PHO1_ARATH
ID PHO1_ARATH Reviewed; 782 AA.
AC Q8S403; Q9LW54;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Phosphate transporter PHO1 {ECO:0000303|PubMed:11971143};
DE AltName: Full=Protein PHO1 {ECO:0000303|PubMed:11971143};
DE Short=AtPHO1 {ECO:0000303|PubMed:11971143};
GN Name=PHO1 {ECO:0000303|PubMed:11971143};
GN OrderedLocusNames=At3g23430 {ECO:0000312|Araport:AT3G23430};
GN ORFNames=MLM24.26 {ECO:0000312|EMBL:BAB02287.1};
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 DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=11971143; DOI=10.1105/tpc.000745;
RA Hamburger D., Rezzonico E., MacDonald-Comber Petetot J., Somerville C.,
RA Poirier Y.;
RT "Identification and characterization of the Arabidopsis PHO1 gene involved
RT in phosphate loading to the xylem.";
RL Plant Cell 14:889-902(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17461783; DOI=10.1111/j.1365-313x.2007.03108.x;
RA Stefanovic A., Ribot C., Rouached H., Wang Y., Chong J., Belbahri L.,
RA Delessert S., Poirier Y.;
RT "Members of the PHO1 gene family show limited functional redundancy in
RT phosphate transfer to the shoot, and are regulated by phosphate deficiency
RT via distinct pathways.";
RL Plant J. 50:982-994(2007).
RN [5]
RP INDUCTION.
RX PubMed=18094993; DOI=10.1007/s00425-007-0677-x;
RA Ribot C., Wang Y., Poirier Y.;
RT "Expression analyses of three members of the AtPHO1 family reveal
RT differential interactions between signaling pathways involved in phosphate
RT deficiency and the responses to auxin, cytokinin, and abscisic acid.";
RL Planta 227:1025-1036(2008).
RN [6]
RP FUNCTION.
RX PubMed=21309867; DOI=10.1111/j.1365-313x.2011.04532.x;
RA Stefanovic A., Arpat A.B., Bligny R., Gout E., Vidoudez C., Bensimon M.,
RA Poirier Y.;
RT "Over-expression of PHO1 in Arabidopsis leaves reveals its role in
RT mediating phosphate efflux.";
RL Plant J. 66:689-699(2011).
RN [7]
RP INTERACTION WITH PHO2, MUTAGENESIS OF GLU-15 AND ALA-312, SUBCELLULAR
RP LOCATION, AND DEGRADATION.
RX PubMed=22634761; DOI=10.1105/tpc.112.096636;
RA Liu T.Y., Huang T.K., Tseng C.Y., Lai Y.S., Lin S.I., Lin W.Y., Chen J.W.,
RA Chiou T.J.;
RT "PHO2-dependent degradation of PHO1 modulates phosphate homeostasis in
RT Arabidopsis.";
RL Plant Cell 24:2168-2183(2012).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22449068; DOI=10.1111/j.1365-313x.2012.05004.x;
RA Arpat A.B., Magliano P., Wege S., Rouached H., Stefanovic A., Poirier Y.;
RT "Functional expression of PHO1 to the Golgi and trans-Golgi network and its
RT role in export of inorganic phosphate.";
RL Plant J. 71:479-491(2012).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY ABSCISIC ACID.
RX PubMed=22612335; DOI=10.1111/j.1365-313x.2012.05058.x;
RA Zimmerli C., Ribot C., Vavasseur A., Bauer H., Hedrich R., Poirier Y.;
RT "PHO1 expression in guard cells mediates the stomatal response to abscisic
RT acid in Arabidopsis.";
RL Plant J. 72:199-211(2012).
RN [10]
RP INDUCTION BY WRKY6 AND WRKY42.
RX PubMed=25733771; DOI=10.1104/pp.114.253799;
RA Su T., Xu Q., Zhang F.C., Chen Y., Li L.Q., Wu W.H., Chen Y.F.;
RT "WRKY42 modulates phosphate homeostasis through regulating phosphate
RT translocation and acquisition in Arabidopsis.";
RL Plant Physiol. 167:1579-1591(2015).
