SPX1_ORYSJ
ID SPX1_ORYSJ Reviewed; 295 AA.
AC Q69XJ0; A0A0P0WYU6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=SPX domain-containing protein 1 {ECO:0000303|PubMed:19566645};
DE AltName: Full=Protein SPX DOMAIN GENE 1 {ECO:0000303|PubMed:19566645};
DE Short=OsSPX1 {ECO:0000303|PubMed:19566645};
GN Name=SPX1 {ECO:0000303|PubMed:19566645};
GN OrderedLocusNames=Os06g0603600 {ECO:0000312|EMBL:BAF19927.1},
GN LOC_Os06g40120 {ECO:0000305};
GN ORFNames=OsJ_21901 {ECO:0000312|EMBL:EAZ37570.1},
GN P0486H12.37 {ECO:0000312|EMBL:BAD35467.1};
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;
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 BY PHOSPHATE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19566645; DOI=10.1111/j.1744-7909.2009.00834.x;
RA Wang Z., Hu H., Huang H., Duan K., Wu Z., Wu P.;
RT "Regulation of OsSPX1 and OsSPX3 on expression of OsSPX domain genes and
RT Pi-starvation signaling in rice.";
RL J. Integr. Plant Biol. 51:663-674(2009).
RN [7]
RP GENE FAMILY, NOMENCLATURE, AND INDUCTION BY COLD.
RX PubMed=19508276; DOI=10.1111/j.1467-7652.2009.00423.x;
RA Zhao L., Liu F., Xu W., Di C., Zhou S., Xue Y., Yu J., Su Z.;
RT "Increased expression of OsSPX1 enhances cold/subfreezing tolerance in
RT tobacco and Arabidopsis thaliana.";
RL Plant Biotechnol. J. 7:550-561(2009).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=19000161; DOI=10.1111/j.1365-313x.2008.03734.x;
RA Wang C., Ying S., Huang H., Li K., Wu P., Shou H.;
RT "Involvement of OsSPX1 in phosphate homeostasis in rice.";
RL Plant J. 57:895-904(2009).
RN [9]
RP FUNCTION, AND INDUCTION.
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 [10]
RP FUNCTION, INTERACTION WITH PHR2, SUBCELLULAR LOCATION, INDUCTION BY PHR2,
RP AND DOMAIN.
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).
CC -!- FUNCTION: Involved in plant adaptation to phosphate starvation
CC (PubMed:19000161). Inhibits PHR2 DNA-binding activity via a Pi-
CC dependent protein interaction (PubMed:25271318). Suppresses the
CC regulation on expression of PT2 by PHR2 and accumulation of shoot Pi
CC (PubMed:20149131). Optimizes growth under phosphate-limited conditions
CC through a negative feedback loop of the PSI (phosphate starvation-
CC induced) signaling pathway (PubMed:19000161, PubMed:20149131).
CC Regulates the expression of SPX2, SPX3 and SPX5 (PubMed:19566645). May
CC be an important link between signal transduction pathways related to
CC phosphate starvation and cold stress (PubMed:19000161).
CC {ECO:0000269|PubMed:19000161, ECO:0000269|PubMed:19566645,
CC ECO:0000269|PubMed:20149131, ECO:0000269|PubMed:25271318}.
CC -!- SUBUNIT: Interacts (via SPX domain) with PHR2 (via C-terminus)
CC (PubMed:25271318). {ECO:0000269|PubMed:25271318}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19566645,
CC ECO:0000269|PubMed:25271318}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in roots and leaves.
CC {ECO:0000269|PubMed:19566645}.
CC -!- INDUCTION: Up-regulated under phosphate starvation (PubMed:19566645,
CC PubMed:19000161). Up-regulated during cold stress (PubMed:19508276).
CC Under negative feedback regulation by PHO2 (PubMed:20149131). Up-
CC regulated by the transcription factor PHR2 (PubMed:25271318).
