ID A0A0B0MDW9_GOSAR Unreviewed; 182 AA.
AC A0A0B0MDW9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 13-SEP-2023, entry version 33.
DE RecName: Full=Co-chaperone protein p23 {ECO:0000256|RuleBase:RU369032};
GN ORFNames=F383_14672 {ECO:0000313|EMBL:KHF97613.1};
OS Gossypium arboreum (Tree cotton) (Gossypium nanking).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29729 {ECO:0000313|EMBL:KHF97613.1, ECO:0000313|Proteomes:UP000032142};
RN [1] {ECO:0000313|Proteomes:UP000032142}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. AKA8401 {ECO:0000313|Proteomes:UP000032142};
RA Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA Wilkins T.A.;
RL Submitted (SEP-2014) 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:KHF97613.1}.
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DR EMBL; JRRC01012571; KHF97613.1; -; Genomic_DNA.
DR RefSeq; XP_017637829.1; XM_017782340.1.
DR AlphaFoldDB; A0A0B0MDW9; -.
DR SMR; A0A0B0MDW9; -.
DR GeneID; 108479626; -.
DR KEGG; gab:108479626; -.
DR OMA; KMHFLKT; -.
DR OrthoDB; 782824at2759; -.
DR Proteomes; UP000032142; Unassembled WGS sequence.
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 InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR045250; p23-like.
DR PANTHER; PTHR22932:SF11; EXPRESSED PROTEIN; 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:UP000032142}.
SQ SEQUENCE 182 AA; 20496 MW; 8C8E9CFDF10893B9 CRC64;
MSRHPIVKWA QRLDDVFITI ELPDAQDVKL KLEPEGKFFF SAKSGADKIP YEVDLDLHDK
VDVDGSKASV GNRNICYLVK KAESKWWSRL LKQEGRPPVF LKVDWDRWVD EDEDDVDTKP
APDMDFGDFD FSKMNMGGGE GFGAVEGEDD DDSDTEDENV EEIPAPKKDA SSSGAEHEVK
NV
//