ID A0A3L6RHH8_PANMI Unreviewed; 202 AA.
AC A0A3L6RHH8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Co-chaperone protein p23 {ECO:0000256|RuleBase:RU369032};
GN ORFNames=C2845_PM13G10560 {ECO:0000313|EMBL:RLN04007.1};
OS Panicum miliaceum (Proso millet) (Broomcorn millet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX NCBI_TaxID=4540 {ECO:0000313|EMBL:RLN04007.1, ECO:0000313|Proteomes:UP000275267};
RN [1] {ECO:0000313|Proteomes:UP000275267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT "The genome of broomcorn millet.";
RL Nat. Commun. 10:436-436(2019).
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:RLN04007.1}.
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DR EMBL; PQIB02000008; RLN04007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6RHH8; -.
DR STRING; 4540.A0A3L6RHH8; -.
DR Proteomes; UP000275267; Chromosome 13.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:UniProtKB-UniRule.
DR CDD; cd06465; p23_hB-ind1_like; 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:SF22; CO-CHAPERONE PROTEIN P23-1; 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:UP000275267}.
FT DOMAIN 2..89
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT REGION 158..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 202 AA; 21838 MW; BC8B5ABCC25CA7E5 CRC64;
MSRHPEVKWA QRIDKVYITV QLPDAKDAKV NLEPDGVFTF SGSAGTNLYE LKLDLNDKVN
VEASKISVGV RSIFCIVEKA EAKWWKKLVR DDQRAPHFVK VDWDKWVDED DDGGDVNLDG
MDFSNFGGMG GMGGMGDMAG LGGMGGLGGM TGMGGLGGMG MDEFEDESDD EEEVSKPQAA
EKADEAEKME AAEAKTETAQ SS
//
