SULP1_CHLRE
ID SULP1_CHLRE Reviewed; 411 AA.
AC Q8RVC7;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Sulfate permease 1, chloroplastic;
DE Flags: Precursor;
GN Name=SULP1; Synonyms=SULP; ORFNames=CHLREDRAFT_128906;
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 [GENOMIC DNA / MRNA].
RX PubMed=12883888; DOI=10.1007/s00425-003-1076-6;
RA Chen H.C., Yokthongwattana K., Newton A.J., Melis A.;
RT "SulP, a nuclear gene encoding a putative chloroplast-targeted sulfate
RT permease in Chlamydomonas reinhardtii.";
RL Planta 218:98-106(2003).
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 FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cw15;
RX PubMed=15278455; DOI=10.1007/s00425-004-1331-5;
RA Chen H.C., Melis A.;
RT "Localization and function of SulP, a nuclear-encoded chloroplast sulfate
RT permease in Chlamydomonas reinhardtii.";
RL Planta 220:198-210(2004).
RN [4]
RP FUNCTION.
RX PubMed=16049788; DOI=10.1007/s11120-004-7157-y;
RA Chen H.C., Newton A.J., Melis A.;
RT "Role of SulP, a nuclear-encoded chloroplast sulfate permease, in sulfate
RT transport and H2 evolution in Chlamydomonas reinhardtii.";
RL Photosyn. Res. 84:289-296(2005).
RN [5]
RP SUBUNIT.
RX PubMed=16307303; DOI=10.1007/s11120-005-7382-z;
RA Melis A., Chen H.C.;
RT "Chloroplast sulfate transport in green algae--genes, proteins and
RT effects.";
RL Photosyn. Res. 86:299-307(2005).
RN [6]
RP SUBUNIT.
RX PubMed=18682979; DOI=10.1007/s00425-008-0795-0;
RA Lindberg P., Melis A.;
RT "The chloroplast sulfate transport system in the green alga Chlamydomonas
RT reinhardtii.";
RL Planta 228:951-961(2008).
CC -!- FUNCTION: Part of the ABC-type chloroplast envelope-localized sulfate
CC transporter. Required for primary uptake and assimilation of sulfate
CC and chloroplast protein biosynthesis. {ECO:0000269|PubMed:15278455,
CC ECO:0000269|PubMed:16049788}.
CC -!- SUBUNIT: Part of the chloroplast sulfate permease holocomplex. May form
CC a heterodimer with SLUP2. {ECO:0000269|PubMed:16307303,
CC ECO:0000269|PubMed:18682979}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:15278455}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:15278455}.
CC -!- INDUCTION: Up-regulated by sulfate deprivation, but not by other
CC environmental stresses. {ECO:0000269|PubMed:15278455}.
CC -!- SIMILARITY: Belongs to the ATP-binding cassette (ABC) (TC 3.A.1)
CC superfamily. {ECO:0000305}.
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DR EMBL; AF481828; AAL88671.1; -; mRNA.
DR EMBL; AF467891; AAL75576.1; -; Genomic_DNA.
DR EMBL; DS496123; EDP03937.1; -; Genomic_DNA.
DR RefSeq; XP_001692459.1; XM_001692407.1.
DR AlphaFoldDB; Q8RVC7; -.
DR SMR; Q8RVC7; -.
DR STRING; 3055.EDP03937; -.
DR TCDB; 3.A.1.6.7; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q8RVC7; -.
DR EnsemblPlants; PNW81257; PNW81257; CHLRE_07g348600v5.
DR GeneID; 5718159; -.
DR Gramene; PNW81257; PNW81257; CHLRE_07g348600v5.
DR KEGG; cre:CHLRE_07g348600v5; -.
DR eggNOG; ENOG502S1I2; Eukaryota.
DR HOGENOM; CLU_669689_0_0_1; -.
DR InParanoid; Q8RVC7; -.
DR OMA; VAMHAYY; -.
DR OrthoDB; 1146066at2759; -.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0015419; F:ABC-type sulfate transporter activity; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR011865; CysT_permease.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR InterPro; IPR005667; Sulph_transpt2.
DR PANTHER; PTHR30406; PTHR30406; 1.
DR PANTHER; PTHR30406:SF8; PTHR30406:SF8; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR TIGRFAMs; TIGR00969; 3a0106s02; 1.
DR TIGRFAMs; TIGR02139; permease_CysT; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Membrane; Plastid; Sulfate transport; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 55..411
FT /note="Sulfate permease 1, chloroplastic"
FT /id="PRO_0000418413"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 199..402
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT REGION 68..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 43709 MW; 1540B14133E9C867 CRC64;
MERVCSHQLA SSRGRPCIAG VQRSPIRLGT SSVAHVQVSP AGLGRYQRQR LQVVASAAAA
AAFDPPGGVS AGFSQPQQQL PQQHPRQPQA VAEVAVAESV SAPASAAPSN DGSPTASMDG
GPSSGLSAVP AAATATDLFS AAARLRLPNL SPIITWTFML SYMAFMLIMP ITALLQKASL
VPLNVFIARA TEPVAMHAYY VTFSCSLIAA AINCVFGFVL AWVLVRYNFA GKKILDAAVD
LPFALPTSVA GLTLATVYGD EFFIGQFLQA QGVQVVFTRL GVVIAMIFVS FPFVVRTMQP
VMQEIQKEME EAAWSLGASQ WRTFTDVVLP PLLPALLTGT ALAFSRALGE FGSIVIVSSN
FAFKDLIAPV LIFQCLEQYD YVGATVIGTV LLLISLVMML AVNQLQKLAR K
