SULP2_CHLRE
ID SULP2_CHLRE Reviewed; 369 AA.
AC Q6QJE2; A8HNS9;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Sulfate permease 2, chloroplastic;
DE Flags: Precursor;
GN Name=SULP2; ORFNames=CHLREDRAFT_116547;
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].
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 [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, AND 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 [4]
RP FUNCTION, INDUCTION, AND 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. {ECO:0000269|PubMed:16307303,
CC ECO:0000269|PubMed:18682979}.
CC -!- SUBUNIT: Part of the chloroplast sulfate permease holocomplex. May form
CC a heterodimer with SLUP1. {ECO:0000269|PubMed:16307303,
CC ECO:0000269|PubMed:18682979}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- INDUCTION: Up-regulated by sulfate deprivation.
CC {ECO:0000269|PubMed:18682979}.
CC -!- SIMILARITY: Belongs to the ATP-binding cassette (ABC) (TC 3.A.1)
CC superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDP10015.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY536251; AAS20262.1; -; mRNA.
DR EMBL; DS496108; EDP10015.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q6QJE2; -.
DR SMR; Q6QJE2; -.
DR STRING; 3055.EDP10015; -.
DR TCDB; 3.A.1.6.7; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q6QJE2; -.
DR EnsemblPlants; PNW73050; PNW73050; CHLRE_14g616900v5.
DR Gramene; PNW73050; PNW73050; CHLRE_14g616900v5.
DR eggNOG; ENOG502S1HK; Eukaryota.
DR HOGENOM; CLU_016047_14_0_1; -.
DR InParanoid; Q6QJE2; -.
DR OrthoDB; 1337168at2759; -.
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; IPR011866; CysW_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:SF1; PTHR30406:SF1; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR TIGRFAMs; TIGR00969; 3a0106s02; 1.
DR TIGRFAMs; TIGR02140; permease_CysW; 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..82
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 83..369
FT /note="Sulfate permease 2, chloroplastic"
FT /id="PRO_0000418414"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 153..356
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 39479 MW; 96E672FB973FF5B8 CRC64;
MASTTLLQPA LGLPSRVGPR SPLSLPKIPR VCTHTSAPST SKYCDSSSVI ESTLGRQTSV
AGRPWLAPRP APQQSRGDLL VSKSGAAGGM GAHGGGLGEP VDNWIKKLLV GVAAAYIGLV
VLVPFLNVFV QAFAKGIIPF LEHCADPDFL HALKMTLMLA FVTVPLNTVF GTVAAINLTR
NEFPGKVFLM SLLDLPFSIS PVVTGLMLTL LYGRTGWFAA LLRETGINVV FAFTGMALAT
MFVTLPFVVR ELIPILENMD LSQEEAARTL GANDWQVFWN VTLPNIRWGL LYGVILCNAR
AMGEFGAVSV ISGNIIGRTQ TLTLFVESAY KEYNTEAAFA AAVLLSALAL GTLWIKDKVE
EAAAAESRK
