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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
 
 
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