RN [11]
RP TOPOLOGY, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=26546667; DOI=10.1104/pp.15.00975;
RA Wege S., Khan G.A., Jung J.Y., Vogiatzaki E., Pradervand S., Aller I.,
RA Meyer A.J., Poirier Y.;
RT "The EXS Domain of PHO1 Participates in the Response of Shoots to Phosphate
RT Deficiency via a Root-to-Shoot Signal.";
RL Plant Physiol. 170:385-400(2016).
RN [12]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF 1-MET--GLU-15; TYR-23; LYS-27;
RP LYS-136; LYS-315; LYS-318; LYS-319 AND LYS-322.
RX PubMed=27080106; DOI=10.1126/science.aad9858;
RA Wild R., Gerasimaite R., Jung J.Y., Truffault V., Pavlovic I., Schmidt A.,
RA Saiardi A., Jessen H.J., Poirier Y., Hothorn M., Mayer A.;
RT "Control of eukaryotic phosphate homeostasis by inositol polyphosphate
RT sensor domains.";
RL Science 352:986-990(2016).
CC -!- FUNCTION: Inositol polyphosphate sensor that associates with
CC transcription factors to regulate inorganic phosphate (Pi) starvation
CC responses (PubMed:27080106). Probably acts by binding inositol
CC polyphosphate via its SPX domain (PubMed:27080106). Acts as a Pi
CC exporter, mediating efflux of Pi out of cells (PubMed:21309867,
CC PubMed:22449068). Transfers Pi from the epidermal and cortical cells to
CC the root xylem vessels (PubMed:11971143). Involved in the transfer of
CC Pi from roots to shoots (PubMed:11971143, PubMed:17461783). Involved in
CC abscisic acid (ABA) induction of stomatal closure and ABA repression of
CC stomatal opening (PubMed:22612335). {ECO:0000269|PubMed:11971143,
CC ECO:0000269|PubMed:17461783, ECO:0000269|PubMed:21309867,
CC ECO:0000269|PubMed:22449068, ECO:0000269|PubMed:22612335,
CC ECO:0000269|PubMed:27080106}.
CC -!- SUBUNIT: Interacts with PHO2. {ECO:0000269|PubMed:22634761}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:22449068, ECO:0000269|PubMed:22634761,
CC ECO:0000269|PubMed:26546667}; Multi-pass membrane protein
CC {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:22449068, ECO:0000269|PubMed:26546667}; Multi-pass
CC membrane protein {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22634761}; Multi-pass membrane protein
CC {ECO:0000305}. Note=In transgenic plants, relocates partially to the
CC plasma membrane in the presence of high extracellular Pi.
CC {ECO:0000269|PubMed:22449068}.
CC -!- TISSUE SPECIFICITY: Predominantly in roots, but also weak expression in
CC the lower part of the hypocotyl (PubMed:11971143). In the stellar
CC cells, including the pericycle and xylem parenchyma cells, but not in
CC the cortical or epidermal cells (PubMed:11971143). Expressed in guard
CC cells (PubMed:22612335). {ECO:0000269|PubMed:11971143,
CC ECO:0000269|PubMed:22612335}.
CC -!- INDUCTION: Up-regulated by sucrose and Pi deficiency in roots
CC (PubMed:18094993). Down-regulated by auxin, cytokinin and abscisic acid
CC (ABA) (PubMed:18094993). Up-regulated in leaves following treatment
CC with ABA (PubMed:22612335). Down-regulated by the transcription factors
CC WRKY6 and WRKY42 (PubMed:25733771). {ECO:0000269|PubMed:18094993,
CC ECO:0000269|PubMed:25733771}.
CC -!- DOMAIN: The EXS domain is essential for Pi efflux out of cells and is
CC necessary for the endomembrane localization.
CC {ECO:0000269|PubMed:26546667}.