CC {ECO:0000269|PubMed:19000161, ECO:0000269|PubMed:19508276,
CC ECO:0000269|PubMed:19566645, ECO:0000269|PubMed:20149131,
CC ECO:0000269|PubMed:25271318}.
CC -!- DOMAIN: The SPX domain is sufficient for inhibition of PHR2 binding to
CC DNA. {ECO:0000269|PubMed:25271318}.
CC -!- MISCELLANEOUS: SPX1 and SPX2 have redundant functions in repressing the
CC activity of PHR2. {ECO:0000269|PubMed:25271318}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP003615; BAD35467.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF19927.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS98511.1; -; Genomic_DNA.
DR EMBL; CM000143; EAZ37570.1; -; Genomic_DNA.
DR EMBL; AK063544; BAG88759.1; -; mRNA.
DR EMBL; AK072067; BAG92810.1; -; mRNA.
DR RefSeq; XP_015644496.1; XM_015789010.1.
DR PDB; 7E40; X-ray; 2.60 A; B/D=1-198.
DR PDBsum; 7E40; -.
DR AlphaFoldDB; Q69XJ0; -.
DR SMR; Q69XJ0; -.
DR STRING; 4530.OS06T0603600-01; -.
DR CarbonylDB; Q69XJ0; -.
DR PaxDb; Q69XJ0; -.
DR PRIDE; Q69XJ0; -.
DR EnsemblPlants; Os06t0603600-01; Os06t0603600-01; Os06g0603600.
DR EnsemblPlants; Os06t0603600-02; Os06t0603600-02; Os06g0603600.
DR GeneID; 4341465; -.
DR Gramene; Os06t0603600-01; Os06t0603600-01; Os06g0603600.
DR Gramene; Os06t0603600-02; Os06t0603600-02; Os06g0603600.
DR KEGG; osa:4341465; -.
DR eggNOG; KOG1161; Eukaryota.
DR HOGENOM; CLU_057600_1_1_1; -.
DR InParanoid; Q69XJ0; -.
DR OMA; MKSLYMK; -.
DR OrthoDB; 1345784at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q69XJ0; OS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070417; P:cellular response to cold; IEP:UniProtKB.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:UniProtKB.
DR GO; GO:0080040; P:positive regulation of cellular response to phosphate starvation; IMP:UniProtKB.
DR InterPro; IPR004331; SPX_dom.
DR InterPro; IPR031142; SPX_prot.
DR PANTHER; PTHR45978; PTHR45978; 1.
DR Pfam; PF03105; SPX; 2.
DR PROSITE; PS51382; SPX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome.
FT CHAIN 1..295
FT /note="SPX domain-containing protein 1"
FT /id="PRO_0000398347"
FT DOMAIN 1..166
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT REGION 199..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:7E40"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:7E40"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:7E40"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:7E40"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:7E40"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:7E40"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:7E40"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:7E40"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:7E40"
FT HELIX 67..108
FT /evidence="ECO:0007829|PDB:7E40"
FT HELIX 114..156
FT /evidence="ECO:0007829|PDB:7E40"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:7E40"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:7E40"
FT HELIX 179..193
FT /evidence="ECO:0007829|PDB:7E40"
SQ SEQUENCE 295 AA; 33112 MW; 86DF8191B1E1DFD7 CRC64;
MKFGKSLSSQ IVETLPEWRD KFLSYKDLKK RLKLIGGGGG GEERQAKRAR VAADGGEEEA
AAAAMTPEEA GFMRLLEAEL DKFNSFFVEK EEEYIIRQKE LQDRVARAAG RESKEELMRV
RKEIVDFHGE MVLLENYSAL NYTGLVKILK KYDKRTGALI RLPFIQKVLQ QPFFTTDLLY
KLVKQCEAML DQLLPSNELS VSSEDGRGDS TNEDKPSNPS SSLVNGGTIP ELDEIEYMES
MYMKGTVAAL RSLKEIRSGS STVSAFSLPP LQGDSSPEEQ QELWNKIPVI EQAAK
