Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Inorganic phosphate transporter 1-4

Gene

PHT1-4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

High-affinity transporter for external inorganic phosphate. Acts as a H+:phosphate symporter in both low- and high-Pi conditions. Confers sensitivity to arsenate.3 Publications

GO - Molecular functioni

GO - Biological processi

  • phosphate ion transport Source: UniProtKB-KW
  • response to abscisic acid Source: TAIR
Complete GO annotation...

Keywords - Biological processi

Phosphate transport, Symport, Transport

Enzyme and pathway databases

BioCyciARA:GQT-2244-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Inorganic phosphate transporter 1-4
Short name:
AtPht1;4
Alternative name(s):
H(+)/Pi cotransporter
Gene namesi
Name:PHT1-4
Synonyms:PHT4, PT2
Ordered Locus Names:At2g38940
ORF Names:T7F6.11
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G38940.

Subcellular locationi

  • Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2424CytoplasmicSequence analysisAdd
BLAST
Transmembranei25 – 4521HelicalSequence analysisAdd
BLAST
Topological domaini46 – 7025ExtracellularSequence analysisAdd
BLAST
Transmembranei71 – 9121HelicalSequence analysisAdd
BLAST
Topological domaini92 – 998CytoplasmicSequence analysis
Transmembranei100 – 12021HelicalSequence analysisAdd
BLAST
Topological domaini121 – 13111ExtracellularSequence analysisAdd
BLAST
Transmembranei132 – 15221HelicalSequence analysisAdd
BLAST
Topological domaini153 – 1619CytoplasmicSequence analysis
Transmembranei162 – 18221HelicalSequence analysisAdd
BLAST
Topological domaini183 – 21129ExtracellularSequence analysisAdd
BLAST
Transmembranei212 – 23221HelicalSequence analysisAdd
BLAST
Topological domaini233 – 29361CytoplasmicSequence analysisAdd
BLAST
Transmembranei294 – 31421HelicalSequence analysisAdd
BLAST
Topological domaini315 – 34935ExtracellularSequence analysisAdd
BLAST
Transmembranei350 – 37021HelicalSequence analysisAdd
BLAST
Topological domaini371 – 3722CytoplasmicSequence analysis
Transmembranei373 – 39321HelicalSequence analysisAdd
BLAST
Topological domaini394 – 40310ExtracellularSequence analysis
Transmembranei404 – 42421HelicalSequence analysisAdd
BLAST
Topological domaini425 – 44218CytoplasmicSequence analysisAdd
BLAST
Transmembranei443 – 46321HelicalSequence analysisAdd
BLAST
Topological domaini464 – 48421ExtracellularSequence analysisAdd
BLAST
Transmembranei485 – 50521HelicalSequence analysisAdd
BLAST
Topological domaini506 – 53429CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • Golgi apparatus Source: TAIR
  • integral component of plasma membrane Source: GO_Central
  • membrane Source: TAIR
  • nucleus Source: TAIR
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 534534Inorganic phosphate transporter 1-4PRO_0000050471Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei524 – 5241PhosphoserineCombined sources
Modified residuei528 – 5281PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ96303.
PRIDEiQ96303.

PTM databases

iPTMnetiQ96303.

Expressioni

Tissue specificityi

Mostly expressed in roots, in tissues connecting the lateral roots to the primary root. Also present in flowers, in senescing anther filaments and in the abscission zone at the base of siliques. Expressed in hydathodes and axillary buds, and in some senescing leaves. After Pi starvation, localized in all cells of undifferentiated root segments, including root tips and root hairs, and in the epidermis, cortex and stellar regions of mature root segments.5 Publications

Inductioni

In roots by phosphate starvation. Repressed by the Pi analog phosphite (Phi).6 Publications

Gene expression databases

GenevisibleiQ96303. AT.

Interactioni

Protein-protein interaction databases

BioGridi3818. 2 interactions.
STRINGi3702.AT2G38940.1.

Structurei

3D structure databases

ProteinModelPortaliQ96303.
SMRiQ96303. Positions 25-513.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0252. Eukaryota.
ENOG410ZVN7. LUCA.
HOGENOMiHOG000171120.
InParanoidiQ96303.
KOiK08176.
OMAiGNMILSV.
PhylomeDBiQ96303.

Family and domain databases

InterProiIPR020846. MFS_dom.
IPR005828. MFS_sugar_transport_like.
IPR004738. Phos_permease.
[Graphical view]
PfamiPF00083. Sugar_tr. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 1 hit.
TIGRFAMsiTIGR00887. 2A0109. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96303-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAREQLQVLN ALDVAKTQWY HFTAIIIAGM GFFTDAYDLF CISLVTKLLG
60 70 80 90 100
RIYYHVEGAQ KPGTLPPNVA AAVNGVAFCG TLAGQLFFGW LGDKLGRKKV
110 120 130 140 150
YGMTLMVMVL CSIASGLSFG HEPKAVMATL CFFRFWLGFG IGGDYPLSAT
160 170 180 190 200
IMSEYANKKT RGAFVSAVFA MQGFGIMAGG IFAIIISSAF EAKFPSPAYA
210 220 230 240 250
DDALGSTIPQ ADLVWRIILM AGAIPAAMTY YSRSKMPETA RYTALVAKDA
260 270 280 290 300
KQAASDMSKV LQVEIEPEQQ KLEEISKEKS KAFGLFSKEF MSRHGLHLLG
310 320 330 340 350
TTSTWFLLDI AFYSQNLFQK DIFSAIGWIP PAQSMNAIQE VFKIARAQTL
360 370 380 390 400
IALCSTVPGY WFTVAFIDVI GRFAIQMMGF FFMTVFMFAL AIPYNHWTHK
410 420 430 440 450
ENRIGFVIMY SLTFFFANFG PNATTFVVPA EIFPARFRST CHGISAASGK
460 470 480 490 500
LGAMVGAFGF LYLAQNPDKD KTDAGYPPGI GVRNSLIVLG VVNFLGILFT
510 520 530
FLVPESKGKS LEEMSGENED NENSNNDSRT VPIV
Length:534
Mass (Da):58,599
Last modified:February 1, 1997 - v1
Checksum:i8186DBBBCBC8379E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62331 mRNA. Translation: AAB17266.1.
AF022872 Genomic DNA. Translation: AAB88291.1.
AB016166 Genomic DNA. Translation: BAA34398.1.
AC005770 Genomic DNA. Translation: AAC79607.1.
CP002685 Genomic DNA. Translation: AEC09615.1.
PIRiC84811.
RefSeqiNP_181428.1. NM_129452.3.
UniGeneiAt.255.
At.67089.

