PHT14_LOTJA
ID PHT14_LOTJA Reviewed; 528 AA.
AC B5RHV8;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Low affinity inorganic phosphate transporter 4 {ECO:0000303|PubMed:19220794};
DE Short=LjPT4 {ECO:0000303|PubMed:19220794};
DE Short=LjPht1;4 {ECO:0000305};
DE AltName: Full=Arbuscular mycorrhiza-induced phosphate transporter PT4 {ECO:0000303|PubMed:19220794};
DE Short=AM-induced phosphate transporter PT4 {ECO:0000303|PubMed:19220794};
DE AltName: Full=H(+)/Pi cotransporter PT4 {ECO:0000305};
GN Name=PT4 {ECO:0000303|PubMed:19220794};
OS Lotus japonicus (Lotus corniculatus var. japonicus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX NCBI_TaxID=34305;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY GLOMEROMYCOTA
RP INTRARADICES.
RC STRAIN=cv. Miyakojima MG-20;
RX PubMed=19220794; DOI=10.1111/j.1365-313x.2009.03824.x;
RA Takeda N., Sato S., Asamizu E., Tabata S., Parniske M.;
RT "Apoplastic plant subtilases support arbuscular mycorrhiza development in
RT Lotus japonicus.";
RL Plant J. 58:766-777(2009).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND
RP INDUCTION BY ARBUSCULAR MYCORRHIZAL FUNGI.
RC STRAIN=cv. Miyakojima MG-20;
RX PubMed=26476189; DOI=10.1111/pce.12659;
RA Volpe V., Giovannetti M., Sun X.-G., Fiorilli V., Bonfante P.;
RT "The phosphate transporters LjPT4 and MtPT4 mediate early root responses to
RT phosphate status in non mycorrhizal roots.";
RL Plant Cell Environ. 39:660-671(2016).
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. Gigaspora margarita and
CC Funnelliformis mosseae) during AM symbiosis; required for propper
CC mycorrhizal arbuscule morphology (PubMed:26476189). 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 (PubMed:26476189). {ECO:0000269|PubMed:26476189}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NH4(+)(in) = NH4(+)(out); Xref=Rhea:RHEA:28747,
CC ChEBI:CHEBI:28938; Evidence={ECO:0000269|PubMed:26476189};
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 only in mycorrhizal roots, exclusively in
CC cortical cells containing arbuscules, upon arbuscular mycorrhizal (AM)
CC symbiosis with AM fungi (e.g. Gigaspora margarita and Funnelliformis
CC mosseae) (PubMed:26476189). Also observed in root tips of non-
CC mycorrhizal roots, in a phosphate (Pi) depended-manner, highest
CC expression levels being observed in low Pi conditions
CC (PubMed:26476189). {ECO:0000269|PubMed:26476189}.
CC -!- INDUCTION: Induced in roots during development of arbuscular mycorrhiza
CC (AM) upon colonization by AM fungus (e.g. Glomeromycota intraradices,
CC Gigaspora margarita and Funnelliformis mosseae) (PubMed:19220794,
CC PubMed:26476189). Induced in root tips by low phosphate (Pi) levels
CC (PubMed:26476189). {ECO:0000269|PubMed:19220794,
CC ECO:0000269|PubMed:26476189}.
CC -!- DISRUPTION PHENOTYPE: Impaired phosphate (Pi) starvation induction of
CC lateral roots formation (PubMed:26476189). Abnormal structures of
CC arbuscular mycorrhiza (AM) fungi (e.g. Gigaspora margarita and
CC Funnelliformis mosseae) during AM symbiosis with swollen main arbuscule
CC trunks and reduced branching (PubMed:26476189). Lower symbiotic Pi
CC transfer for AM fungi to the host plant (PubMed:26476189).
CC {ECO:0000269|PubMed:26476189}.
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; AP010874; BAG71408.1; -; Genomic_DNA.
DR AlphaFoldDB; B5RHV8; -.
DR SMR; B5RHV8; -.
DR OMA; QIGFAGK; -.
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:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0036377; P:arbuscular mycorrhizal association; IMP:UniProtKB.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IMP:UniProtKB.
DR GO; GO:0010247; P:detection of phosphate ion; IMP:UniProtKB.
DR GO; GO:0010311; P:lateral root formation; IMP:UniProtKB.
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 InterPro; IPR004738; Phos_permease.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00887; 2A0109; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Phosphate transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..528
FT /note="Low affinity inorganic phosphate transporter 4"
FT /id="PRO_0000450034"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 19..39
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..68
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 69..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 97..117
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..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..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 159..179
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..208
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 209..229
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..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..341
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 342..362
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..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..401
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 402..422
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 434..454
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..467
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 468..488
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 489..528
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 496..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 528 AA; 58681 MW; 7F4286DCF03C2D95 CRC64;
MALEVLEALD SARTQWYHVT AIVIAGMGFF TDAYDLFCIT TVSKLLGRLY YFDPSTGKPG
KLPNNVNNLV TGVALVGTLS GQLFFGYLGD KLGRKKVYGV TLILMVACAI CSGLSFGASA
KSVMGTLCFF RFWLGFGIGG DYPLSATIMS EYANKRTRGA FIAAVFAMQG VGIIFAGLVS
MCLSAGFKAS YHAPSFHDDP IMSTQPQGDL MWRLVLMIGA VPAAMTYYWR MKMPETGRYT
AIIEGNAKQA AADMARVLDI EIQAEQDKLA EFKAANDYPL WSNEFFTRHG RHLIGTMTSW
FLLDIAFYSQ NLTQKDIFPA MGLIDKDFEM NAIQEVFETS RAMFVIALFG TFPGYWFTVF
FIEKLGRYKI QLIGFFMMSV FMFIIGVKYD YLRNENSHMF ALLYGLTFFF ANFGPNSTTF
VLPAELFPTR VRSTCHALSA AAGKAGAMVG AFGIQNYTQK GEQKQIKHAM MILAVTNLIG
FFCSFLVTET KGRSLEEISG EDGRESELTP TPPNNRVPTR QEPRSETM
