ID A0A1J7H4P7_LUPAN Unreviewed; 223 AA.
AC A0A1J7H4P7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Co-chaperone protein p23 {ECO:0000256|RuleBase:RU369032};
GN ORFNames=TanjilG_14524 {ECO:0000313|EMBL:OIV95370.1};
OS Lupinus angustifolius (Narrow-leaved blue lupine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3871 {ECO:0000313|EMBL:OIV95370.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIV95370.1, ECO:0000313|Proteomes:UP000188354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC TISSUE=Whole plant {ECO:0000313|EMBL:OIV95370.1};
RX PubMed=27557478; DOI=10.1111/pbi.12615;
RA Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT an emerging health food: insights into plant-microbe interactions and
RT legume evolution.";
RL Plant Biotechnol. J. 15:318-330(2017).
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 EMBL; CM007376; OIV95370.1; -; Genomic_DNA.
DR RefSeq; XP_019417991.1; XM_019562446.1.
DR AlphaFoldDB; A0A1J7H4P7; -.
DR STRING; 3871.A0A1J7H4P7; -.
DR EnsemblPlants; OIV95370; OIV95370; TanjilG_14524.
DR GeneID; 109328840; -.
DR Gramene; OIV95370; OIV95370; TanjilG_14524.
DR KEGG; lang:109328840; -.
DR OMA; INGCHAR; -.
DR OrthoDB; 782824at2759; -.
DR Proteomes; UP000188354; Chromosome LG16.
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: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:UP000188354}.
FT DOMAIN 2..91
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT REGION 175..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 223 AA; 23585 MW; 210FDB8F16DB0DA7 CRC64;
MSRHPEVKWA QRAEKVYITV QLADSKDAKV DLTPDGVFAF SAGAGTGGNQ YELKLELFDK
VNVEESKINV GKRSIFCVVQ KAEDEWWKRL LRAEGKAPHY VKVDWDKWVD EDEDEGGEPD
MGGTDFSKFG GMGDDAMGGL GGMGGLGGMG GLGGMGGMDF SKLAGMGGDA MGGMDFSKFG
GMGDDIDGSD DEEQEVSNPG EQDAGKSTGD ASKDKQEAAP STS
//
