PHT14_ARATH
ID PHT14_ARATH Reviewed; 534 AA.
AC Q96303;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Inorganic phosphate transporter 1-4;
DE Short=AtPht1;4;
DE AltName: Full=H(+)/Pi cotransporter;
GN Name=PHT1-4; Synonyms=PHT4, PT2; OrderedLocusNames=At2g38940;
GN ORFNames=T7F6.11;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=8927627; DOI=10.1073/pnas.93.19.10519;
RA Muchhal U.S., Pardo J.M., Raghothama K.G.;
RT "Phosphate transporters from the higher plant Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10519-10523(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RA Mukatira U.T., Muchhal U.S., Raghothama K.G.;
RT "Cloning of Arabidopsis thaliana phosphate transporter gene, AtPT2.";
RL (er) Plant Gene Register PGR97-163(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9872450; DOI=10.1093/dnares/5.5.261;
RA Okumura S., Mitsukawa N., Shirano Y., Shibata D.;
RT "Phosphate transporter gene family of Arabidopsis thaliana.";
RL DNA Res. 5:261-269(1998).
RN [4]
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 [5]
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 [6]
RP TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12164813; DOI=10.1046/j.1365-313x.2002.01356.x;
RA Mudge S.R., Rae A.L., Diatloff E., Smith F.W.;
RT "Expression analysis suggests novel roles for members of the Pht1 family of
RT phosphate transporters in Arabidopsis.";
RL Plant J. 31:341-353(2002).
RN [7]
RP INDUCTION.
RX PubMed=12114577; DOI=10.1104/pp.010835;
RA Varadarajan D.K., Karthikeyan A.S., Matilda P.D., Raghothama K.G.;
RT "Phosphite, an analog of phosphate, suppresses the coordinated expression
RT of genes under phosphate starvation.";
RL Plant Physiol. 129:1232-1240(2002).
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12226502; DOI=10.1104/pp.020007;
RA Karthikeyan A.S., Varadarajan D.K., Mukatira U.T., D'Urzo M.P., Damsz B.,
RA Raghothama K.G.;
RT "Regulated expression of Arabidopsis phosphate transporters.";
RL Plant Physiol. 130:221-233(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT proteome.";
RL Mol. Cell. Proteomics 3:675-691(2004).
RN [11]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [12]
RP FUNCTION, AND INDUCTION.
RX PubMed=15272879; DOI=10.1111/j.1365-313x.2004.02161.x;
RA Shin H., Shin H.-S., Dewbre G.R., Harrison M.J.;
RT "Phosphate transport in Arabidopsis: Pht1;1 and Pht1;4 play a major role in
RT phosphate acquisition from both low- and high-phosphate environments.";
RL Plant J. 39:629-642(2004).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15604713; DOI=10.1007/s11103-004-1965-5;
RA Misson J., Thibaud M.-C., Bechtold N., Raghothama K., Nussaume L.;
RT "Transcriptional regulation and functional properties of Arabidopsis
RT Pht1;4, a high affinity transporter contributing greatly to phosphate
RT uptake in phosphate deprived plants.";
RL Plant Mol. Biol. 55:727-741(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524 AND SER-528, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
CC -!- FUNCTION: High-affinity transporter for external inorganic phosphate.
CC Acts as a H(+):phosphate symporter in both low- and high-Pi conditions.
CC Confers sensitivity to arsenate. {ECO:0000269|PubMed:15272879,
CC ECO:0000269|PubMed:15604713, ECO:0000269|PubMed:8927627}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130,
CC ECO:0000305|PubMed:15308754}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:15308754}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, in tissues connecting
CC the lateral roots to the primary root. Also present in flowers, in
CC senescing anther filaments and in the abscission zone at the base of
CC siliques. Expressed in hydathodes and axillary buds, and in some
CC senescing leaves. After Pi starvation, localized in all cells of
CC undifferentiated root segments, including root tips and root hairs, and
CC in the epidermis, cortex and stellar regions of mature root segments.
