SULT2_CHLRE
ID SULT2_CHLRE Reviewed; 764 AA.
AC A8J6J0;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Proton/sulfate cotransporter 2;
GN Name=SULTR2; ORFNames=CHLREDRAFT_150514;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION BY SULFUR, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20498339; DOI=10.1104/pp.110.157875;
RA Pootakham W., Gonzalez-Ballester D., Grossman A.R.;
RT "Identification and regulation of plasma membrane sulfate transporters in
RT Chlamydomonas.";
RL Plant Physiol. 153:1653-1668(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [3]
RP INDUCTION BY SULFUR.
RX PubMed=18326790; DOI=10.1104/pp.108.116137;
RA Gonzalez-Ballester D., Pollock S.V., Pootakham W., Grossman A.R.;
RT "The central role of a SNRK2 kinase in sulfur deprivation responses.";
RL Plant Physiol. 147:216-227(2008).
CC -!- FUNCTION: H(+)/sulfate cotransporter with a probable high-affinity for
CC sulfate and a proteasome independent turnover.
CC {ECO:0000269|PubMed:20498339}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20498339};
CC Multi-pass membrane protein {ECO:0000269|PubMed:20498339}.
CC -!- INDUCTION: Up-regulated by sulfur deprivation.
CC {ECO:0000269|PubMed:18326790, ECO:0000269|PubMed:20498339}.
CC -!- DISRUPTION PHENOTYPE: No effect on sulfate uptake, due to the
CC redundancy with SLT1 and SLTR2. Slt1 and sultr2 double mutants, as well
CC as slt2 and sultr2 show a 50% decline in uptake while the slt1, slt2
CC and sultr2 triple mutant exhibits no increase in sulfate uptake
CC capacity when deprived of sulfur. {ECO:0000269|PubMed:20498339}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000305}.
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DR EMBL; GU181277; ACZ63170.1; -; mRNA.
DR EMBL; DS496139; EDP00477.1; -; Genomic_DNA.
DR RefSeq; XP_001697222.1; XM_001697170.1.
DR AlphaFoldDB; A8J6J0; -.
DR SMR; A8J6J0; -.
DR STRING; 3055.EDP00477; -.
DR TCDB; 2.A.53.1.8; the sulfate permease (sulp) family.
DR PaxDb; A8J6J0; -.
DR EnsemblPlants; PNW70519; PNW70519; CHLRE_17g723350v5.
DR GeneID; 5722730; -.
DR Gramene; PNW70519; PNW70519; CHLRE_17g723350v5.
DR KEGG; cre:CHLRE_17g723350v5; -.
DR eggNOG; KOG0236; Eukaryota.
DR HOGENOM; CLU_003182_13_2_1; -.
DR InParanoid; A8J6J0; -.
DR OMA; PNCVLAS; -.
DR OrthoDB; 690428at2759; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.750.24; -; 1.
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; PS50801; STAS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Stress response; Sulfate transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..764
FT /note="Proton/sulfate cotransporter 2"
FT /id="PRO_0000417127"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 542..664
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 764 AA; 83230 MW; 050C75A8A9DAFDCA CRC64;
MKRNTSNVDT GGVPAPLNST PSTRLIQNGY GDSKYETERM EFPFPEDPRY HPRDSVKGAW
EKVKEDHHHR VATYNWVDWL AFFIPCVRWL RTYRRSYLLN DIVAGISVGF MVVPQGLSYA
NLAGLPSVYG LYGAFLPCIV YSLVGSSRQL AVGPVAVTSL LLGTKLKDIL PEAAGISNPN
IPGSPELDAV QEKYNRLAIQ LAFLVACLYT GVGIFRLGFV TNFLSHAVIG GFTSGAAITI
GLSQVKYILG ISIPRQDRLQ DQAKTYVDNM HNMKWQEFIM GTTFLFLLVL FKEVGKRSKR
FKWLRPIGPL TVCIIGLCAV YVGNVQNKGI KIIGAIKAGL PAPTVSWWFP MPEISQLFPT
AIVVMLVDLL ESTSIARALA RKNKYELHAN QEIVGLGLAN FAGAIFNCYT TTGSFSRSAV
NNESGAKTGL ACFITAWVVG FVLIFLTPVF AHLPYCTLGA IIVSSIVGLL EYEQAIYLWK
VNKLDWLVWM ASFLGVLFIS VEIGLGIAIG LAILIVIYES AFPNTALVGR IPGTTIWRNI
KQYPNAQLAP GLLVFRIDAP IYFANIQWIK ERLEGFASAH RVWSQEHGVP LEYVILDFSP
VTHIDATGLH TLETIVETLA GHGTQVVLAN PSQEIIALMR RGGLFDMIGR DYVFITVNEA
VTFCSRQMAE RGYAVKEDNT SSYPHFGSRR TPGALPAPSS QLDSSPPTSV TESTSGTPAA
GTYSSIGGAV PAVAGHTAAG NGGSHSPSAQ PGVQLTTTGS QRQQ
