ANTR1_ARATH
ID ANTR1_ARATH Reviewed; 512 AA.
AC O82390; Q3EBS0; Q8H0X1; Q8W4H0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Sodium-dependent phosphate transport protein 1, chloroplastic;
DE AltName: Full=Anion transporter 1;
DE AltName: Full=Na(+)/PI cotransporter 1;
DE AltName: Full=Phosphate transporter PHT4;1;
DE AltName: Full=Sodium/phosphate cotransporter 1;
DE Flags: Precursor;
GN Name=ANTR1; Synonyms=PHT4;1; OrderedLocusNames=At2g29650;
GN ORFNames=T27A16.25;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP SUBCELLULAR LOCATION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14564522; DOI=10.1007/s00425-003-1121-5;
RA Roth C., Menzel G., Petetot J.M., Rochat-Hacker S., Poirier Y.;
RT "Characterization of a protein of the plastid inner envelope having
RT homology to animal inorganic phosphate, chloride and organic-anion
RT transporters.";
RL Planta 218:406-416(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=18353780; DOI=10.1074/jbc.m709371200;
RA Pavon L.R., Lundh F., Lundin B., Mishra A., Persson B.L., Spetea C.;
RT "Arabidopsis ANTR1 is a thylakoid Na+-dependent phosphate transporter:
RT functional characterization in Escherichia coli.";
RL J. Biol. Chem. 283:13520-13527(2008).
RN [7]
RP FUNCTION.
RX PubMed=18086223; DOI=10.1111/j.1469-8137.2007.02331.x;
RA Guo B., Jin Y., Wussler C., Blancaflor E.B., Motes C.M., Versaw W.K.;
RT "Functional analysis of the Arabidopsis PHT4 family of intracellular
RT phosphate transporters.";
RL New Phytol. 177:889-898(2008).
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19513231; DOI=10.4161/psb.3.10.6666;
RA Guo B., Irigoyen S., Fowler T.B., Versaw W.K.;
RT "Differential expression and phylogenetic analysis suggest specialization
RT of plastid-localized members of the PHT4 phosphate transporter family for
RT photosynthetic and heterotrophic tissues.";
RL Plant Signal. Behav. 3:784-790(2008).
RN [9]
RP FUNCTION.
RX PubMed=25557369; DOI=10.1038/ncomms6928;
RA Miyaji T., Kuromori T., Takeuchi Y., Yamaji N., Yokosho K., Shimazawa A.,
RA Sugimoto E., Omote H., Ma J.F., Shinozaki K., Moriyama Y.;
RT "AtPHT4;4 is a chloroplast-localized ascorbate transporter in
RT Arabidopsis.";
RL Nat. Commun. 6:5928-5928(2015).
CC -!- FUNCTION: Specific for inorganic phosphate transport across the
CC thylakoid membrane in a sodium dependent manner. Binds glutamate but
CC cannot transport it. May act as an ascorbate transporter at the
CC thylakoid membrane (Probable). {ECO:0000269|PubMed:18086223,
CC ECO:0000269|PubMed:18353780, ECO:0000305|PubMed:25557369}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.17 mM for sodium {ECO:0000269|PubMed:18353780};
CC KM=78.7 uM for inorganic phosphate {ECO:0000269|PubMed:18353780};
CC Vmax=99.15 nmol/h/mg enzyme toward sodium
CC {ECO:0000269|PubMed:18353780};
CC Vmax=161 nmol/h/mg enzyme toward inorganic phosphate
CC {ECO:0000269|PubMed:18353780};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:18353780};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:14564522, ECO:0000269|PubMed:18353780}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:14564522,
CC ECO:0000269|PubMed:18353780}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O82390-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O82390-2; Sequence=VSP_033252, VSP_033253;
CC Name=3;
CC IsoId=O82390-3; Sequence=VSP_033250, VSP_033251;
CC -!- TISSUE SPECIFICITY: Expressed in flower buds, sepals of mature flowers
CC and mature leaves, less in senescent leaves and at low levels in roots.
CC {ECO:0000269|PubMed:18353780, ECO:0000269|PubMed:19513231}.
CC -!- INDUCTION: Expressed with a circadian rhythm showing a peak during the
CC middle of the day (under long day conditions).
CC {ECO:0000269|PubMed:19513231}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion
CC cotransporter (TC 2.A.1.14) family. {ECO:0000305}.
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DR EMBL; AC005496; AAC35230.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08285.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08286.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08287.1; -; Genomic_DNA.