CC -!- DOMAIN: The SPX domain provides a basic binding surface for inositol
CC polyphosphate signaling molecules (PubMed:27080106).
CC -!- PTM: PHO1 degradation is PHO2 dependent and involves multivesicular
CC body-mediated vacuolar proteolysis (PubMed:22634761).
CC {ECO:0000269|PubMed:22634761}.
CC -!- DISRUPTION PHENOTYPE: Strong reduction in plant size and biomass.
CC Severe deficiency in shoot Pi level, but normal root Pi content.
CC {ECO:0000269|PubMed:11971143, ECO:0000269|PubMed:17461783}.
CC -!- MISCELLANEOUS: Pi content in shoot of pho1 mutant can be restored to
CC wild-type levels after treatment with cytokinins.
CC -!- SIMILARITY: Belongs to the SYG1 (TC 2.A.94) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02287.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF474076; AAM09652.1; -; mRNA.
DR EMBL; AB015474; BAB02287.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76764.1; -; Genomic_DNA.
DR RefSeq; NP_188985.2; NM_113246.5.
DR AlphaFoldDB; Q8S403; -.
DR BioGRID; 7256; 4.
DR STRING; 3702.AT3G23430.1; -.
DR TCDB; 2.A.94.1.1; the phosphate permease (pho1) family.
DR iPTMnet; Q8S403; -.
DR PaxDb; Q8S403; -.
DR PRIDE; Q8S403; -.
DR ProteomicsDB; 236351; -.
DR EnsemblPlants; AT3G23430.1; AT3G23430.1; AT3G23430.
DR GeneID; 821924; -.
DR Gramene; AT3G23430.1; AT3G23430.1; AT3G23430.
DR KEGG; ath:AT3G23430; -.
DR Araport; AT3G23430; -.
DR TAIR; locus:2090930; AT3G23430.
DR eggNOG; KOG1162; Eukaryota.
DR HOGENOM; CLU_006116_2_0_1; -.
DR InParanoid; Q8S403; -.
DR OMA; GNWTEAR; -.
DR OrthoDB; 536327at2759; -.
DR PhylomeDB; Q8S403; -.
DR PRO; PR:Q8S403; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8S403; baseline and differential.
DR Genevisible; Q8S403; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; IDA:UniProtKB.
DR GO; GO:0015114; F:phosphate ion transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR GO; GO:0048016; P:inositol phosphate-mediated signaling; IMP:UniProtKB.
DR GO; GO:0006817; P:phosphate ion transport; IBA:GO_Central.
DR GO; GO:0006799; P:polyphosphate biosynthetic process; IMP:UniProtKB.
DR CDD; cd14476; SPX_PHO1_like; 1.
DR InterPro; IPR004342; EXS_C.
DR InterPro; IPR034092; PHO1_SPX.
DR InterPro; IPR004331; SPX_dom.
DR Pfam; PF03124; EXS; 1.
DR Pfam; PF03105; SPX; 1.
DR PROSITE; PS51380; EXS; 1.
DR PROSITE; PS51382; SPX; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Golgi apparatus; Membrane; Phosphate transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..782
FT /note="Phosphate transporter PHO1"
FT /id="PRO_0000058403"
FT TOPO_DOM 1..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26546667"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..423
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..506
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 528..593
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26546667"
FT TRANSMEM 594..614
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 615..619
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:26546667"
FT TRANSMEM 620..639
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 640..782
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26546667"
FT DOMAIN 2..334
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT DOMAIN 591..782
FT /note="EXS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00712"
FT REGION 165..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..322
FT /note="Important for inositol polyphosphate binding"
FT /evidence="ECO:0000250|UniProtKB:P43585"
FT COMPBIAS 172..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 23
FT /note="Important for inositol polyphosphate binding"
FT /evidence="ECO:0000250|UniProtKB:P43585"
FT SITE 27
FT /note="Important for inositol polyphosphate binding"
FT /evidence="ECO:0000250|UniProtKB:P43585"
FT MUTAGEN 1..15
FT /note="Missing: Decreased Pi content and reduced growth."
