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Database: UniProt
Entry: A0AAD4X845_9MAGN
LinkDB: A0AAD4X845_9MAGN
Original site: A0AAD4X845_9MAGN 
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}.
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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
//
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