PHR2_ORYSI
ID PHR2_ORYSI Reviewed; 426 AA.
AC B8B5N8;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Protein PHOSPHATE STARVATION RESPONSE 2 {ECO:0000250|UniProtKB:Q6Z156};
DE Short=OsPHR2 {ECO:0000250|UniProtKB:Q6Z156};
GN Name=PHR2 {ECO:0000250|UniProtKB:Q6Z156};
GN ORFNames=OsI_25821 {ECO:0000312|EMBL:EEC81946.1};
OS Oryza sativa subsp. indica (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=39946 {ECO:0000312|Proteomes:UP000007015};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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).
CC -!- FUNCTION: Transcription factor involved in phosphate starvation
CC signaling. Binds to P1BS, an imperfect palindromic sequence 5'-
CC GNATATNC-3', to promote the expression of inorganic phosphate (Pi)
CC starvation-responsive genes. Functionally redundant with PHR1 and PHR3
CC in regulating Pi starvation response and Pi homeostasis. PHR2 binding
CC to DNA is repressed redundantly by SPX1, SPX2 and SPX4 in a PI-
CC dependent manner. {ECO:0000250|UniProtKB:Q6Z156}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
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DR EMBL; CM000132; EEC81946.1; -; Genomic_DNA.
DR PDB; 7D3T; X-ray; 2.70 A; A/B/C/D=180-313.
DR PDBsum; 7D3T; -.
DR AlphaFoldDB; B8B5N8; -.
DR SMR; B8B5N8; -.
DR STRING; 39946.B8B5N8; -.
DR EnsemblPlants; BGIOSGA025605-TA; BGIOSGA025605-PA; BGIOSGA025605.
DR Gramene; BGIOSGA025605-TA; BGIOSGA025605-PA; BGIOSGA025605.
DR HOGENOM; CLU_044541_2_1_1; -.
DR OMA; PHEKHSR; -.
DR Proteomes; UP000007015; Chromosome 7.
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; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..426
FT /note="Protein PHOSPHATE STARVATION RESPONSE 2"
FT /id="PRO_0000436718"
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:7D3T"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:7D3T"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:7D3T"
FT HELIX 288..299
FT /evidence="ECO:0007829|PDB:7D3T"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:7D3T"
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