CC {ECO:0000269|PubMed:12164813, ECO:0000269|PubMed:12226502,
CC ECO:0000269|PubMed:15604713, ECO:0000269|PubMed:8927627,
CC ECO:0000269|PubMed:9872450}.
CC -!- INDUCTION: In roots by phosphate starvation. Repressed by the Pi analog
CC phosphite (Phi). {ECO:0000269|PubMed:12114577,
CC ECO:0000269|PubMed:12164813, ECO:0000269|PubMed:12226502,
CC ECO:0000269|PubMed:15272879, ECO:0000269|PubMed:15604713,
CC ECO:0000269|PubMed:8927627}.
CC -!- MISCELLANEOUS: Although related to the sugar transporter family, it
CC does not transport sugars.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC phosphate:H(+) symporter (TC 2.A.1.9) family. {ECO:0000305}.
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DR EMBL; U62331; AAB17266.1; -; mRNA.
DR EMBL; AF022872; AAB88291.1; -; Genomic_DNA.
DR EMBL; AB016166; BAA34398.1; -; Genomic_DNA.
DR EMBL; AC005770; AAC79607.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09615.1; -; Genomic_DNA.
DR PIR; C84811; C84811.
DR RefSeq; NP_181428.1; NM_129452.4.
DR AlphaFoldDB; Q96303; -.
DR SMR; Q96303; -.
DR BioGRID; 3818; 7.
DR STRING; 3702.AT2G38940.1; -.
DR iPTMnet; Q96303; -.
DR PaxDb; Q96303; -.
DR PRIDE; Q96303; -.
DR ProteomicsDB; 234664; -.
DR EnsemblPlants; AT2G38940.1; AT2G38940.1; AT2G38940.
DR GeneID; 818479; -.
DR Gramene; AT2G38940.1; AT2G38940.1; AT2G38940.
DR KEGG; ath:AT2G38940; -.
DR Araport; AT2G38940; -.
DR TAIR; locus:2064895; AT2G38940.
DR eggNOG; KOG0252; Eukaryota.
DR HOGENOM; CLU_001265_46_14_1; -.
DR InParanoid; Q96303; -.
DR OMA; FAPTRWR; -.
DR OrthoDB; 762280at2759; -.
DR PhylomeDB; Q96303; -.
DR PRO; PR:Q96303; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q96303; baseline and differential.
DR Genevisible; Q96303; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; ISS:TAIR.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004738; Phos_permease.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00887; 2A0109; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphate transport; Phosphoprotein;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..534
FT /note="Inorganic phosphate transporter 1-4"
FT /id="PRO_0000050471"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..70
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..131
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..211
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..349
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..403
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 425..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..484
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..534
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 512..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754, ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
SQ SEQUENCE 534 AA; 58599 MW; 8186DBBBCBC8379E CRC64;
MAREQLQVLN ALDVAKTQWY HFTAIIIAGM GFFTDAYDLF CISLVTKLLG RIYYHVEGAQ
KPGTLPPNVA AAVNGVAFCG TLAGQLFFGW LGDKLGRKKV YGMTLMVMVL CSIASGLSFG
HEPKAVMATL CFFRFWLGFG IGGDYPLSAT IMSEYANKKT RGAFVSAVFA MQGFGIMAGG
IFAIIISSAF EAKFPSPAYA DDALGSTIPQ ADLVWRIILM AGAIPAAMTY YSRSKMPETA
RYTALVAKDA KQAASDMSKV LQVEIEPEQQ KLEEISKEKS KAFGLFSKEF MSRHGLHLLG
TTSTWFLLDI AFYSQNLFQK DIFSAIGWIP PAQSMNAIQE VFKIARAQTL IALCSTVPGY
WFTVAFIDVI GRFAIQMMGF FFMTVFMFAL AIPYNHWTHK ENRIGFVIMY SLTFFFANFG
PNATTFVVPA EIFPARFRST CHGISAASGK LGAMVGAFGF LYLAQNPDKD KTDAGYPPGI
GVRNSLIVLG VVNFLGILFT FLVPESKGKS LEEMSGENED NENSNNDSRT VPIV
