PHT16_ARATH
ID PHT16_ARATH Reviewed; 516 AA.
AC Q9ZWT3;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Probable inorganic phosphate transporter 1-6;
DE Short=AtPht1;6;
DE AltName: Full=H(+)/Pi cotransporter;
GN Name=PHT1-6; Synonyms=PHT6; OrderedLocusNames=At5g43340; ORFNames=MWF20.3;
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 [GENOMIC DNA].
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 [2]
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 [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 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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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: Expressed in anthers, tapetumand mature pollen and,
CC to a lower extent, in hydathodes and vascular tissues of cotyledons of
CC flowering plants. {ECO:0000269|PubMed:12164813}.
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; AB005746; BAA34390.1; -; Genomic_DNA.
DR EMBL; AB025638; BAA97413.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94947.1; -; Genomic_DNA.
DR RefSeq; NP_199148.1; NM_123700.1.
DR AlphaFoldDB; Q9ZWT3; -.
DR SMR; Q9ZWT3; -.
DR BioGRID; 19602; 1.
DR STRING; 3702.AT5G43340.1; -.
DR iPTMnet; Q9ZWT3; -.
DR PaxDb; Q9ZWT3; -.
DR PRIDE; Q9ZWT3; -.
DR ProteomicsDB; 235084; -.
DR EnsemblPlants; AT5G43340.1; AT5G43340.1; AT5G43340.
DR GeneID; 834352; -.
DR Gramene; AT5G43340.1; AT5G43340.1; AT5G43340.
DR KEGG; ath:AT5G43340; -.
DR Araport; AT5G43340; -.
DR TAIR; locus:2176451; AT5G43340.
DR eggNOG; KOG0252; Eukaryota.
DR HOGENOM; CLU_001265_46_14_1; -.
DR InParanoid; Q9ZWT3; -.
DR OMA; FAKNDQA; -.
DR OrthoDB; 762280at2759; -.
DR PhylomeDB; Q9ZWT3; -.
DR PRO; PR:Q9ZWT3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9ZWT3; baseline and differential.
DR Genevisible; Q9ZWT3; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00887; 2A0109; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Phosphate transport; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..516
FT /note="Probable inorganic phosphate transporter 1-6"
FT /id="PRO_0000050473"
FT TOPO_DOM 2..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..71
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..132
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..212
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..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..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..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..471
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..516
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 516 AA; 56247 MW; 97B2BEFEA894A145 CRC64;
MANEEQGSIL KALDVAKTQW YHVTAVVVSG MGFFTDSYDL FVISLITKLL GRIYYQVPGS
SSPGSLPDGI SAAVSGVAFA GTFIGQIFFG CLGDKLGRKR VYGLTLLIMT ICSICSGLSL
GRDPKTVMVT LCFFRFWLGF GIGGDYPLSA TIMSEYSNKR TRGAFIAAVF GMQGIGILAA
GAVSLLVSAV FESKFPSRAY ILDGAASTVP QADYVWRIIL MVGALPALLT YYWRMKMPET
ARYTALVSKN AEQAALDMTK VLNVDIEASA AKNDQARVSS DEFGLFSMKF LRRHGLHLLG
TASTWFLLDI AFYSQNLFQK DIFTTIGWLP SAKTMNAIQE LYMIAKAQTI IACCSTVPGY
FFTVGFIDYM GRKKIQIMGF AMMTIFMLSL AIPYHHWTLP ANRIGFVVLY SFTFFFSNFG
PNATTFIVPA EIFPARIRST CHGISAASGK AGAMVGSFGF SALVKALGMS NTLYIMAGIN
LLGLLLTFTI PETNGKSLEE LSGETEPEKI KEKIVV
