ID PHT13_PETHY Reviewed; 538 AA.
AC B2CPI5;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Low affinity inorganic phosphate transporter 3 {ECO:0000303|PubMed:18315538};
DE Short=PhPT3 {ECO:0000303|PubMed:18315538};
DE Short=PhPht1;3 {ECO:0000305};
DE AltName: Full=Arbuscular mycorrhiza-induced phosphate transporter PT3 {ECO:0000305};
DE Short=AM-induced phosphate transporter PT3 {ECO:0000305};
DE AltName: Full=H(+)/Pi cotransporter PT3 {ECO:0000305};
GN Name=PT3 {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).
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=H(+)(in) + phosphate(in) = H(+)(out) + phosphate(out);
CC Xref=Rhea:RHEA:29939, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000250|UniProtKB:Q8GSG4};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29941;
CC 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: Accumulates during arbuscular mycorrhiza (AM) formation
CC after inoculation with AM fungi (e.g. Glomus intraradices).
CC {ECO:0000269|PubMed:18315538}.
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; EU532762; ACB37440.1; -; Genomic_DNA.
DR AlphaFoldDB; B2CPI5; -.
DR SMR; B2CPI5; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro.
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 CDD; cd17364; MFS_PhT; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 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 NCBIfam; TIGR00887; 2A0109; 1.
DR PANTHER; PTHR24064:SF556; INORGANIC PHOSPHATE TRANSPORTER 1-4-LIKE; 1.
DR PANTHER; PTHR24064; SOLUTE CARRIER FAMILY 22 MEMBER; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Phosphate transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..538
FT /note="Low affinity inorganic phosphate transporter 3"
FT /id="PRO_0000450038"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 25..45
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..70
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 71..91
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..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..122
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 123..143
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 165..185
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..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..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 293..313
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..345
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 346..366
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 372..392
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..402
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 403..423
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 443..463
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..483
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 484..504
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 506..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 58723 MW; DA642FABE29BC4E9 CRC64;
MAKDQLQVLN ALDVAKTQLY HFTAIVIAGM GFFTDAYDLF CISLVTKLLG RIYYFHEGAP
KPGILPSGIS AAVNGVAFIG TLSGQLFFGW LGDKLGRKKV YGMTLMLMVI CSIACGLSFG
KTANGVIATL CFFRFWLGFG IGGDYPLSAT IMSEYANKKT RGAFIAAVFA MQGFGILAGG
IVALIVSAGF KNAYPAPTYS AHGKDSTPPE ADYVWRIIVM IGALPALLTY YWRMKMPETA
RYTALVAKNT VKAAADMSKV LNVEIEEDKA TVEKIEENGN SFGLFSKEFL RRHGLHLLGT
TSTWFLLDIA FYSQNLFQKD IFSKIGWIPP PETMNALDEV FRIARAQTLI ALCSTVPGYW
FTVAFIDKMG RFAIQLMGSF FMTVFMFALA IPYDHWTKKE NRIGFVIMYS LTFFFANFGP
NATTFVVPAE IFPARLRSTC HGISAAAGKA GAIVGAFGFL YAAQSTDPKK VDAGYPTGIG
VKNALIVLGC VNFLGMLSTL LVPESKGKSL EEMSKENEGE EENYGTETKG ENAQTVPV
//
