVGFM GGAAITIALQ QLKGFLGIKK FTKKTDIISV
LESVFKAAHH GWNWQTILIG ASFLTFLLTS KIIGKKSKKL FWVPAIAPLI SVIVSTFFVY
ITRADKQGVQ IVKHLDQGIN PSSFHLIYFT GDNLAKGIRI GVVAGMVALT EAVAIGRTFA
AMKDYQIDGN KEMVALGMMN VVGSMSSCYV ATGSFSRSAV NFMAGCQTAV SNIIMSIVVL
LTLLFLTPLF KYTPNAILAA IIINAVIPLI DIQAAILIFK VDKLDFIACI GAFFGVIFVS
VEIGLLIAVS ISFAKILLQV TRPRTAVLGN IPRTSVYRNI QQYPEATMVP GVLTIRVDSA
IYFSNSNYVR ERIQRWLHEE EEKVKAASLP RIQFLIIEMS PVTDIDTSGI HALEDLYKSL
QKRDIQLILA NPGPLVIGKL HLSHFADMLG QDNIYLTVAD AVEACCPKLS NEV
