PHT11_ARATH
ID PHT11_ARATH Reviewed; 524 AA.
AC Q8VYM2; Q96264; Q96302;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Inorganic phosphate transporter 1-1;
DE Short=AtPht1;1;
DE AltName: Full=H(+)/Pi cotransporter;
GN Name=PHT1-1; Synonyms=APT2, PHT1, PT1; OrderedLocusNames=At5g43350;
GN ORFNames=MWF20.4;
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], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=9025304; DOI=10.1046/j.1365-313x.1997.11010083.x;
RA Smith F.W., Ealing P.M., Dong B., Delhaize E.;
RT "The cloning of two Arabidopsis genes belonging to a phosphate transporter
RT family.";
RL Plant J. 11:83-92(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=9192698; DOI=10.1073/pnas.94.13.7098;
RA Mitsukawa N., Okumura S., Shirano Y., Sato S., Kato T., Harashima S.,
RA Shibata D.;
RT "Overexpression of an Arabidopsis thaliana high-affinity phosphate
RT transporter gene in tobacco cultured cells enhances cell growth under
RT phosphate-limited conditions.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7098-7102(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP INDUCTION, TISSUE SPECIFICITY, 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 [8]
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 [9]
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 [10]
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 [11]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16233751; DOI=10.1263/jbb.99.38;
RA Koyama T., Ono T., Shimizu M., Jinbo T., Mizuno R., Tomita K.,
RA Mitsukawa N., Kawazu T., Kimura T., Ohmiya K., Sakka K.;
RT "Promoter of Arabidopsis thaliana phosphate transporter gene drives root-
RT specific expression of transgene in rice.";
RL J. Biosci. Bioeng. 99:38-42(2005).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=16284308; DOI=10.1105/tpc.105.036640;
RA Gonzalez E., Solano R., Rubio V., Leyva A., Paz-Ares J.;
RT "PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1 is a plant-specific SEC12-
RT related protein that enables the endoplasmic reticulum exit of a high-
RT affinity phosphate transporter in Arabidopsis.";
RL Plant Cell 17:3500-3512(2005).
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:8927627, ECO:0000269|PubMed:9192698}.
CC -!- ACTIVITY REGULATION: Inhibited by protonophores (e.g. 2,4-dinitrophenol
CC and carbonylcyanide m-chlorophenylhydrazone), the plasma membrane H(+)-
CC ATPase inhibitor diethylstilbestorol, and the phosphate analog
CC arsenate. {ECO:0000269|PubMed:9192698}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 uM for inorganic phosphate {ECO:0000269|PubMed:9192698};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16284308};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16284308}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, especially in
CC trichoblasts and in emerging secondary roots and root hairs, but not in
CC root tips. Also present in hydathodes, axillary buds and peripheral
CC endosperm of germinating seeds. {ECO:0000269|PubMed:12164813,
CC ECO:0000269|PubMed:12226502, ECO:0000269|PubMed:16233751,
CC ECO:0000269|PubMed:8927627, ECO:0000269|PubMed:9025304,
CC ECO:0000269|PubMed:9192698}.
CC -!- INDUCTION: In roots by phosphate starvation. Repressed by auxin,
CC cytokinins, and the Pi analog phosphite (Phi).
CC {ECO:0000269|PubMed:12114577, ECO:0000269|PubMed:12164813,
CC ECO:0000269|PubMed:12226502, ECO:0000269|PubMed:15272879,
CC ECO:0000269|PubMed:16233751, ECO:0000269|PubMed:8927627,
CC ECO:0000269|PubMed:9025304}.
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; U62330; AAB17265.1; -; mRNA.
DR EMBL; Y07682; CAA68946.1; -; Genomic_DNA.
DR EMBL; D86591; BAA21503.1; -; mRNA.
DR EMBL; D86608; BAA21504.1; -; Genomic_DNA.
DR EMBL; AB025638; BAA97414.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94948.1; -; Genomic_DNA.
DR EMBL; AY070432; AAL49927.1; -; mRNA.
DR RefSeq; NP_199149.1; NM_123701.4.
DR AlphaFoldDB; Q8VYM2; -.
DR SMR; Q8VYM2; -.
DR BioGRID; 19603; 8.
DR IntAct; Q8VYM2; 2.
DR STRING; 3702.AT5G43350.1; -.
DR TCDB; 2.A.1.9.9; the major facilitator superfamily (mfs).
DR iPTMnet; Q8VYM2; -.
DR PaxDb; Q8VYM2; -.
DR PRIDE; Q8VYM2; -.
DR ProteomicsDB; 236733; -.
DR EnsemblPlants; AT5G43350.1; AT5G43350.1; AT5G43350.
DR GeneID; 834353; -.
DR Gramene; AT5G43350.1; AT5G43350.1; AT5G43350.
DR KEGG; ath:AT5G43350; -.
DR Araport; AT5G43350; -.
DR TAIR; locus:2176461; AT5G43350.
DR eggNOG; KOG0252; Eukaryota.
DR HOGENOM; CLU_001265_46_14_1; -.
DR InParanoid; Q8VYM2; -.
DR OMA; VLFIDIM; -.
DR OrthoDB; 762280at2759; -.
DR PhylomeDB; Q8VYM2; -.
DR BioCyc; MetaCyc:MON-21678; -.
DR PRO; PR:Q8VYM2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VYM2; baseline and differential.
DR Genevisible; Q8VYM2; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:1901683; F:arsenate ion transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015114; F:phosphate ion transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:1901684; P:arsenate ion transmembrane transport; IMP:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR GO; GO:0006817; P:phosphate ion transport; IDA:TAIR.
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; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..524
FT /note="Inorganic phosphate transporter 1-1"
FT /id="PRO_0000050468"
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..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..348
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..402
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..484
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..524
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 185
FT /note="A -> T (in Ref. 6; AAL49927)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="A -> P (in Ref. 2; CAA68946)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 57616 MW; 2D12D50987127BD6 CRC64;
MAEQQLGVLK ALDVAKTQLY HFTAIVIAGM GFFTDAYDLF CVSLVTKLLG RIYYFNPESA
KPGSLPPHVA AAVNGVALCG TLSGQLFFGW LGDKLGRKKV YGLTLVMMIL CSVASGLSFG
HEAKGVMTTL CFFRFWLGFG IGGDYPLSAT IMSEYANKKT RGAFIAAVFA MQGVGILAGG
FVALAVSSIF DKKFPAPTYA VNRALSTPPQ VDYIWRIIVM FGALPAALTY YWRMKMPETA
RYTALVAKNI KQATADMSKV LQTDIELEER VEDDVKDPKQ NYGLFSKEFL RRHGLHLLGT
TSTWFLLDIA FYSQNLFQKD IFSAIGWIPK AATMNATHEV FRIARAQTLI ALCSTVPGYW
FTVAFIDTIG RFKIQLNGFF MMTVFMFAIA FPYNHWIKPE NRIGFVVMYS LTFFFANFGP
NATTFIVPAE IFPARLRSTC HGISAAAGKA GAIVGAFGFL YAAQSQDKAK VDAGYPPGIG
VKNSLIMLGV LNFIGMLFTF LVPEPKGKSL EELSGEAEVS HDEK