DR EMBL; AY062564; AAL32642.1; -; mRNA.
DR EMBL; AY114683; AAM48002.1; -; mRNA.
DR EMBL; BT001983; AAN71994.1; -; mRNA.
DR EMBL; BT008489; AAP37848.1; -; mRNA.
DR EMBL; BX820656; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; H84698; H84698.
DR RefSeq; NP_180526.1; NM_128519.6. [O82390-1]
DR RefSeq; NP_850136.1; NM_179805.2. [O82390-2]
DR RefSeq; NP_973561.1; NM_201832.1. [O82390-3]
DR AlphaFoldDB; O82390; -.
DR SMR; O82390; -.
DR BioGRID; 2865; 31.
DR IntAct; O82390; 31.
DR STRING; 3702.AT2G29650.1; -.
DR TCDB; 2.A.1.14.22; the major facilitator superfamily (mfs).
DR PaxDb; O82390; -.
DR PRIDE; O82390; -.
DR ProteomicsDB; 245056; -. [O82390-1]
DR EnsemblPlants; AT2G29650.1; AT2G29650.1; AT2G29650. [O82390-1]
DR EnsemblPlants; AT2G29650.2; AT2G29650.2; AT2G29650. [O82390-2]
DR EnsemblPlants; AT2G29650.3; AT2G29650.3; AT2G29650. [O82390-3]
DR GeneID; 817515; -.
DR Gramene; AT2G29650.1; AT2G29650.1; AT2G29650. [O82390-1]
DR Gramene; AT2G29650.2; AT2G29650.2; AT2G29650. [O82390-2]
DR Gramene; AT2G29650.3; AT2G29650.3; AT2G29650. [O82390-3]
DR KEGG; ath:AT2G29650; -.
DR Araport; AT2G29650; -.
DR TAIR; locus:2060694; AT2G29650.
DR eggNOG; KOG2532; Eukaryota.
DR InParanoid; O82390; -.
DR OMA; RVVTTWF; -.
DR OrthoDB; 497052at2759; -.
DR PhylomeDB; O82390; -.
DR BRENDA; 7.3.2.1; 399.
DR SABIO-RK; O82390; -.
DR PRO; PR:O82390; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82390; baseline and differential.
DR Genevisible; O82390; AT.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009579; C:thylakoid; IDA:TAIR.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR GO; GO:0009624; P:response to nematode; HEP:TAIR.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR CDD; cd17380; MFS_SLC17A9_like; 1.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR044777; SLC17A9-like.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Ion transport; Membrane; Plastid;
KW Reference proteome; Sodium; Sodium transport; Symport; Thylakoid;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..59
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 60..512
FT /note="Sodium-dependent phosphate transport protein 1,
FT chloroplastic"
FT /id="PRO_0000331534"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..112
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_033250"
FT VAR_SEQ 113..120
FT /note="FLLCNMDR -> MVGRVSEA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_033251"
FT VAR_SEQ 397..398
FT /note="IM -> FL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_033252"
FT VAR_SEQ 399..512
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_033253"
FT CONFLICT 314
FT /note="W -> R (in Ref. 3; AAM48002/AAL32642)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="H -> N (in Ref. 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 56499 MW; 540536BFA0784834 CRC64;
MNARALLCSS NIHSLYTSNR PPEKTSSSRS LRNLKPSPKS LRVWIYPRNR SSVFRVLVRS
SDKSESSNSY YVEGDKVSGN NDVVSDSPSS IVLPWWEEFP KRWVIVLLCF SAFLLCNMDR
VNMSIAILPM SAEYGWNPAT VGLIQSSFFW GYLLTQIAGG IWADTVGGKR VLGFGVIWWS
IATILTPVAA KLGLPYLLVV RAFMGVGEGV AMPAMNNILS KWVPVQERSR SLALVYSGMY
LGSVTGLAFS PFLIHQFGWP SVFYSFGSLG TVWLTLWLTK AESSPLEDPT LLPEERKLIA
DNCASKEPVK SIPWRLILSK PPVWALISCH FCHNWGTFIL LTWMPTYYHQ VLKFNLMESG
LLSVFPWMTM AISANAGGWI ADTLVSRGFS VTNVRKIMQT IGFLGPAFFL TQLKHIDSPT
MAVLCMACSQ GTDAFSQSGL YSNHQDIAPR YSGVLLGLSN TAGVLAGVLG TAATGHILQH
GSWDDVFTIS VGLYLVGTVI WNLFSTGEKI ID
