PHR2_ORYSJ
ID PHR2_ORYSJ Reviewed; 426 AA.
AC Q6Z156; B9FWZ1;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Protein PHOSPHATE STARVATION RESPONSE 2 {ECO:0000303|PubMed:18263782};
DE Short=OsPHR2 {ECO:0000303|PubMed:18263782};
GN Name=PHR2 {ECO:0000303|PubMed:18263782};
GN OrderedLocusNames=Os07g0438800 {ECO:0000312|EMBL:BAF21429.2},
GN LOC_Os07g25710 {ECO:0000305};
GN ORFNames=OSJNBa0026I22.19 {ECO:0000312|EMBL:BAD30836.1},
GN P0443H10.4 {ECO:0000312|EMBL:BAC84294.1};
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 {ECO:0000312|EMBL:BAC84294.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, LACK OF INDUCTION BY
RP PHOSPHATE, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=18263782; DOI=10.1104/pp.107.111443;
RA Zhou J., Jiao F., Wu Z., Li Y., Wang X., He X., Zhong W., Wu P.;
RT "OsPHR2 is involved in phosphate-starvation signaling and excessive
RT phosphate accumulation in shoots of plants.";
RL Plant Physiol. 146:1673-1686(2008).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION.
RX PubMed=19704822; DOI=10.4161/psb.3.9.5781;
RA Wu P., Wang X.;
RT "Role of OsPHR2 on phosphorus homeostasis and root hairs development in
RT rice (Oryza sativa L.).";
RL Plant Signal. Behav. 3:674-675(2008).
RN [8]
RP FUNCTION.
RX PubMed=20149131; DOI=10.1111/j.1365-313x.2010.04170.x;
RA Liu F., Wang Z., Ren H., Shen C., Li Y., Ling H.Q., Wu C., Lian X., Wu P.;
RT "OsSPX1 suppresses the function of OsPHR2 in the regulation of expression
RT of OsPT2 and phosphate homeostasis in shoots of rice.";
RL Plant J. 62:508-517(2010).
RN [9]
RP FUNCTION, INTERACTION WITH SPX4, AND SUBCELLULAR LOCATION.
RX PubMed=24692424; DOI=10.1105/tpc.114.123208;
RA Lv Q., Zhong Y., Wang Y., Wang Z., Zhang L., Shi J., Wu Z., Liu Y., Mao C.,
RA Yi K., Wu P.;
RT "SPX4 negatively regulates phosphate signaling and homeostasis through its
RT interaction with PHR2 in Rice.";
RL Plant Cell 26:1586-1597(2014).
RN [10]
RP FUNCTION, AND INTERACTION WITH SPX1 AND SPX2.
RX PubMed=25271318; DOI=10.1073/pnas.1404680111;
RA Wang Z., Ruan W., Shi J., Zhang L., Xiang D., Yang C., Li C., Wu Z.,
RA Liu Y., Yu Y., Shou H., Mo X., Mao C., Wu P.;
RT "Rice SPX1 and SPX2 inhibit phosphate starvation responses through
RT interacting with PHR2 in a phosphate-dependent manner.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:14953-14958(2014).
RN [11]
RP FUNCTION.
RX PubMed=25657119; DOI=10.1007/s11103-015-0289-y;
RA Ruan W., Guo M., Cai L., Hu H., Li C., Liu Y., Wu Z., Mao C., Yi K., Wu P.,
RA Mo X.;
RT "Genetic manipulation of a high-affinity PHR1 target cis-element to improve
RT phosphorous uptake in Oryza sativa L.";
RL Plant Mol. Biol. 87:429-440(2015).
RN [12]
RP FUNCTION, GENE FAMILY, NOMENCLATURE, DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, AND LACK OF INDUCTION BY PHOSPHATE.
RX PubMed=26082401; DOI=10.1104/pp.15.00736;
RA Guo M., Ruan W., Li C., Huang F., Zeng M., Liu Y., Yu Y., Ding X., Wu Y.,
RA Wu Z., Mao C., Yi K., Wu P., Mo X.;
RT "Integrative Comparison of the Role of the PHOSPHATE RESPONSE1 Subfamily in
RT Phosphate Signaling and Homeostasis in Rice.";
RL Plant Physiol. 168:1762-1776(2015).
RN [13]
RP INTERACTION WITH SPX4.
RX PubMed=27080106; DOI=10.1126/science.aad9858;
RA Wild R., Gerasimaite R., Jung J.Y., Truffault V., Pavlovic I., Schmidt A.,
RA Saiardi A., Jessen H.J., Poirier Y., Hothorn M., Mayer A.;
RT "Control of eukaryotic phosphate homeostasis by inositol polyphosphate
RT sensor domains.";
RL Science 352:986-990(2016).
CC -!- FUNCTION: Transcription factor involved in phosphate starvation
CC signaling (PubMed:18263782, PubMed:26082401). Binds to P1BS, an
CC imperfect palindromic sequence 5'-GNATATNC-3', to promote the
CC expression of inorganic phosphate (Pi) starvation-responsive genes
CC (PubMed:25657119, PubMed:26082401). Functionally redundant with PHR1
CC and PHR3 in regulating Pi starvation response and Pi homeostasis
CC (PubMed:26082401). Involved in both systematic and local Pi-signaling
CC pathways (PubMed:19704822). Regulates several Pi transporters
CC (PubMed:18263782). Regulates the expression of PT2 (PubMed:20149131).
