PHT17_ARATH
ID PHT17_ARATH Reviewed; 535 AA.
AC Q494P0; Q9M1T0;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Probable inorganic phosphate transporter 1-7;
DE Short=AtPht1;7;
DE AltName: Full=H(+)/Pi cotransporter;
GN Name=PHT1-7; OrderedLocusNames=At3g54700; ORFNames=T5N23.60;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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] OF 50-535.
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP 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).
CC -!- FUNCTION: High-affinity transporter for external inorganic phosphate.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mature pollen. {ECO:0000269|PubMed:12164813}.
CC -!- INDUCTION: Slightly induced in roots during phosphate starvation.
CC {ECO:0000269|PubMed:12164813, ECO:0000269|PubMed:15604713}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAZ23928.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL138650; CAB77590.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79268.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63815.1; -; Genomic_DNA.
DR EMBL; BT023736; AAZ23928.1; ALT_INIT; mRNA.
DR PIR; T47629; T47629.
DR RefSeq; NP_001319749.1; NM_001339687.1.
DR RefSeq; NP_191030.3; NM_115327.3.
DR AlphaFoldDB; Q494P0; -.
DR SMR; Q494P0; -.
DR STRING; 3702.AT3G54700.1; -.
DR PaxDb; Q494P0; -.
DR PRIDE; Q494P0; -.
DR ProteomicsDB; 234665; -.
DR EnsemblPlants; AT3G54700.1; AT3G54700.1; AT3G54700.
DR EnsemblPlants; AT3G54700.2; AT3G54700.2; AT3G54700.
DR GeneID; 824635; -.
DR Gramene; AT3G54700.1; AT3G54700.1; AT3G54700.
DR Gramene; AT3G54700.2; AT3G54700.2; AT3G54700.
DR KEGG; ath:AT3G54700; -.
DR Araport; AT3G54700; -.
DR TAIR; locus:2102450; AT3G54700.
DR eggNOG; KOG0252; Eukaryota.
DR HOGENOM; CLU_001265_46_14_1; -.
DR InParanoid; Q494P0; -.
DR OMA; YKNAQQH; -.
DR OrthoDB; 762280at2759; -.
DR PhylomeDB; Q494P0; -.
DR PRO; PR:Q494P0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q494P0; baseline and differential.
DR Genevisible; Q494P0; 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; IEA:InterPro.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:1901684; P:arsenate ion transmembrane transport; IMP:TAIR.
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 2: Evidence at transcript level;
KW Membrane; Phosphate transport; Phosphoprotein; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..535
FT /note="Probable inorganic phosphate transporter 1-7"
FT /id="PRO_0000050474"
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..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..345
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..399
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 421..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..480
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..535
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 506..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96303"
FT CONFLICT 77
FT /note="A -> P (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 58333 MW; 8FA274A5413FF800 CRC64;
MAGDQLNVLN ALDVAKTQWY HFTAIIIAGM GFFTDAYDLF CISLVTKLLG RIYYHVDGSE
KPGTLPPNVS AAVNGVAFCG TLAGQLFFGW LGDKLGRKKV YGMTLMVMVL CSIASGLSFG
SNPKTVMTTL CFFRFWLGFG IGGDYPLSAT IMSEYANKKT RGAFIAAVFA MQGFGILTGG
IFAIIVSAAF EAKFPAPTYQ IDALASTVPQ ADYVWRIILM VGALPAAMTY YSRSKMPETA
RYTALVAKDA KLAASNMSKV LQVEIEAEQQ GTEDKSNSFG LFSKEFMKRH GLHLLGTTST
WFLLDIAFYS QNLFQKDIFS AIGWIPPAQT MNAIQEVFKI ARAQTLIALC STVPGYWFTV
AFIDVIGRFA IQMMGFFFMT VFMFALAIPY DHWTHKENRI GFVAMYSLTF FFANFGPNAT
TFVVPAEIFP ARFRSTCHGI SAASGKLGAM VGAFGFLYLA QSPDKTKTEH GYPPGIGVKN
SLIVLGVVNL LGMVFTLLVP ESKGKSLEEM SGENEQNDES SSSSNNNSNN AVSTA