Genome annotation databases

EnsemblPlantsiAT2G38940.1; AT2G38940.1; AT2G38940.
GeneIDi818479.
GrameneiAT2G38940.1; AT2G38940.1; AT2G38940.
KEGGiath:AT2G38940.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62331 mRNA. Translation: AAB17266.1.
AF022872 Genomic DNA. Translation: AAB88291.1.
AB016166 Genomic DNA. Translation: BAA34398.1.
AC005770 Genomic DNA. Translation: AAC79607.1.
CP002685 Genomic DNA. Translation: AEC09615.1.
PIRiC84811.
RefSeqiNP_181428.1. NM_129452.3.
UniGeneiAt.255.
At.67089.

3D structure databases

ProteinModelPortaliQ96303.
SMRiQ96303. Positions 25-513.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi3818. 2 interactions.
STRINGi3702.AT2G38940.1.

PTM databases

iPTMnetiQ96303.

Proteomic databases

PaxDbiQ96303.
PRIDEiQ96303.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G38940.1; AT2G38940.1; AT2G38940.
GeneIDi818479.
GrameneiAT2G38940.1; AT2G38940.1; AT2G38940.
KEGGiath:AT2G38940.

Organism-specific databases

TAIRiAT2G38940.

Phylogenomic databases

eggNOGiKOG0252. Eukaryota.
ENOG410ZVN7. LUCA.
HOGENOMiHOG000171120.
InParanoidiQ96303.
KOiK08176.
OMAiGNMILSV.
PhylomeDBiQ96303.

Enzyme and pathway databases

BioCyciARA:GQT-2244-MONOMER.

Miscellaneous databases

PROiQ96303.

Gene expression databases

GenevisibleiQ96303. AT.

Family and domain databases

InterProiIPR020846. MFS_dom.
IPR005828. MFS_sugar_transport_like.
IPR004738. Phos_permease.
[Graphical view]
PfamiPF00083. Sugar_tr. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 1 hit.
TIGRFAMsiTIGR00887. 2A0109. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Phosphate transporters from the higher plant Arabidopsis thaliana."
    Muchhal U.S., Pardo J.M., Raghothama K.G.
    Proc. Natl. Acad. Sci. U.S.A. 93:10519-10523(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION.
    Strain: cv. Columbia.
    Tissue: Root.
  2. "Cloning of Arabidopsis thaliana phosphate transporter gene, AtPT2."
    Mukatira U.T., Muchhal U.S., Raghothama K.G.
    Plant Gene Register PGR97-163
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Landsberg erecta.
  3. "Phosphate transporter gene family of Arabidopsis thaliana."
    Okumura S., Mitsukawa N., Shirano Y., Shibata D.
    DNA Res. 5:261-269(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    Strain: cv. Columbia.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. "Expression analysis suggests novel roles for members of the Pht1 family of phosphate transporters in Arabidopsis."
    Mudge S.R., Rae A.L., Diatloff E., Smith F.W.
    Plant J. 31:341-353(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, NOMENCLATURE.
  7. "Phosphite, an analog of phosphate, suppresses the coordinated expression of genes under phosphate starvation."
    Varadarajan D.K., Karthikeyan A.S., Matilda P.D., Raghothama K.G.
    Plant Physiol. 129:1232-1240(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. Cited for: TISSUE SPECIFICITY, INDUCTION.
  9. "Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry."
    Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.
    Mol. Cell. Proteomics 2:1234-1243(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. La-0.
  10. "Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database."
    Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.
    Plant Cell 16:2394-2405(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Phosphate transport in Arabidopsis: Pht1;1 and Pht1;4 play a major role in phosphate acquisition from both low- and high-phosphate environments."
    Shin H., Shin H.-S., Dewbre G.R., Harrison M.J.
    Plant J. 39:629-642(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  12. "Transcriptional regulation and functional properties of Arabidopsis Pht1;4, a high affinity transporter contributing greatly to phosphate uptake in phosphate deprived plants."
    Misson J., Thibaud M.-C., Bechtold N., Raghothama K., Nussaume L.
    Plant Mol. Biol. 55:727-741(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Root.
  14. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524 AND SER-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.

Entry informationi

Entry nameiPHT14_ARATH
AccessioniPrimary (citable) accession number: Q96303
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: February 1, 1997
Last modified: February 17, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Although related to the sugar transporter family, it does not transport sugars.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.