CC Directly up-regulates SPX1 and SPX2 expression, but PHR2 binding to DNA
CC is repressed redundantly by SPX1 and SPX2 in a PI-dependent manner
CC (PubMed:25271318). The DNA-binding activity is also repressed by SPX4
CC (PubMed:24692424). Involved in root growth under Pi deprivation
CC (PubMed:18263782). {ECO:0000269|PubMed:18263782,
CC ECO:0000269|PubMed:19704822, ECO:0000269|PubMed:20149131,
CC ECO:0000269|PubMed:24692424, ECO:0000269|PubMed:25271318,
CC ECO:0000269|PubMed:25657119, ECO:0000269|PubMed:26082401}.
CC -!- SUBUNIT: Interacts (via C-terminus) with SPX4 (via N-terminus) in the
CC presence of inositol polyphosphate (PubMed:24692424, PubMed:27080106).
CC Interacts (via C-terminus) with SPX1 and SPX2 (via SPX domain)
CC (PubMed:25271318). {ECO:0000269|PubMed:24692424,
CC ECO:0000269|PubMed:25271318, ECO:0000269|PubMed:27080106}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18263782,
CC ECO:0000269|PubMed:24692424}. Cytoplasm {ECO:0000269|PubMed:24692424}.
CC Note=Interaction with SPX4 trap PHR2 within the cytoplasm and affects
CC the nuclear localization. {ECO:0000269|PubMed:24692424}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and fruits
CC (PubMed:18263782). Expressed in the root cap and in the exodermis,
CC sclerenchyma and vascular tissues of the root, in the cortex cells and
CC the stele of lateral roots, in the mesophyll cells of the leaf, in
CC pollen, vascular cylinder of the anther and the veins of the lemma,
CC palea and pistils, and in all node I tissues (PubMed:26082401).
CC {ECO:0000269|PubMed:18263782, ECO:0000269|PubMed:26082401}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout all stages of plant growth.
CC {ECO:0000269|PubMed:26082401}.
CC -!- INDUCTION: Not regulated by Pi starvation.
CC {ECO:0000269|PubMed:18263782, ECO:0000269|PubMed:26082401}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEE67078.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP005101; BAD30836.1; -; Genomic_DNA.
DR EMBL; AP005451; BAC84294.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF21429.2; -; Genomic_DNA.
DR EMBL; AP014963; BAT01257.1; -; Genomic_DNA.
DR EMBL; CM000144; EEE67078.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK100065; BAG94425.1; -; mRNA.
DR RefSeq; XP_015647735.1; XM_015792249.1.
DR RefSeq; XP_015647736.1; XM_015792250.1.
DR PDB; 7D3Y; X-ray; 3.11 A; C/D/E=225-362.
DR PDB; 7E40; X-ray; 2.60 A; A/C=248-380.
DR PDBsum; 7D3Y; -.
DR PDBsum; 7E40; -.
DR AlphaFoldDB; Q6Z156; -.
DR SMR; Q6Z156; -.
DR STRING; 4530.OS07T0438800-01; -.
DR PaxDb; Q6Z156; -.
DR PRIDE; Q6Z156; -.
DR EnsemblPlants; Os07t0438800-01; Os07t0438800-01; Os07g0438800.
DR GeneID; 4343086; -.
DR Gramene; Os07t0438800-01; Os07t0438800-01; Os07g0438800.
DR KEGG; osa:4343086; -.
DR eggNOG; ENOG502QXMH; Eukaryota.
DR HOGENOM; CLU_044541_2_1_1; -.
DR InParanoid; Q6Z156; -.
DR OMA; PHEKHSR; -.
DR OrthoDB; 812231at2759; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR ExpressionAtlas; Q6Z156; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR025756; Myb_CC_LHEQLE.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR006447; Myb_dom_plants.
DR InterPro; IPR044848; PHR1-like.
DR PANTHER; PTHR31314; PTHR31314; 1.
DR Pfam; PF14379; Myb_CC_LHEQLE; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR TIGRFAMs; TIGR01557; myb_SHAQKYF; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..426
FT /note="Protein PHOSPHATE STARVATION RESPONSE 2"
FT /id="PRO_0000436715"
FT DOMAIN 243..303
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 274..299
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 27..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 253..265
FT /evidence="ECO:0007829|PDB:7E40"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:7E40"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:7E40"
FT HELIX 288..301
FT /evidence="ECO:0007829|PDB:7E40"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:7D3Y"
FT HELIX 331..374
FT /evidence="ECO:0007829|PDB:7E40"
SQ SEQUENCE 426 AA; 46232 MW; 56A608B14E001AB4 CRC64;
MERISTNQLY NSGIPVTVPS PLPAIPATLD ENIPRIPDGQ NVPRERELRS TPMPPHQNQS
TVAPLHGHFQ SSTGSVGPLR SSQAIRFSSV SSNEQYTNAN PYNSQPPSSG SSSTLNYGSQ
YGGFEPSLTD FPRDAGPTWC PDPVDGLLGY TDDVPAGNNL TENSSIAAGD ELAKQSEWWN
DFMNYDWKDI DNTACTETQP QVGPAAQSSV AVHQSAAQQS VSSQSGEPSA VAIPSPSGAS
NTSNSKTRMR WTPELHERFV DAVNLLGGSE KATPKGVLKL MKADNLTIYH VKSHLQKYRT
ARYRPELSEG SSEKKAASKE DIPSIDLKGG NFDLTEALRL QLELQKRLHE QLEIQRSLQL
RIEEQGKCLQ MMLEQQCIPG TDKAVDASTS AEGTKPSSDL PESSAVKDVP ENSQNGIAKQ
TESGDR
