PHO12_ORYSJ
ID PHO12_ORYSJ Reviewed; 815 AA.
AC Q6K991; A0A0N7KGA9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Phosphate transporter PHO1-2;
DE AltName: Full=Protein PHO1-2;
DE Short=OsPHO1;2;
GN Name=PHO1-2; OrderedLocusNames=Os02g0809800, LOC_Os02g56510;
GN ORFNames=OJ1112_G06.31, OJ1520_C09.43, OsJ_08812;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, NOMENCLATURE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=20081045; DOI=10.1104/pp.109.149872;
RA Secco D., Baumann A., Poirier Y.;
RT "Characterization of the rice PHO1 gene family reveals a key role for
RT OsPHO1;2 in phosphate homeostasis and the evolution of a distinct clade in
RT dicotyledons.";
RL Plant Physiol. 152:1693-1704(2010).
CC -!- FUNCTION: Involved in the transfer of inorganic phosphate (Pi) from
CC roots to shoots. {ECO:0000269|PubMed:20081045}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in roots.
CC {ECO:0000269|PubMed:20081045}.
CC -!- INDUCTION: Not induced by Pi deficiency in roots.
CC {ECO:0000269|PubMed:20081045}.
CC -!- DISRUPTION PHENOTYPE: Strong decrease in root and shoot biomass and Pi
CC content. 25-fold reduction in Pi transfer from roots to shoots.
CC {ECO:0000269|PubMed:20081045}.
CC -!- SIMILARITY: Belongs to the SYG1 (TC 2.A.94) family. {ECO:0000305}.
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DR EMBL; AP003996; BAD19144.1; -; Genomic_DNA.
DR EMBL; AP004064; BAD19259.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF10378.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS81505.1; -; Genomic_DNA.
DR EMBL; CM000139; EEE58023.1; -; Genomic_DNA.
DR EMBL; AK100323; BAG94551.1; -; mRNA.
DR RefSeq; XP_015626153.1; XM_015770667.1.
DR AlphaFoldDB; Q6K991; -.
DR SMR; Q6K991; -.
DR STRING; 4530.OS02T0809800-01; -.
DR PaxDb; Q6K991; -.
DR PRIDE; Q6K991; -.
DR EnsemblPlants; Os02t0809800-01; Os02t0809800-01; Os02g0809800.
DR GeneID; 4331090; -.
DR Gramene; Os02t0809800-01; Os02t0809800-01; Os02g0809800.
DR KEGG; osa:4331090; -.
DR eggNOG; KOG1162; Eukaryota.
DR HOGENOM; CLU_006116_2_0_1; -.
DR InParanoid; Q6K991; -.
DR OMA; GNWTEAR; -.
DR OrthoDB; 536327at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6K991; OS.
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; IBA:GO_Central.
DR GO; GO:0006817; P:phosphate ion transport; IMP:UniProtKB.
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..815
FT /note="Phosphate transporter PHO1-2"
FT /id="PRO_0000398166"
FT TOPO_DOM 1..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..458
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 530..538
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 539..559
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 560..686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 687..707
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 708..734
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 735..751
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 752..815
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 2..368
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT DOMAIN 624..815
FT /note="EXS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00712"
FT REGION 83..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 815 AA; 91524 MW; 5177F5151C6BD288 CRC64;
MVKFSREYEA SIIPEWKAAF VDYKRLKKLI KRIKVTRRDD SFAAANAAAA ADHLLPPPPA
EKEAGGYGFS ILDPVRAIAA RFSAGQQPSA SEDEECPDRG ELVRSTDKHE REFMERADEE
LEKVNAFYTG QEAELLARGD ALLEQLRILA DVKRILADHA AARRARGLAR SRSMPPPPPS
SSPPSSVHGS SGRYLLSGLS SPQSMSDGSL ELQQAQVSEG AAVADEVMAA LERNGVSFVG
LAGKKDGKTK DGSGKGRGGG GGGGGGVLQL PATVRIDIPA TSPGRAALKV WEELVNVLRK
DGADPAAAFV HRKKIQHAEK NIRDAFMALY RGLELLKKFS SLNVKAFTKI LKKFVKVSEQ
QRATDLFSEK VKRSPFSSSD KVLQLADEVE CIFMKHFTGN DRKVAMKYLK PQQPRNTHMI
TFLVGLFTGT FVSLFIIYAI LAHVSGIFTS TGNSAYMEIV YHVFSMFALI SLHIFLYGCN
LFMWKNTRIN HNFIFDFSSN TALTHRDAFL MSASIMCTVV AALVINLFLK NAGVAYANAL
PGALLLLSTG VLFCPFDIFY RSTRYCFMRV MRNIIFSPFY KVLMADFFMA DQLTSQIPLL
RHMEFTACYF MAGSFRTHPY ETCTSGQQYK HLAYVISFLP YFWRALQCLR RYLEEGHDIN
QLANAGKYVS AMVAAAVRFK YAATPTPFWV WMVIISSSGA TIYQLYWDFV KDWGFLNPKS
KNRWLRNELI LKNKSIYYVS MMLNLALRLA WTESVMKIHI GKVESRLLDF SLASLEIIRR
GHWNFYRLEN EHLNNVGKFR AVKTVPLPFR ELETD
