SUT22_ARATH
ID SUT22_ARATH Reviewed; 677 AA.
AC P92946; O64434; Q8LPG2; Q8VXW4; Q9SH01;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Sulfate transporter 2.2;
DE AltName: Full=AST56;
DE AltName: Full=AtH14;
GN Name=SULTR2;2; OrderedLocusNames=At1g77990; ORFNames=F28K19.21;
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 [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] OF 11-677,
RP AND CHARACTERIZATION.
RC STRAIN=cv. Columbia;
RX PubMed=8772182; DOI=10.1016/0014-5793(96)00787-9;
RA Takahashi H., Sasakura N., Noji M., Saito K.;
RT "Isolation and characterization of a cDNA encoding a sulfate transporter
RT from Arabidopsis thaliana.";
RL FEBS Lett. 392:95-99(1996).
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] OF 4-677.
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 FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
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 [6]
RP INDUCTION.
RX PubMed=12514246; DOI=10.1093/pcp/pcf183;
RA Ohkama N., Takei K., Sakakibara H., Hayashi H., Yoneyama T., Fujiwara T.;
RT "Regulation of sulfur-responsive gene expression by exogenously applied
RT cytokinins in Arabidopsis thaliana.";
RL Plant Cell Physiol. 43:1493-1501(2002).
CC -!- FUNCTION: Low-affinity H(+)/sulfate cotransporter that may be involved
CC in the distribution of sulfate from vascular bundles to the palisade
CC cells of the leaves. Plays a central role in the regulation of sulfate
CC assimilation. {ECO:0000269|PubMed:10929111}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the phloem in roots and in the phloem
CC of vascular bundles in leaves. {ECO:0000269|PubMed:10929111}.
CC -!- INDUCTION: In leaves by sulfate starvation. Up-regulated after
CC treatment with zeatin, an exogenous cytokinin.
CC {ECO:0000269|PubMed:10929111, ECO:0000269|PubMed:12514246}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF17693.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAL67130.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM20714.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA12811.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA12811.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA25174.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009243; AAF17693.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36054.1; -; Genomic_DNA.
DR EMBL; AY074516; AAL67130.2; ALT_INIT; mRNA.
DR EMBL; AY099863; AAM20714.1; ALT_INIT; mRNA.
DR EMBL; AB012047; BAA25174.1; ALT_SEQ; Genomic_DNA.
DR EMBL; D85416; BAA12811.1; ALT_SEQ; mRNA.
DR PIR; S74246; S74246.
DR RefSeq; NP_565165.2; NM_106448.4.
DR AlphaFoldDB; P92946; -.
DR SMR; P92946; -.
DR STRING; 3702.AT1G77990.1; -.
DR iPTMnet; P92946; -.
DR PaxDb; P92946; -.
DR PRIDE; P92946; -.
DR ProteomicsDB; 226755; -.
DR EnsemblPlants; AT1G77990.1; AT1G77990.1; AT1G77990.
DR GeneID; 844134; -.
DR Gramene; AT1G77990.1; AT1G77990.1; AT1G77990.
DR KEGG; ath:AT1G77990; -.
DR Araport; AT1G77990; -.
DR TAIR; locus:2029496; AT1G77990.
DR eggNOG; KOG0236; Eukaryota.
DR HOGENOM; CLU_003182_13_2_1; -.
DR InParanoid; P92946; -.
DR OMA; TECQKIG; -.
DR OrthoDB; 289441at2759; -.
DR PRO; PR:P92946; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P92946; baseline and differential.
DR Genevisible; P92946; 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 Gene3D; 3.30.750.24; -; 1.
DR InterPro; IPR030315; Low_suf_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:SF61; PTHR11814:SF61; 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 Glycoprotein; Membrane; Reference proteome; Sulfate transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..677
FT /note="Sulfate transporter 2.2"
FT /id="PRO_0000080176"
FT TOPO_DOM 1..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..133
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..190
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..352
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411..422
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..482
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..677
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 540..666
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 108
FT /note="K -> R (in Ref. 4; BAA12811)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="L -> P (in Ref. 2; AAL67130)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 677 AA; 74498 MW; 904D9361F9A0D822 CRC64;
MQLSSLSHTS ITHKDKKKKM GIELQNHQSH HEEASPAEEP MSRWLINTPE PPSMWQELIG
YIRTNVLAKK KHKRNKTKNS SSNLVYSCLK SAFPILSWGR QYKLNLFKKD LMAGLTLASL
CIPQSIGYAN LAGLDPEYGL YTSVVPPLIY STMGTSRELA IGPVAVVSLL LSSMVRDLQD
PVTDPIAYRK IVFTVTFFAG AFQAIFGLFR LGFLVDFLSH AALVGFMAGA AIVIGLQQLK
GLFGLTHFTN KTDVVSVLSS VFHSLHHPWQ PLNFVIGSSF LIFILLARFI GKRNNKLFWI
PAMAPLISVV LATLIVYLSN AESRGVKIVK HIKPGFNQLS VNQLQFKSPH LGQIAKIGLI
SAIIALTEAI AVGRSFATIK GYRLDGNKEM MAMGFMNIAG SLSSCYVATG SFSRTAVNFS
AGCETVVSNI VMAITVMISL EVLTRFLYFT PTAILASIIL SALPGLIDVS GALHIWKLDK
LDFLVLIAAF FGVLFASVEI GLLLAVGISF ARIMLSSIRP SIEALGRLSK TDIFGDINQY
PMANKTAGLL TLRISSPLLC FANANFIRDR ILNSVQEIEG EENEQEVLKE NGLQVVILDM
SCVMGVDTSG VFALEELHQE LASNDIRLVI ASPRWRVLHK LKRAKLDEKI KTENIYMTVG
EAVDIYVRAR STSHELC
