PHO1A_ARATH
ID PHO1A_ARATH Reviewed; 777 AA.
AC Q6R8G0; Q9C789;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Phosphate transporter PHO1 homolog 10;
DE AltName: Full=Protein PHO1 homolog 10;
DE Short=AtPHO1;H10;
GN Name=PHO1-H10; OrderedLocusNames=At1g69480; ORFNames=F10D13.13;
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 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).
RN [5]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=18434606; DOI=10.1104/pp.108.119321;
RA Ribot C., Zimmerli C., Farmer E.E., Reymond P., Poirier Y.;
RT "Induction of the Arabidopsis PHO1;H10 gene by 12-oxo-phytodienoic acid but
RT not jasmonic acid via a CORONATINE INSENSITIVE1-dependent pathway.";
RL Plant Physiol. 147:696-706(2008).
CC -!- FUNCTION: May transport inorganic phosphate (Pi). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in root epidermis and cortex, leaf blades
CC and hydathodes, stems and flowers. {ECO:0000269|PubMed:15122012,
CC ECO:0000269|PubMed:18434606}.
CC -!- INDUCTION: By wounding, dehydration, salt and cold treatments, osmotic
CC shock and infection by P.syringae pv. tomato in leaves. Induced by salt
CC treatment in roots. Induced by auxin, cytokinin, abscisic acid (ABA)
CC and 12-oxo-phytodienoic acid (OPDA), but not by jasmonic acid (JA).
CC Induced by Pi deficiency in roots and leaves. Down-regulated by
CC sucrose. {ECO:0000269|PubMed:15122012, ECO:0000269|PubMed:18094993,
CC ECO:0000269|PubMed:18434606}.
CC -!- SIMILARITY: Belongs to the SYG1 (TC 2.A.94) family. {ECO:0000305}.
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DR EMBL; AY507962; AAR99492.1; -; mRNA.
DR EMBL; AC073178; AAG60105.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34930.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM57979.1; -; Genomic_DNA.
DR RefSeq; NP_001320450.1; NM_001334410.1.
DR RefSeq; NP_177107.2; NM_105615.4.
DR AlphaFoldDB; Q6R8G0; -.
DR STRING; 3702.AT1G69480.1; -.
DR iPTMnet; Q6R8G0; -.
DR PaxDb; Q6R8G0; -.
DR PRIDE; Q6R8G0; -.
DR ProteomicsDB; 236145; -.
DR EnsemblPlants; AT1G69480.1; AT1G69480.1; AT1G69480.
DR EnsemblPlants; AT1G69480.2; AT1G69480.2; AT1G69480.
DR GeneID; 843280; -.
DR Gramene; AT1G69480.1; AT1G69480.1; AT1G69480.
DR Gramene; AT1G69480.2; AT1G69480.2; AT1G69480.
DR KEGG; ath:AT1G69480; -.
DR Araport; AT1G69480; -.
DR TAIR; locus:2007156; AT1G69480.
DR eggNOG; KOG1162; Eukaryota.
DR HOGENOM; CLU_006116_2_0_1; -.
DR InParanoid; Q6R8G0; -.
DR OMA; HETENIV; -.
DR OrthoDB; 536327at2759; -.
DR PhylomeDB; Q6R8G0; -.
DR PRO; PR:Q6R8G0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6R8G0; baseline and differential.
DR Genevisible; Q6R8G0; 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:0005802; C:trans-Golgi network; 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; IBA:GO_Central.
DR GO; GO:0006817; P:phosphate ion transport; IBA:GO_Central.
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..777
FT /note="Phosphate transporter PHO1 homolog 10"
FT /id="PRO_0000398164"
FT TOPO_DOM 1..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..408
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..459
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..496
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518..646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 647..667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 668..691
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..712
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 713..777
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1..322
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT DOMAIN 581..775
FT /note="EXS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00712"
FT CONFLICT 699
FT /note="V -> M (in Ref. 2; AAG60105)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 777 AA; 90598 MW; F82705E543F09CE4 CRC64;
MKFGKIFKKQ MVPEWVEAYV DYNGLKRVLK EIRSYKHSKL TRAASRVSQQ AEALHRSFSG
LSFHPRHSER AGDIEDQVIK VDTVQEEGSR KLYETKFLKK SEEGGEFEES FFKKLDENLN
KVNKFYRDKV KEVIEEAALL DKQMDALIAL RVKMQKPDVD NLNLEKHPSD KVVVDTSDNT
MRTQGTANTD MVHGIERTNI PEEEASHIMA DIVPVSHTNG DEEEASIGDK QDLREILERV
KMNDVLESPI TTLKGVFGDS NEPISKKGLK KGEEQLRLVF SEFYQKLRRL KEYSFMNLLA
FSKIMKKYEK IASRNASRNY MKIVDNSLIG SSDEVNRLLE RVEVTFVKHF SSGNRREGMK
CLRPKVKRER HRVTFFSGFF SGCSIALVIA VVFKIESRKI MEKNYGTEYM ANIIPLYSLF
GFIILHMLMY SANIYFWKRY RVNYTFIFGF KQGTELGDRE VFLVSTGLAV LAFVCFLLNL
QLDMDWRMKH HKTLPEVIPL CLATIVLFIL FCPFNIIYRS SRFFFIRSLF HCICAPLYEV
TLPDFFLGDH LTSQIQAIRS FELFICYYGL GEYLQRQNKC HSHGVYNAFY FVVAVIPYWL
RFLQCIRRLC EEKESVHGYN ALKYMLTIIA VIVRTAYELK KGRTWMILAL VSSGVATGMN
TFWDIVIDWG LLRKHSKNPY LRDKLLVPHK SVYFAAMVVN VILRVAWMQL VLEFNLKSLH
KIAVTSIISC LEIIRRGIWS FFRLENEHLN NVGKYRAFKS VPHPFHYYDD DDVDKDD
