PHT15_PETHY
ID PHT15_PETHY Reviewed; 529 AA.
AC B2CPI7;
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 5 {ECO:0000303|PubMed:18315538};
DE Short=PhPT5 {ECO:0000303|PubMed:18315538};
DE Short=PhPht1;5 {ECO:0000305};
DE AltName: Full=Arbuscular mycorrhiza-induced phosphate transporter PT5 {ECO:0000305};
DE Short=AM-induced phosphate transporter PT5 {ECO:0000305};
DE AltName: Full=H(+)/Pi cotransporter PT5 {ECO:0000305};
GN Name=PT5 {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], INDUCTION BY ARBUSCULAR MYCORRHIZAL
RP FUNGI, AND TISSUE SPECIFICITY.
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 during AM symbiosis.
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 -!- TISSUE SPECIFICITY: Expressed at low levels in non-mycorrhized roots.
CC {ECO:0000269|PubMed:18315538}.
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; EU532764; ACB37442.1; -; Genomic_DNA.
DR AlphaFoldDB; B2CPI7; -.
DR SMR; B2CPI7; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR GO; GO:0009610; P:response to symbiotic fungus; IEP: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 5"
FT /id="PRO_0000450039"
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..124
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 125..145
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 164..184
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..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..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 473..493
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..529
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 500..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"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 529 AA; 58914 MW; EEB9D563081BCC7A CRC64;
MASNNLNVLN ALDTAHTQWY HVTAVVIAGM GFFTDAYDLF CISTISKLLG RLYYYDPHTH
APGKLPHTVN NWVTGVALVG TLTGQLVFGW LGDKLGRKKV YGLTLILMVI CALSSGLSFG
YSRKVVIGTL CFFRFWLGFG IGGDYPLSAT IMSEYANKRT RGAFIAAVFA MQGVGIIFAG
LVLMTVSKVF LMRYAGKAFS TDEVFSTEPE ADYVWRIVLM LGALPALLTY YWRMKMPETG
RYTAIIEGNA KQAAIDMGKV LEIEIQAEGE KLAKFKSAND YSLLSNEFFQ RHGLHLIGTM
STWFLLDIAF YSQNLTQKDI FPTMGLVSDA KSISALREMF ETSRAMFVIA LLGTFPGYWF
TVFFIEKIGR FKIQLMGFFM MSIFMAIIGV RYDYLKTKDH KWTFAALYGL TFFFANSGPN
STTFVLPAEL FPTRVRSTCH ALSAASGKAG AMVSAFGVQQ YTQDGEVHKI KKAMLFLAFT
NMVGFCCTFL VTETKGRSLE EISGEDENQN ETKMKGRPVS GGHQDDGWD
