SPX1_ARATH
ID SPX1_ARATH Reviewed; 256 AA.
AC Q8LBH4; Q8RY68;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=SPX domain-containing protein 1 {ECO:0000303|PubMed:18315545};
DE AltName: Full=Protein SPX DOMAIN GENE 1 {ECO:0000303|PubMed:18315545};
DE Short=AtSPX1 {ECO:0000303|PubMed:18315545};
GN Name=SPX1 {ECO:0000303|PubMed:18315545};
GN OrderedLocusNames=At5g20150 {ECO:0000312|Araport:AT5G20150};
GN ORFNames=F5O24.40 {ECO:0000312|EMBL:AF296825};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, SUBCELLULAR LOCATION, INDUCTION, AND FUNCTION.
RX PubMed=18315545; DOI=10.1111/j.1365-313x.2008.03460.x;
RA Duan K., Yi K., Dang L., Huang H., Wu W., Wu P.;
RT "Characterization of a sub-family of Arabidopsis genes with the SPX domain
RT reveals their diverse functions in plant tolerance to phosphorus
RT starvation.";
RL Plant J. 54:965-975(2008).
RN [6]
RP FUNCTION, INTERACTION WITH PHR1, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=25271326; DOI=10.1073/pnas.1404654111;
RA Puga M.I., Mateos I., Charukesi R., Wang Z., Franco-Zorrilla J.M.,
RA de Lorenzo L., Irigoyen M.L., Masiero S., Bustos R., Rodriguez J.,
RA Leyva A., Rubio V., Sommer H., Paz-Ares J.;
RT "SPX1 is a phosphate-dependent inhibitor of PHOSPHATE STARVATION RESPONSE 1
RT in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:14947-14952(2014).
CC -!- FUNCTION: Plays a positive role in plant adaptation to phosphate
CC starvation (PubMed:18315545). Inhibits PHR1 DNA-binding activity in a
CC Pi-dependent manner (PubMed:25271326). {ECO:0000269|PubMed:18315545,
CC ECO:0000269|PubMed:25271326}.
CC -!- SUBUNIT: Interacts with PHR1 in a highly Pi-dependent manner
CC (PubMed:25271326). {ECO:0000269|PubMed:25271326}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18315545,
CC ECO:0000269|PubMed:25271326}.
CC -!- INDUCTION: Up-regulated under phosphate starvation.
CC {ECO:0000269|PubMed:18315545}.
CC -!- DISRUPTION PHENOTYPE: No effect on Pi accumulation, due to the
CC redundancy with SPX2. Spx1 and spx2 double mutants have an increased
CC root-to-shoot growth ratio and a reduced rot hair size when grown in
CC Pi-sufficient conditions. {ECO:0000269|PubMed:25271326}.
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DR EMBL; AF296825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92801.1; -; Genomic_DNA.
DR EMBL; AY075605; AAL91621.1; -; mRNA.
DR EMBL; BT000868; AAN38706.1; -; mRNA.
DR EMBL; AY087206; AAM64762.1; -; mRNA.
DR RefSeq; NP_197515.1; NM_122022.3.
DR AlphaFoldDB; Q8LBH4; -.
DR SMR; Q8LBH4; -.
DR BioGRID; 17413; 8.
DR IntAct; Q8LBH4; 2.
DR STRING; 3702.AT5G20150.1; -.
DR PaxDb; Q8LBH4; -.
DR PRIDE; Q8LBH4; -.
DR ProteomicsDB; 245250; -.
DR DNASU; 832137; -.
DR EnsemblPlants; AT5G20150.1; AT5G20150.1; AT5G20150.
DR GeneID; 832137; -.
DR Gramene; AT5G20150.1; AT5G20150.1; AT5G20150.
DR KEGG; ath:AT5G20150; -.
DR Araport; AT5G20150; -.
DR TAIR; locus:2149254; AT5G20150.
DR eggNOG; KOG1161; Eukaryota.
DR HOGENOM; CLU_057600_1_1_1; -.
DR InParanoid; Q8LBH4; -.
DR OMA; PTISHRN; -.
DR OrthoDB; 1345784at2759; -.
DR PRO; PR:Q8LBH4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LBH4; baseline and differential.
DR Genevisible; Q8LBH4; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR GO; GO:0080040; P:positive regulation of cellular response to phosphate starvation; IMP:TAIR.
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 Nucleus; Reference proteome.
FT CHAIN 1..256
FT /note="SPX domain-containing protein 1"
FT /id="PRO_0000398342"
FT DOMAIN 1..155
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT MOTIF 30..46
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT CONFLICT 62
FT /note="N -> D (in Ref. 4; AAM64762)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 256 AA; 30073 MW; 335491905F62E1F7 CRC64;
MKFGKSLSNQ IEQTLPEWQD KFLSYKELKK RLKLIGSKTA DRPVKRLRLD EFSVGISKEE
INFIQLLEDE LEKFNNFFVE KEEEYIIRLK EFRDRIAKAK DSMEKMIKIR KEIVDFHGEM
VLLENYSALN YTGLVKILKK YDKRTGDLMR LPFIQKVLQQ PFYTTDLLFK LVKESEAMLD
QIFPANETES EIIQAELSEH KFMESLHMKS TIAALRVLKE IRSGSSTVSV FSLPPLQLNG
LDETWKKIPL LEQEAK
