P23A_ARATH
ID P23A_ARATH Reviewed; 241 AA.
AC Q8L7U4; O81288; Q9FT78;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Co-chaperone protein p23-1 {ECO:0000305};
DE AltName: Full=Atp23-1 {ECO:0000303|PubMed:20349287};
DE AltName: Full=p23 co-chaperone {ECO:0000312|EMBL:CAC16575.1};
GN Name=P23-1 {ECO:0000305}; Synonyms=P23 {ECO:0000312|EMBL:CAC16575.1};
GN OrderedLocusNames=At4g02450 {ECO:0000312|Araport:AT4G02450};
GN ORFNames=T14P8.5 {ECO:0000312|EMBL:AAC19287.1};
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 [MRNA] (ISOFORM 2).
RA Bowra S.;
RT "A plant p23: the missing link suggesting glucocorticoid receptors exist in
RT plants.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP INDUCTION BY HEAT, INTERACTION WITH HSP90, AND FUNCTION.
RX PubMed=20349287; DOI=10.1007/s12192-010-0182-1;
RA Zhang Z., Sullivan W., Felts S.J., Prasad B.D., Toft D.O., Krishna P.;
RT "Characterization of plant p23-like proteins for their co-chaperone
RT activities.";
RL Cell Stress Chaperones 15:703-715(2010).
RN [7]
RP INTERACTION WITH HSP90-5; HSP90-6 AND HSP90-7.
RX PubMed=20493581; DOI=10.1016/j.jplph.2010.03.016;
RA Song H., Fan P., Shi W., Zhao R., Li Y.;
RT "Expression of five AtHsp90 genes in Saccharomyces cerevisiae reveals
RT functional differences of AtHsp90s under abiotic stresses.";
RL J. Plant Physiol. 167:1172-1178(2010).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=26163704; DOI=10.1093/jxb/erv330;
RA D'Alessandro S., Golin S., Hardtke C.S., Lo Schiavo F., Zottini M.;
RT "The co-chaperone p23 controls root development through the modulation of
RT auxin distribution in the Arabidopsis root meristem.";
RL J. Exp. Bot. 66:5113-5122(2015).
CC -!- FUNCTION: Acts as a co-chaperone for HSP90 (PubMed:20349287). Controls
CC root development through the modulation of auxin distribution in the
CC root meristem (PubMed:26163704). {ECO:0000269|PubMed:20349287,
CC ECO:0000269|PubMed:26163704}.
CC -!- SUBUNIT: Interacts with HSP90 in an ATP-dependent manner
CC (PubMed:20349287). Interacts with HSP90-5, HSP90-6 and HSP90-7
CC (PubMed:20493581). {ECO:0000269|PubMed:20349287,
CC ECO:0000269|PubMed:20493581}.
CC -!- INTERACTION:
CC Q8L7U4; Q0Q0I7: HSP90-2; Xeno; NbExp=2; IntAct=EBI-8417738, EBI-8081141;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26163704}. Nucleus
CC {ECO:0000269|PubMed:26163704}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8L7U4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8L7U4-2; Sequence=VSP_059664;
CC -!- TISSUE SPECIFICITY: Widely expressed but preferentially in the root
CC meristem. {ECO:0000269|PubMed:26163704}.
CC -!- INDUCTION: Inhibited by heat shock treatment.
CC {ECO:0000269|PubMed:20349287}.
CC -!- DISRUPTION PHENOTYPE: Short root length. Impaired cell division in the
CC root meristem. {ECO:0000269|PubMed:26163704}.
CC -!- SIMILARITY: Belongs to the p23/wos2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC19287.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80738.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ297951; CAC16575.1; -; mRNA.
DR EMBL; AF069298; AAC19287.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161494; CAB80738.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82173.1; -; Genomic_DNA.
DR EMBL; AY126999; AAM83226.1; -; mRNA.
DR EMBL; BT000527; AAN18096.1; -; mRNA.
DR PIR; T01305; T01305.
