ID   P23A_BRANA              Reviewed;         178 AA.
AC   Q9FR62;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Co-chaperone protein p23-1 {ECO:0000305};
DE   AltName: Full=Bnp23-1 {ECO:0000303|PubMed:20349287};
GN   Name=P23-1 {ECO:0000305}; Synonyms=P23 {ECO:0000312|EMBL:AAG41763.1};
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Topas;
RA   Cordewener J.H.G., Jansen H.J., Hause G., Fiers M.A.,
RA   van Lookeren Campagne M.M.;
RT   "Bnp23, the plant ortholog of mammalian p23, is upregulated during
RT   microspore embryogenesis in Brassica napus.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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).
CC   -!- FUNCTION: Acts as a co-chaperone for HSP90.
CC       {ECO:0000269|PubMed:20349287}.
CC   -!- SUBUNIT: Interacts with HSP90 in an ATP-dependent manner.
CC       {ECO:0000269|PubMed:20349287}.
CC   -!- INDUCTION: Induced by heat shock treatment.
CC       {ECO:0000269|PubMed:20349287}.
CC   -!- SIMILARITY: Belongs to the p23/wos2 family. {ECO:0000305}.
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DR   EMBL; AF153128; AAG41763.1; -; mRNA.
DR   AlphaFoldDB; Q9FR62; -.
DR   SMR; Q9FR62; -.
DR   GO; GO:0101031; C:chaperone complex; 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: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   Chaperone.
FT   CHAIN           1..178
FT                   /note="Co-chaperone protein p23-1"
FT                   /id="PRO_0000444947"
FT   DOMAIN          2..91
FT                   /note="CS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT   REGION          112..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..154
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   178 AA;  20096 MW;  216EE6DA6777F46A CRC64;
     MSRHPTVKWA QRSDWVYITV ELPDAEDVKL KLEPEGKFFF SATSGASKTL YEVDLDLLDS
     VDVNESKASV SSRSVFYLVK KAESKWWNRL TKPEGKHPLY LKVDWDKWVD EDDEDKGGEG
     DMDFGDFDFN GLNMGDTDEI GEEVAEEDGD GEGETAAETK EKKIDGEKDE EGVNAKKD