ID A0AAD4X845_9MAGN Unreviewed; 115 AA.
AC A0AAD4X845;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 7.
DE RecName: Full=Co-chaperone protein p23 {ECO:0000256|RuleBase:RU369032};
GN ORFNames=MKW98_008672 {ECO:0000313|EMBL:KAI3862832.1};
OS Papaver atlanticum.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Papaver.
OX NCBI_TaxID=357466 {ECO:0000313|EMBL:KAI3862832.1, ECO:0000313|Proteomes:UP001202328};
RN [1] {ECO:0000313|EMBL:KAI3862832.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S-188037 {ECO:0000313|EMBL:KAI3862832.1};
RA Catania T.;
RT "A functionally conserved STORR gene fusion in Papaver species that
RT diverged 16.8 million years ago.";
RL Submitted (APR-2022) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAI3862832.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JAJJMB010014087; KAI3862832.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAD4X845; -.
DR Proteomes; UP001202328; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0101031; C:protein folding chaperone complex; IEA:UniProtKB-ARBA.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:TreeGrafter.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:TreeGrafter.
DR GO; GO:0006457; P:protein folding; IEA:TreeGrafter.
DR CDD; cd06465; p23_hB-ind1_like; 1.
DR FunFam; 2.60.40.790:FF:000013; Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase; 1.
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:SF10; CO-CHAPERONE PROTEIN P23; 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:UP001202328}.
FT DOMAIN 2..89
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
SQ SEQUENCE 115 AA; 13540 MW; 0D93CB4B6DD7BE89 CRC64;
MSRHPTIKWA QRSDKIFLTV DLPDADDVKL KLEPQGRFVF SATKDGIPYE VDVELYDKIN
AEESKVNNGV RNIVYVIKKT ESKWWDRLLK QEGKPPVFFK VDWDKWIDED DEKGI
//