DR RefSeq; NP_192154.2; NM_116478.5. [Q8L7U4-1]
DR AlphaFoldDB; Q8L7U4; -.
DR SMR; Q8L7U4; -.
DR IntAct; Q8L7U4; 1.
DR MINT; Q8L7U4; -.
DR STRING; 3702.AT4G02450.1; -.
DR iPTMnet; Q8L7U4; -.
DR PaxDb; Q8L7U4; -.
DR PRIDE; Q8L7U4; -.
DR EnsemblPlants; AT4G02450.1; AT4G02450.1; AT4G02450. [Q8L7U4-1]
DR GeneID; 828006; -.
DR Gramene; AT4G02450.1; AT4G02450.1; AT4G02450. [Q8L7U4-1]
DR KEGG; ath:AT4G02450; -.
DR Araport; AT4G02450; -.
DR TAIR; locus:2133269; AT4G02450.
DR eggNOG; KOG3158; Eukaryota.
DR HOGENOM; CLU_078883_2_0_1; -.
DR InParanoid; Q8L7U4; -.
DR OMA; NALGMNM; -.
DR OrthoDB; 1461729at2759; -.
DR PRO; PR:Q8L7U4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8L7U4; baseline and differential.
DR GO; GO:0101031; C:chaperone complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0051087; F:chaperone binding; IDA:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; IDA:UniProtKB.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:UniProtKB.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR GO; GO:0080037; P:negative regulation of cytokinin-activated signaling pathway; IGI:TAIR.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:TAIR.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:2000012; P:regulation of auxin polar transport; IGI:TAIR.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0010449; P:root meristem growth; IMP:TAIR.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR045250; p23-like.
DR PANTHER; PTHR22932; PTHR22932; 1.
DR Pfam; PF04969; CS; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..241
FT /note="Co-chaperone protein p23-1"
FT /id="PRO_0000444946"
FT DOMAIN 2..91
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT REPEAT 129..131
FT /note="MGG 1"
FT REPEAT 132..134
FT /note="MGG 2"
FT REPEAT 135..137
FT /note="MGG 3"
FT REPEAT 138..140
FT /note="MGG 4"
FT REPEAT 141..143
FT /note="MGG 5"
FT REPEAT 144..146
FT /note="MGG 6"
FT REPEAT 147..149
FT /note="MGG 7"
FT REPEAT 150..152
FT /note="MGG 8"
FT REPEAT 162..164
FT /note="MGG 9"
FT REPEAT 165..167
FT /note="MGG 10"
FT REPEAT 168..170
FT /note="MGG 11"
FT REPEAT 171..173
FT /note="MGG 12"
FT REPEAT 180..182
FT /note="MGG 13"
FT REPEAT 183..185
FT /note="MGG 14"
FT REPEAT 186..188
FT /note="MGG 15"
FT REPEAT 189..191
FT /note="MGG 16"
FT REPEAT 192..194
FT /note="MGG 17"
FT REGION 129..194
FT /note="17 X 3 AA repeats of M-G-G"
FT REGION 188..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 154..164
FT /note="EGMDFSKLMGG -> GGMEGMDFSKL (in isoform 2)"
FT /id="VSP_059664"
FT CONFLICT 223
FT /note="L -> P (in Ref. 1; CAC16575)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 241 AA; 25471 MW; 7B05DE4B379B2C9F CRC64;
MSRHPEVKWA ETTEKIFLTV VLADTKDTKV NLDPEGVFDF SAKVGPENHV YELKLELADK
VNVEESKINI GERSIFCIIE KAEPERWNKL LRVKKPPHYV KVDWDKWVDE DDEGSAGAAD
MDMAGMEGMG GMGGMGGMGG MGGMGGMGGM GGMEGMDFSK LMGGMGGMGG MGGLEGLGGM
GGMGGMGGMG GMGGMEEFED SDDEEETAKS GDKKDDAVKE EGLATEKAPA AEETTSVKED
K
