PHT18_MEDTR
ID PHT18_MEDTR Reviewed; 557 AA.
AC G7KDA1;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Low affinity inorganic phosphate transporter 8 {ECO:0000303|PubMed:25841038};
DE Short=MtPT8 {ECO:0000303|PubMed:25841038};
DE Short=MtPht1;8 {ECO:0000305};
DE AltName: Full=Arbuscular mycorrhiza-induced phosphate transporter PT8 {ECO:0000305};
DE Short=AM-induced phosphate transporter PT8 {ECO:0000305};
DE AltName: Full=H(+)/Pi cotransporter PT8 {ECO:0000305};
GN Name=PT8 {ECO:0000303|PubMed:25841038};
GN OrderedLocusNames=MTR_5g068140 {ECO:0000312|EMBL:AES98403.1};
GN ORFNames=MtrunA17_Chr5g0428481 {ECO:0000312|EMBL:RHN56345.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F.,
RA De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K.,
RA Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H.,
RA Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M.,
RA Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N.,
RA Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M.,
RA Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J.,
RA Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H.,
RA Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J.,
RA Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C.,
RA O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F.,
RA Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O.,
RA Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R.,
RA Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B.,
RA Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17;
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=30397259; DOI=10.1038/s41477-018-0286-7;
RA Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S.,
RA Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M.,
RA Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W.,
RA Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F.,
RA Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F.,
RA Benhamed M., Crespi M., Gouzy J., Gamas P.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 4:1017-1025(2018).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, INDUCTION BY ARBUSCULAR
RP MYCORRHIZAL FUNGI, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Jemalong A17;
RX PubMed=25841038; DOI=10.1105/tpc.114.131144;
RA Breuillin-Sessoms F., Floss D.S., Gomez S.K., Pumplin N., Ding Y.,
RA Levesque-Tremblay V., Noar R.D., Daniels D.A., Bravo A., Eaglesham J.B.,
RA Benedito V.A., Udvardi M.K., Harrison M.J.;
RT "Suppression of arbuscule degeneration in Medicago truncatula phosphate
RT transporter4 mutants is dependent on the ammonium transporter 2 family
RT protein AMT2;3.";
RL Plant Cell 27:1352-1366(2015).
CC -!- FUNCTION: Low-affinity transporter for external inorganic phosphate
CC (Pi) that may be involved in the acquisition of phosphate released by
CC arbuscular mycorrhizal (AM) fungi (e.g. Glomus versiforme and
CC G.intraradices) during AM symbiosis; not required for mycorrhizal
CC arbuscule development. {ECO:0000269|PubMed:25841038}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NH4(+)(in) = NH4(+)(out); Xref=Rhea:RHEA:28747,
CC ChEBI:CHEBI:28938; Evidence={ECO:0000269|PubMed:25841038};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25841038};
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:0000269|PubMed:25841038}.
CC -!- DEVELOPMENTAL STAGE: During arbuscular mycorrhizal (AM) symbiosis with
CC AM fungi, accumulates exclusively in cortical cells harboring
CC arbuscules. {ECO:0000269|PubMed:25841038}.
CC -!- INDUCTION: Accumulates in roots during colonization by arbuscular
CC mycorrhizal (AM) fungi (e.g. Glomus versiforme).
CC {ECO:0000269|PubMed:25841038}.
CC -!- DISRUPTION PHENOTYPE: Normal arbuscular mycorrhizal (AM) symbiosis with
CC AM fungi (PubMed:25841038). Plants missing both PT4 and PT8 fail to
CC establish AM symbiosis with AM fungi in high nitrogen conditions,
CC leading to premature arbuscule degeneration (PAD); these phenotypes are
CC suppressed in nitrogen-deprived conditions in an AMT2-3-dependent
CC manner (PubMed:25841038). {ECO:0000269|PubMed:25841038}.
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; CM001221; AES98403.1; -; Genomic_DNA.
DR EMBL; PSQE01000005; RHN56345.1; -; Genomic_DNA.
DR RefSeq; XP_003615445.1; XM_003615397.1.
DR AlphaFoldDB; G7KDA1; -.
DR SMR; G7KDA1; -.
DR STRING; 3880.AES98403; -.
DR EnsemblPlants; AES98403; AES98403; MTR_5g068140.
DR GeneID; 11405771; -.
DR Gramene; AES98403; AES98403; MTR_5g068140.
DR KEGG; mtr:MTR_5g068140; -.
DR eggNOG; KOG0252; Eukaryota.
DR HOGENOM; CLU_001265_46_14_1; -.
DR OMA; HWHADYV; -.
DR OrthoDB; 762280at2759; -.
DR Proteomes; UP000002051; Chromosome 5.
DR Proteomes; UP000265566; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0085042; C:periarbuscular membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0036377; P:arbuscular mycorrhizal association; IMP:UniProtKB.
DR GO; GO:0043562; P:cellular response to nitrogen levels; IMP:UniProtKB.
DR GO; GO:0006817; P:phosphate ion transport; IMP:UniProtKB.
DR GO; GO:0009610; P:response to symbiotic fungus; IEP:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IDA:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 2.
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 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Hydrolase; Membrane; Phosphate transport;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..557
FT /note="Low affinity inorganic phosphate transporter 8"
FT /id="PRO_0000450033"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..70
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..130
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..210
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..346
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..414
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 479..490
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..557
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 519..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 557 AA; 61025 MW; 14BE9379B97298F3 CRC64;
MATSHGVLRS LDNAKTQSYH YLAIVIAGMG FFTDAYDLFC ITAVTKLIGR LYYSDPTNHS
PGILPTNVNN AITGVALCGT LAGQLFFGWL GDKLGRKKVY GITLTTMVGF ALLSGLSFGS
TPKTVVTSLC FFRFWLGFGI GGDYPLSAVI MSEYANQKTR GSFIAAVFAM QGVGILVAGG
VAMFVSKLFL LYFPAPDFET DAVLSTQPEG DFVWRIVLMF GAVPAALTYY WRMKMPETAR
YTALVEGDHK KAVEDMAKVL DRNILSEESN TRIAIRPLES HSYGLFSSEF LNRHGLHLLG
TTSTWFLLDI AFYSLQLTQK DIYPTSGLVY KASKMNAIEE VFQLSRAMFA VALIATVPGY
WCTVFLIEKI GRFRIQLIGF LVMSVCMWFL GHNYRSFRGE ESACKNGSKY SFCNGNPVMF
AILFGLTLFF ANFGPNSTTF IVPAELFPAR LRSTCHGISA AAGKSGAIVG AFGVQSYIGN
SHDKSKGTKQ AIMALAVVNL LGFFFTFLVP ETQGRSLEEI SGEEKDFQGN NADEEISGER
NGTRNASVDK SPETSMV
