SUT41_ARATH
ID SUT41_ARATH Reviewed; 685 AA.
AC Q9FY46; O22123; Q8GW68; Q9FNB8;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Sulfate transporter 4.1, chloroplastic;
DE AltName: Full=AST82;
DE Flags: Precursor;
GN Name=SULTR4;1; OrderedLocusNames=At5g13550; ORFNames=MSH12.1, T6I14_80;
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.
RC STRAIN=cv. Columbia;
RA Takahashi H., Asanuma W., Saito K.;
RT "Cloning of an Arabidopsis cDNA encoding a chloroplast localizing sulphate
RT transporter isoform.";
RL J. Exp. Bot. 50:1713-1714(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-389.
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: H(+)/sulfate cotransporter that may play a role in the
CC regulation of sulfate assimilation.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed both in roots and leaves.
CC -!- INDUCTION: By sulfate starvation in leaves.
CC {ECO:0000269|PubMed:10929111}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC43623.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB008782; BAA23424.1; -; mRNA.
DR EMBL; AL391710; CAC05432.1; -; Genomic_DNA.
DR EMBL; AB006704; BAB17026.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91910.1; -; Genomic_DNA.
DR EMBL; AK119047; BAC43623.1; ALT_SEQ; mRNA.
DR RefSeq; NP_196859.1; NM_121358.3.
DR PDB; 7LHV; EM; 2.75 A; A/B=1-685.
DR PDBsum; 7LHV; -.
DR AlphaFoldDB; Q9FY46; -.
DR SMR; Q9FY46; -.
DR BioGRID; 16477; 1.
DR STRING; 3702.AT5G13550.1; -.
DR TCDB; 2.A.53.1.14; the sulfate permease (sulp) family.
DR iPTMnet; Q9FY46; -.
DR PaxDb; Q9FY46; -.
DR PRIDE; Q9FY46; -.
DR ProteomicsDB; 226832; -.
DR EnsemblPlants; AT5G13550.1; AT5G13550.1; AT5G13550.
DR GeneID; 831199; -.
DR Gramene; AT5G13550.1; AT5G13550.1; AT5G13550.
DR KEGG; ath:AT5G13550; -.
DR Araport; AT5G13550; -.
DR TAIR; locus:2185031; AT5G13550.
DR eggNOG; KOG0236; Eukaryota.
DR HOGENOM; CLU_003182_13_2_1; -.
DR InParanoid; Q9FY46; -.
DR OMA; EAPHDIK; -.
DR OrthoDB; 690428at2759; -.
DR PhylomeDB; Q9FY46; -.
DR PRO; PR:Q9FY46; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FY46; baseline and differential.
DR Genevisible; Q9FY46; AT.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
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:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.750.24; -; 1.
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 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 3D-structure; Chloroplast; Membrane; Plastid; Reference proteome;
KW Stress response; Sulfate transport; Symport; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..23
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 24..685
FT /note="Sulfate transporter 4.1, chloroplastic"
FT /id="PRO_0000032664"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 518..642
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT REGION 15..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 229
FT /note="L -> Q (in Ref. 5; BAC43623)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="A -> P (in Ref. 1; BAA23424)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="E -> D (in Ref. 1; BAA23424)"
FT /evidence="ECO:0000305"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 91..119
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 125..141
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 153..166
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 173..194
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:7LHV"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 206..229
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 255..277
FT /evidence="ECO:0007829|PDB:7LHV"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 284..300
FT /evidence="ECO:0007829|PDB:7LHV"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 330..346
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 348..358
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 365..381
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 391..399
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 406..421
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 423..426
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 431..443
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 448..457
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 459..474
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 477..496
FT /evidence="ECO:0007829|PDB:7LHV"
FT STRAND 501..504
FT /evidence="ECO:0007829|PDB:7LHV"
FT TURN 512..515
FT /evidence="ECO:0007829|PDB:7LHV"
FT STRAND 527..533
FT /evidence="ECO:0007829|PDB:7LHV"
FT TURN 539..541
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 542..560
FT /evidence="ECO:0007829|PDB:7LHV"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:7LHV"
FT STRAND 569..575
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 584..599
FT /evidence="ECO:0007829|PDB:7LHV"
FT STRAND 603..606
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 611..619
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 622..626
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:7LHV"
FT HELIX 635..643
FT /evidence="ECO:0007829|PDB:7LHV"
SQ SEQUENCE 685 AA; 75096 MW; 8C0087229BC39ADD CRC64;
MSYASLSVKD LTSLVSRSGT GSSSSLKPPG QTRPVKVIPL QHPDTSNEAR PPSIPFDDIF
SGWTAKIKRM RLVDWIDTLF PCFRWIRTYR WSEYFKLDLM AGITVGIMLV PQAMSYAKLA
GLPPIYGLYS SFVPVFVYAI FGSSRQLAIG PVALVSLLVS NALGGIADTN EELHIELAIL
LALLVGILEC IMGLLRLGWL IRFISHSVIS GFTSASAIVI GLSQIKYFLG YSIARSSKIV
PIVESIIAGA DKFQWPPFVM GSLILVILQV MKHVGKAKKE LQFLRAAAPL TGIVLGTTIA
KVFHPPSISL VGEIPQGLPT FSFPRSFDHA KTLLPTSALI TGVAILESVG IAKALAAKNR
YELDSNSELF GLGVANILGS LFSAYPATGS FSRSAVNNES EAKTGLSGLI TGIIIGCSLL
FLTPMFKYIP QCALAAIVIS AVSGLVDYDE AIFLWRVDKR DFSLWTITST ITLFFGIEIG
VLVGVGFSLA FVIHESANPH IAVLGRLPGT TVYRNIKQYP EAYTYNGIVI VRIDSPIYFA
NISYIKDRLR EYEVAVDKYT NRGLEVDRIN FVILEMSPVT HIDSSAVEAL KELYQEYKTR
DIQLAISNPN KDVHLTIARS GMVELVGKEW FFVRVHDAVQ VCLQYVQSSN LEDKHLSFTR
RYGGSNNNSS SSNALLKEPL LSVEK
