PHT11_PETHY
ID PHT11_PETHY Reviewed; 534 AA.
AC A7KTC5; B2CPI3;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Low affinity inorganic phosphate transporter 1 {ECO:0000303|PubMed:18315538, ECO:0000303|PubMed:19380421};
DE Short=PhPT1 {ECO:0000303|PubMed:18315538, ECO:0000303|PubMed:19380421};
DE Short=PhPht1;1 {ECO:0000303|PubMed:18315538};
DE AltName: Full=Arbuscular mycorrhiza-induced phosphate transporter PT1 {ECO:0000305};
DE Short=AM-induced phosphate transporter PT1 {ECO:0000305};
DE AltName: Full=H(+)/Pi cotransporter PT1 {ECO:0000305};
GN Name=PT1 {ECO:0000303|PubMed:18315538, ECO:0000303|PubMed:19380421};
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 [MRNA], FUNCTION, AND INDUCTION BY ETHYLENE.
RC STRAIN=cv. Mitchell; TISSUE=Corolla;
RX PubMed=19380421; DOI=10.1093/jxb/erp092;
RA Chapin L.J., Jones M.L.;
RT "Ethylene regulates phosphorus remobilization and expression of a phosphate
RT transporter (PhPT1) during petunia corolla senescence.";
RL J. Exp. Bot. 60:2179-2190(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 232-504.
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) (By similarity). Involved in phosphorus (P) remobilization from
CC dying to developing tissues during corolla senescence in an ethylene-
CC dependent manner (PubMed:19380421). {ECO:0000250|UniProtKB:Q8GSG4,
CC ECO:0000269|PubMed:19380421}.
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}.
CC -!- INDUCTION: By ethylene during corolla senescence.
CC {ECO:0000269|PubMed:19380421}.
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; EF564180; ABS12068.1; -; mRNA.
DR EMBL; EU532760; ACB37438.1; -; Genomic_DNA.
DR AlphaFoldDB; A7KTC5; -.
DR SMR; A7KTC5; -.
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:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0080187; P:floral organ senescence; IEP:UniProtKB.
DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR GO; GO:0009723; P:response to ethylene; 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 2: Evidence at transcript level;
KW Cell membrane; Ethylene signaling pathway; Membrane; Phosphate transport;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..534
FT /note="Low affinity inorganic phosphate transporter 1"
FT /id="PRO_0000450036"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 24..44
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..69
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 70..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 99..119
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..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..210
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 211..231
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 291..311
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..343
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 344..364
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 370..390
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..400
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 401..421
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 441..461
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..481
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 482..502
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..534
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 507..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 534 AA; 58563 MW; E9E6334FEA54551B CRC64;
MAKDLQVLTA LDVAKTQLYH FTAIVIAGMG FFTDAYDLFC ISLVTKLLGR IYYHHEGALK
PGSLPPNVAA AVNGVAFCGT LAGQLFFGWL GDKLGRKKVY GMTLMLMVIC SIASGLSFGH
TPKSVMATLC FFRFWLGFGI GGDYPLSATI MSEYANKKTR GAFIAAVFAM QGFGILAGGM
VAIIVSAAFK NQFPAPAYKD GALASTISQA DFVWRIIVMF GAIPTALTYY WRMKMPETAR
YTALVAKNLK QATNDMSKVL QVEIEPEQEK VEEISQGNDF GLFTKQFLRR HGLHLLGTAS
TWFLLDIAFY SQNLFQKDIF SAIGWIPPAE TMNALEEVYR IARAQTLIAL CSTVPGYWFT
VAFIDKIGRF AIQLMGFFFM TVFMFALAIP YTHWTHKDNR IGFVIMYSLT FFFANFGPNA
TTFVVPAEIF PARLRSTCHG ISAAAGKAGA MVGAFGFLYA AQSTDPKKTD AGYPAGIGVR
NSLIVLGCVN FLGMLFTLLV PESKGKSLEE MSRENEGEDE NGTEMRASGR TVPV
