ID A0A1U7UZL1_NICSY Unreviewed; 152 AA.
AC A0A1U7UZL1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Co-chaperone protein p23 {ECO:0000256|RuleBase:RU369032};
GN Name=LOC104212105 {ECO:0000313|RefSeq:XP_009759593.1};
OS Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4096 {ECO:0000313|Proteomes:UP000189701, ECO:0000313|RefSeq:XP_009759593.1};
RN [1] {ECO:0000313|Proteomes:UP000189701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA Peitsch M.C., Ivanov N.V.;
RT "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT tomentosiformis.";
RL Genome Biol. 14:R60.1-R60.17(2013).
RN [2] {ECO:0000313|RefSeq:XP_009759593.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_009759593.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_009759593.1; XM_009761291.1.
DR AlphaFoldDB; A0A1U7UZL1; -.
DR SMR; A0A1U7UZL1; -.
DR GeneID; 104212105; -.
DR OrthoDB; 782824at2759; -.
DR Proteomes; UP000189701; Unplaced.
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 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:UP000189701}.
FT DOMAIN 2..93
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT REGION 112..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..138
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 152 AA; 17325 MW; EE878764529D1C21 CRC64;
MSRQPEVLWA QRSEKIYLTI SLPDAKDVTL KCEGDGVFNF CAVGVQGDSF TFTLQLYGNI
SPERSKRCKT NVGLRNILCS IQKEQKGWWP RLLKSEEKPA PYLKVDWNKW CDEDDEESSD
SDDDVEYTGE DDESSDDGGM LYLPDLEKAR GN
//
