PHT14_PETHY
ID PHT14_PETHY Reviewed; 529 AA.
AC B2CPI6;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Low affinity inorganic phosphate transporter 4 {ECO:0000303|PubMed:18315538};
DE Short=PhPT4 {ECO:0000303|PubMed:18315538};
DE Short=PhPht1;4 {ECO:0000305};
DE AltName: Full=Arbuscular mycorrhiza-induced phosphate transporter PT4 {ECO:0000305};
DE Short=AM-induced phosphate transporter PT4 {ECO:0000305};
DE AltName: Full=H(+)/Pi cotransporter PT4 {ECO:0000305};
DE AltName: Full=Protein Pi TRANSPORTER DOWN-REGULATED {ECO:0000303|PubMed:18315538};
GN Name=PT4 {ECO:0000303|PubMed:18315538};
GN Synonyms=PTD1 {ECO:0000303|PubMed:18315538};
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY ARBUSCULAR MYCORRHIZAL
RP FUNGI.
RC STRAIN=cv. W115, and cv. W138;
RX PubMed=18315538; DOI=10.1111/j.1365-313x.2008.03474.x;
RA Wegmueller S., Svistoonoff S., Reinhardt D., Stuurman J., Amrhein N.,
RA Bucher M.;
RT "A transgenic dTph1 insertional mutagenesis system for forward genetics in
RT mycorrhizal phosphate transport of Petunia.";
RL Plant J. 54:1115-1127(2008).
RN [2]
RP INDUCTION BY RAM1 AND RHIZOPHAGUS IRREGULARIS.
RC STRAIN=cv. W138;
RX PubMed=25971550; DOI=10.1104/pp.15.00310;
RA Rich M.K., Schorderet M., Bapaume L., Falquet L., Morel P.,
RA Vandenbussche M., Reinhardt D.;
RT "The Petunia GRAS transcription factor ATA/RAM1 regulates symbiotic gene
RT expression and fungal morphogenesis in arbuscular mycorrhiza.";
RL Plant Physiol. 168:788-797(2015).
CC -!- FUNCTION: Low-affinity transporter for external inorganic phosphate
CC (Pi) probably involved in the acquisition of phosphate released by
CC arbuscular mycorrhizal (AM) fungi (e.g. Rhizophagus irregularis and
CC Glomus intraradices) during AM symbiosis (Probable). Acts as a Pi-
CC sensing machinery at the root tip level, independently of AM fungi,
CC involved in the regulation of early root branching and lateral roots
CC formation (By similarity). {ECO:0000250|UniProtKB:B5RHV8,
CC ECO:0000305|PubMed:18315538}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NH4(+)(in) = NH4(+)(out); Xref=Rhea:RHEA:28747,
CC ChEBI:CHEBI:28938; Evidence={ECO:0000250|UniProtKB:Q8GSG4};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8GSG4};
CC Multi-pass membrane protein {ECO:0000255}. Note=Present on the
CC periarbuscular membrane in cells containing arbuscules during
CC arbuscular mycorrhizal (AM) symbiosis with AM fungi.
CC {ECO:0000250|UniProtKB:Q8GSG4}.
CC -!- INDUCTION: Regulated positively by RAM1 during arbuscular mycorrhiza
CC (AM) formation after inoculation with AM fungi (e.g. Rhizophagus
CC irregularis and Glomus intraradices). {ECO:0000269|PubMed:18315538,
CC ECO:0000269|PubMed:25971550}.
CC -!- MISCELLANEOUS: Although related to the sugar transporter family, it
CC does not transport sugars. {ECO:0000305}.
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; EU532763; ACB37441.1; -; Genomic_DNA.
DR AlphaFoldDB; B2CPI6; -.
DR SMR; B2CPI6; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0085042; C:periarbuscular membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0036377; P:arbuscular mycorrhizal association; IDA:UniProtKB.
DR GO; GO:0006817; P:phosphate ion transport; IDA:UniProtKB.
DR GO; GO:0009610; P:response to symbiotic fungus; IDA:UniProtKB.
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 Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Phosphate transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..529
FT /note="Low affinity inorganic phosphate transporter 4"
FT /id="PRO_0000450035"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 22..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..71
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 72..92
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 100..120
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..125
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 126..146
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 162..182
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..211
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 212..232
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 292..312
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..344
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 345..365
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 375..395
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..405
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 406..426
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 438..458
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..471
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 472..492
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..529
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 501..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 529 AA; 58875 MW; 556905E1379B741D CRC64;
MASDNLVVLN ALDTARTQWY HVTAVIIAGM GFFTDAYDLF CISTVSKLLG RLYYYDPSTK
APGKLPHMAN NWVIGVALVG TLSGQLVFGW LGDKLGRKKV YGLTLILMVI CALCSGLSLG
YSPKSVIGTL CFFRFWLGFG IGGDYPLSAT IMSEYANKST RGAFIAAVFA MQGVGIIFAG
LVSMTISKVF LMNFEGKPFN VDEVLSTEPE ADYVWRIVLM LGALPALLTY YWRMKMPETG
RYTAIIEGNA KQAAIDMGKV LDIEIQAEGD KLAQFKAANE YSLLSNEFFQ RHGLHLIGTM
STWFLLDIAF YSQNLTQKDI FPVMGLTSKA NTISALREMF ETSRAMFVIA LFGTFPGYWF
TVFFIEKIGR FKIQLVGFFM MSVFMAIIGV KYDYLRNKEH KWTFAALYGL TFFFANFGPN
STTFVLPAEL FPTRVRSTCH ALSAALGKAG AMISAFGIQQ YTQDQDVRKI KTAMLLLAFT
NMVGFCCTFL VTETKGRSLE EISGEDGRQN ETQMKTTRPV SGHPDDGWE
