PHO11_ARATH
ID PHO11_ARATH Reviewed; 784 AA.
AC Q93ZF5; Q6R8G9; Q9CA38; Q9SX34;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Phosphate transporter PHO1 homolog 1;
DE AltName: Full=Protein PHO1 homolog 1;
DE Short=AtPHO1;H1;
GN Name=PHO1-H1; OrderedLocusNames=At1g68740; ORFNames=F14K14.15, F24J5.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, AND
RP NOMENCLATURE.
RX PubMed=15122012; DOI=10.1104/pp.103.037945;
RA Wang Y., Ribot C., Rezzonico E., Poirier Y.;
RT "Structure and expression profile of the Arabidopsis PHO1 gene family
RT indicates a broad role in inorganic phosphate homeostasis.";
RL Plant Physiol. 135:400-411(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17461783; DOI=10.1111/j.1365-313x.2007.03108.x;
RA Stefanovic A., Ribot C., Rouached H., Wang Y., Chong J., Belbahri L.,
RA Delessert S., Poirier Y.;
RT "Members of the PHO1 gene family show limited functional redundancy in
RT phosphate transfer to the shoot, and are regulated by phosphate deficiency
RT via distinct pathways.";
RL Plant J. 50:982-994(2007).
RN [6]
RP INDUCTION.
RX PubMed=18094993; DOI=10.1007/s00425-007-0677-x;
RA Ribot C., Wang Y., Poirier Y.;
RT "Expression analyses of three members of the AtPHO1 family reveal
RT differential interactions between signaling pathways involved in phosphate
RT deficiency and the responses to auxin, cytokinin, and abscisic acid.";
RL Planta 227:1025-1036(2008).
CC -!- FUNCTION: Contributes to the loading of inorganic phosphate (Pi) into
CC the root xylem vessels. {ECO:0000269|PubMed:17461783}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in vascular cylinder of roots, leaves,
CC stems, petals, sepals and filaments. Expressed in receptacle, stigma
CC apex and anther connective tissue. {ECO:0000269|PubMed:15122012,
CC ECO:0000269|PubMed:17461783}.
CC -!- INDUCTION: By Pi deficiency in roots and shoots. Induced by sucrose,
CC auxin and cytokinin. Down-regulated by abscisic acid (ABA).
CC {ECO:0000269|PubMed:15122012, ECO:0000269|PubMed:17461783,
CC ECO:0000269|PubMed:18094993}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:17461783}.
CC -!- SIMILARITY: Belongs to the SYG1 (TC 2.A.94) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD49969.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG52042.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY507953; AAR99483.1; -; mRNA.
DR EMBL; AC008075; AAD49969.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011914; AAG52042.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34834.1; -; Genomic_DNA.
DR EMBL; AY057574; AAL09813.1; -; mRNA.
DR PIR; B96712; B96712.
DR RefSeq; NP_564940.1; NM_105547.3.
DR AlphaFoldDB; Q93ZF5; -.
DR STRING; 3702.AT1G68740.1; -.
DR PaxDb; Q93ZF5; -.
DR PRIDE; Q93ZF5; -.
DR EnsemblPlants; AT1G68740.1; AT1G68740.1; AT1G68740.
DR GeneID; 843205; -.
DR Gramene; AT1G68740.1; AT1G68740.1; AT1G68740.
DR KEGG; ath:AT1G68740; -.
DR Araport; AT1G68740; -.
DR TAIR; locus:2012458; AT1G68740.
DR eggNOG; KOG1162; Eukaryota.
DR HOGENOM; CLU_006116_2_0_1; -.
DR InParanoid; Q93ZF5; -.
DR OMA; QGVIQVH; -.
DR OrthoDB; 536327at2759; -.
DR PhylomeDB; Q93ZF5; -.
DR PRO; PR:Q93ZF5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93ZF5; baseline and differential.
DR Genevisible; Q93ZF5; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; IBA:GO_Central.
DR GO; GO:0015114; F:phosphate ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR GO; GO:0006817; P:phosphate ion transport; IMP:TAIR.
DR CDD; cd14476; SPX_PHO1_like; 1.
DR InterPro; IPR004342; EXS_C.
DR InterPro; IPR034092; PHO1_SPX.
DR InterPro; IPR004331; SPX_dom.
DR Pfam; PF03124; EXS; 1.
DR Pfam; PF03105; SPX; 1.
DR PROSITE; PS51380; EXS; 1.
DR PROSITE; PS51382; SPX; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Phosphate transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..784
FT /note="Phosphate transporter PHO1 homolog 1"
FT /id="PRO_0000398155"
FT TOPO_DOM 1..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..429
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..507
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..528
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 529..654
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 676..703
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 704..724
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 725..784
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 2..335
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT DOMAIN 593..784
FT /note="EXS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00712"
FT CONFLICT 20
FT /note="F -> S (in Ref. 1; AAR99483)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 784 AA; 90711 MW; 4CBE64EEC67F35D7 CRC64;
MVKFTKQFEG QLVPEWKDAF VDYSQLKKDL KKIHLFTNGV EKKHTETSLI KTVKSSLGRL
SIFGNKGREQ SRVIQVHKKL ASSGSNNDVY ETELLEKIAD DTDAAKEFFA CLDMQLNKVN
QFYKTKEKEF LERGECLKKQ MDILIELKDA FKQKQANGES TQESKEDDSI SCTISCEYDS
VRGRTEEMQL QVSCLDNLED NGEEALESLG SEEPIKANNE DSKLTTVSSR VFSCQGKNVK
IKIPLTNPSR TFSAISYLIN QSSSKKNGPD GGNKLQISKK KLSHAEKMIK GALTELFKGL
NYLKTYRNLN ILAFMNILKK FDKVTGKQIL PIYLKVVESS YFNISDKVMI LSDEVEEWFI
KHLAGENRRK AMKYLKPHHR KESHSVTFFI GLFTGCFVAL LAGYIIVAHL TGMYRQHSAN
TFYMETAYPV LSMFGLLFLH LFLYGCNIFM WRKARINYSF IFELGSKNEL KYRDVFLICT
ASMSAIAGVM FVHLSLLEKG YSFRQVQVIP GLLLLGFLLI LICPLNIFYK SSRYRLISVI
RNIVFSPLYK VVMLDFFMAD QLCSQVPMLR NLEYIACYYI TGSYATQDYE YCMRVKYYRD
LAYAVSFLPY YWRAMQCARR WFDEGETSHL VNLGKYVSAM LAAGTKVAYE KERSLGWLCL
VVAMSSVATI YQLYWDFVKD WGLLQHNSNN PWLRNQLMLR QKSIYYFSMV LNLVLRLAWL
QTVLHSSFEH VDYRVTGLFL AALEVIRRGQ WNFYRLENEH LNNAGKFRAV KTVPLPFREV
DEED
