ID B9SI84_RICCO Unreviewed; 144 AA.
AC B9SI84;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Co-chaperone protein p23 {ECO:0000256|RuleBase:RU369032};
GN ORFNames=RCOM_1321760 {ECO:0000313|EMBL:EEF36686.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
CC -!- FUNCTION: Acts as a co-chaperone for HSP90.
CC {ECO:0000256|RuleBase:RU369032}.
CC -!- SUBUNIT: Interacts with HSP90 in an ATP-dependent manner.
CC {ECO:0000256|RuleBase:RU369032}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU369032}.
CC Nucleus {ECO:0000256|RuleBase:RU369032}.
CC -!- SIMILARITY: Belongs to the p23/wos2 family.
CC {ECO:0000256|ARBA:ARBA00025733, ECO:0000256|RuleBase:RU369032}.
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DR EMBL; EQ973969; EEF36686.1; -; Genomic_DNA.
DR AlphaFoldDB; B9SI84; -.
DR STRING; 3988.B9SI84; -.
DR eggNOG; KOG3158; Eukaryota.
DR InParanoid; B9SI84; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051879; F:Hsp90 protein binding; IBA:GO_Central.
DR GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central.
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:0006950; P:response to stress; IEA:UniProt.
DR CDD; cd06465; p23_hB-ind1_like; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 6.10.140.350; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR045250; p23-like.
DR PANTHER; PTHR22932:SF1; CO-CHAPERONE PROTEIN DAF-41; 1.
DR PANTHER; PTHR22932; TELOMERASE-BINDING PROTEIN P23 HSP90 CO-CHAPERONE; 1.
DR Pfam; PF04969; CS; 1.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR PROSITE; PS51203; CS; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|RuleBase:RU369032};
KW Cytoplasm {ECO:0000256|RuleBase:RU369032};
KW Nucleus {ECO:0000256|RuleBase:RU369032};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311}.
FT DOMAIN 2..90
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT REGION 112..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 144 AA; 16237 MW; D85E1093F1113498 CRC64;
MSRHPEVLWA QRSDKVYLTI ALPDAKNISV KCEAEGLFSF SAVGIQGESF DFTLQLYGSV
IPEGCKTNVG LRNIICSVQK QEKGWWKRLL KSEEKPAPYI KVDWNKWCDE DDEESTSDLA
SDGDNDAYDD DNDESSDDDG MLCE
//