FT /evidence="ECO:0000269|PubMed:27080106"
FT MUTAGEN 15
FT /note="E->K: In pho1-5; disruption of Pi accumulation."
FT /evidence="ECO:0000269|PubMed:22634761"
FT MUTAGEN 23
FT /note="Y->F: In PBC; decreased Pi content and reduced
FT growth; when associated with A-27 and A-319."
FT /evidence="ECO:0000269|PubMed:27080106"
FT MUTAGEN 27
FT /note="K->A: In PBC; decreased Pi content and reduced
FT growth; when associated with F-23 and A-319."
FT /evidence="ECO:0000269|PubMed:27080106"
FT MUTAGEN 136
FT /note="K->A: No effect on Pi content and growth."
FT /evidence="ECO:0000269|PubMed:27080106"
FT MUTAGEN 312
FT /note="A->T: In pho1-6; disruptionDisruption of Pi
FT accumulation."
FT /evidence="ECO:0000269|PubMed:22634761"
FT MUTAGEN 315
FT /note="K->A: In KSC; decreased Pi content and reduced
FT growth; when associated with A-318 and A-322."
FT /evidence="ECO:0000269|PubMed:27080106"
FT MUTAGEN 318
FT /note="K->A: In KSC; decreased Pi content and reduced
FT growth; when associated with A-315 and A-322."
FT /evidence="ECO:0000269|PubMed:27080106"
FT MUTAGEN 319
FT /note="K->A: In PBC; decreased Pi content and reduced
FT growth; when associated with F-23 and A-27."
FT /evidence="ECO:0000269|PubMed:27080106"
FT MUTAGEN 322
FT /note="K->A: In KSC; decreased Pi content and reduced
FT growth; when associated with A-315 and A-318."
FT /evidence="ECO:0000269|PubMed:27080106"
SQ SEQUENCE 782 AA; 90537 MW; EC49F6794EEAB96C CRC64;
MVKFSKELEA QLIPEWKEAF VNYCLLKKQI KKIKTSRKPK PASHYPIGHH SDFGRSLFDP
VRKLARTFSD KLFSNSEKPE ILQVRRRRGS SETGDDVDEI YQTELVQLFS EEDEVKVFFA
RLDEELNKVN QFHKPKETEF LERGEILKKQ LETLAELKQI LSDRKKRNLS GSNSHRSFSS
SVRNSDFSAG SPGELSEIQS ETSRTDEIIE ALERNGVSFI NSATRSKTKG GKPKMSLRVD
IPDAVAGAEG GIARSIATAM SVLWEELVNN PRSDFTNWKN IQSAEKKIRS AFVELYRGLG
LLKTYSSLNM IAFTKIMKKF DKVAGQNASS TYLKVVKRSQ FISSDKVVRL MDEVESIFTK
HFANNDRKKA MKFLKPHQTK DSHMVTFFVG LFTGCFISLF VIYIILAHLS GIFTSSDQVS
YLETVYPVFS VFALLSLHMF MYGCNLYMWK NTRINYTFIF EFAPNTALRY RDAFLMGTTF
MTSVVAAMVI HLILRASGFS ASQVDTIPGI LLLIFICVLI CPFNTFYRPT RFCFIRILRK
IVCSPFYKVL MVDFFMGDQL TSQIPLLRHL ETTGCYFLAQ SFKTHEYNTC KNGRYYREFA
YLISFLPYFW RAMQCVRRWW DESNPDHLIN MGKYVSAMVA AGVRITYARE NNDLWLTMVL
VSSVVATIYQ LYWDFVKDWG LLNPKSKNPW LRDNLVLRNK NFYYLSIALN LVLRVAWIET
IMRFRVSPVQ SHLLDFFLAS LEVIRRGHWN FYRVENEHLN NVGQFRAVKT VPLPFLDRDS
DG
