P23B_ARATH
ID P23B_ARATH Reviewed; 150 AA.
AC Q6ID70; Q6DSR5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Co-chaperone protein p23-2 {ECO:0000305};
DE AltName: Full=Atp23-2 {ECO:0000303|PubMed:20349287};
GN Name=P23-2 {ECO:0000303|PubMed:21735091};
GN OrderedLocusNames=At3g03773 {ECO:0000312|Araport:AT3G03773};
GN ORFNames=F20H23.30 {ECO:0000312|EMBL:AC009540};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RA Xiao Y.-L., Underwood B.A., Moskal W.A. Jr., Torian U., Redman J.C.,
RA Wu H.C., Utterback T., Town C.D.;
RT "Reconstruction of cDNA sequences for hypothetical genes in Arabidopsis
RT thaliana from 5' and 3' RACE products.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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 PHOSPHORYLATION BY CK2, AND SUBCELLULAR LOCATION.
RX PubMed=21735091; DOI=10.1007/s11010-011-0969-0;
RA Tosoni K., Costa A., Sarno S., D'Alessandro S., Sparla F., Pinna L.A.,
RA Zottini M., Ruzzene M.;
RT "The p23 co-chaperone protein is a novel substrate of CK2 in Arabidopsis.";
RL Mol. Cell. Biochem. 356:245-254(2011).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
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).
RN [9] {ECO:0007744|PDB:2KMW}
RP STRUCTURE BY NMR OF 2-150.
RA Sahu S.C., Singh S., Tonelli M., Markley J.L.;
RT "Solution structure of At3g03773.1 protein from Arabidopsis thaliana.";
RL Submitted (AUG-2009) to the PDB data bank.
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 {ECO:0000269|PubMed:20349287}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21735091}. Nucleus
CC {ECO:0000269|PubMed:21735091}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ID70-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ID70-2; Sequence=VSP_015488, VSP_015489;
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 -!- PTM: Phosphorylated by casein kinase 2 in vitro.
CC {ECO:0000269|PubMed:21735091}.
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}.
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DR EMBL; AC009540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002686; AEE73986.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64317.1; -; Genomic_DNA.
DR EMBL; BT014803; AAT41786.1; -; mRNA.
DR EMBL; BT015020; AAT70471.1; -; mRNA.
DR EMBL; AY648332; AAT68743.1; -; mRNA.
DR EMBL; AY648333; AAT68744.1; -; mRNA.
DR EMBL; AY954843; AAX55169.1; -; mRNA.
DR RefSeq; NP_001326356.1; NM_001337483.1. [Q6ID70-2]
DR RefSeq; NP_683525.2; NM_148683.5. [Q6ID70-1]
DR PDB; 2KMW; NMR; -; A=2-150.
DR PDBsum; 2KMW; -.
DR AlphaFoldDB; Q6ID70; -.
DR BMRB; Q6ID70; -.
DR SMR; Q6ID70; -.
DR BioGRID; 6492; 2.
DR STRING; 3702.AT3G03773.2; -.
DR PaxDb; Q6ID70; -.
DR PRIDE; Q6ID70; -.
DR DNASU; 821159; -.
DR EnsemblPlants; AT3G03773.1; AT3G03773.1; AT3G03773. [Q6ID70-1]
DR EnsemblPlants; AT3G03773.3; AT3G03773.3; AT3G03773. [Q6ID70-2]
DR GeneID; 821159; -.
DR Gramene; AT3G03773.1; AT3G03773.1; AT3G03773. [Q6ID70-1]
DR Gramene; AT3G03773.3; AT3G03773.3; AT3G03773. [Q6ID70-2]
DR KEGG; ath:AT3G03773; -.
DR Araport; AT3G03773; -.
DR eggNOG; KOG3158; Eukaryota.
DR HOGENOM; CLU_078883_3_0_1; -.
DR InParanoid; Q6ID70; -.
DR OMA; RCKTNIG; -.
DR PhylomeDB; Q6ID70; -.
DR EvolutionaryTrace; Q6ID70; -.
DR PRO; PR:Q6ID70; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q6ID70; baseline and differential.
DR GO; GO:0101031; C:chaperone complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
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 3D-structure; Alternative splicing; Chaperone; Cytoplasm; Nucleus;
KW Reference proteome.
FT CHAIN 1..150
FT /note="Co-chaperone protein p23-2"
FT /id="PRO_0000218957"
FT DOMAIN 2..89
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT REGION 112..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 115..117
FT /note="SET -> CKS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_015488"
FT VAR_SEQ 118..150
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_015489"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:2KMW"
FT STRAND 13..20
FT /evidence="ECO:0007829|PDB:2KMW"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:2KMW"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:2KMW"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:2KMW"
FT STRAND 48..58
FT /evidence="ECO:0007829|PDB:2KMW"
FT STRAND 60..79
FT /evidence="ECO:0007829|PDB:2KMW"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2KMW"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:2KMW"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:2KMW"
SQ SEQUENCE 150 AA; 17366 MW; 79B0F24C9FFA724F CRC64;
MSRNPEVLWA QRSDKVYLTV ALPDAKDISV KCEPQGLFSF SALGAQGERF EFSLELYGKI
MTEYRKNVGL RNIIFSIQKE ERSWWTRLLK SEEKPAPYIK VDWNKWCDED EEVNSETASD
DESAFVNQDS ESSDDDGLLY LPDLEKARNK
