ID H2LLR4_ORYLA Unreviewed; 369 AA.
AC H2LLR4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Hsp90 co-chaperone Cdc37 {ECO:0000256|ARBA:ARBA00020496, ECO:0000256|RuleBase:RU369110};
DE AltName: Full=Hsp90 chaperone protein kinase-targeting subunit {ECO:0000256|RuleBase:RU369110};
GN Name=CDC37 {ECO:0000313|Ensembl:ENSORLP00000006979.1};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000006979.1, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000006979.1, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000006979.1,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000006979.1}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000006979.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Co-chaperone that binds to numerous kinases and promotes
CC their interaction with the Hsp90 complex, resulting in stabilization
CC and promotion of their activity. {ECO:0000256|RuleBase:RU369110}.
CC -!- SUBUNIT: Forms a complex with Hsp90. {ECO:0000256|RuleBase:RU369110}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU369110}.
CC -!- SIMILARITY: Belongs to the CDC37 family.
CC {ECO:0000256|ARBA:ARBA00006222, ECO:0000256|RuleBase:RU369110}.
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DR RefSeq; XP_004071400.1; XM_004071352.2.
DR AlphaFoldDB; H2LLR4; -.
DR STRING; 8090.ENSORLP00000006979; -.
DR Ensembl; ENSORLT00000006980.2; ENSORLP00000006979.1; ENSORLG00000005543.2.
DR GeneID; 101156088; -.
DR KEGG; ola:101156088; -.
DR eggNOG; KOG2260; Eukaryota.
DR GeneTree; ENSGT00390000013443; -.
DR HOGENOM; CLU_046495_0_0_1; -.
DR InParanoid; H2LLR4; -.
DR OMA; CINLEME; -.
DR OrthoDB; 297041at2759; -.
DR TreeFam; TF101059; -.
DR Proteomes; UP000001038; Chromosome 8.
DR Bgee; ENSORLG00000005543; Expressed in blastula and 14 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR Gene3D; 6.10.140.250; -; 1.
DR Gene3D; 1.20.58.610; Cdc37, Hsp90 binding domain; 1.
DR InterPro; IPR004918; Cdc37.
DR InterPro; IPR013873; Cdc37_C.
DR InterPro; IPR013874; Cdc37_Hsp90-bd.
DR InterPro; IPR038189; Cdc37_Hsp90-bd_sf.
DR InterPro; IPR013855; Cdc37_N_dom.
DR PANTHER; PTHR12800; CDC37-RELATED; 1.
DR PANTHER; PTHR12800:SF3; HSP90 CO-CHAPERONE CDC37; 1.
DR Pfam; PF08564; CDC37_C; 1.
DR Pfam; PF08565; CDC37_M; 1.
DR Pfam; PF03234; CDC37_N; 1.
DR SMART; SM01069; CDC37_C; 1.
DR SMART; SM01070; CDC37_M; 1.
DR SMART; SM01071; CDC37_N; 1.
DR SUPFAM; SSF101391; Hsp90 co-chaperone CDC37; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|RuleBase:RU369110};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU369110};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038}.
FT DOMAIN 3..129
FT /note="Cdc37 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01071"
FT DOMAIN 122..283
FT /note="Cdc37 Hsp90 binding"
FT /evidence="ECO:0000259|SMART:SM01070"
FT DOMAIN 287..369
FT /note="Cdc37 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01069"
FT REGION 340..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 42..110
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 351..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 43856 MW; C1B63BD40036E090 CRC64;
MSRIDYSVWD HIEVSDDEDD THPNIDTPSL FRWRHQARVE RMEEFQKKGE DLKKGLAECR
RKLTELQTKI QDLNLSDGVK TELTKYQADE KKLKKEERDW EKKLDEYYRE EKKMPWNVDT
LSKEGFSKSI VNIKPETSED TEEEKEKKHK TFVEKHEKQI KHFGMLRRWD DSQKYLSDNP
HLVCEETANY LVIMCIDLEV EEKHALMEQV AHQTIVMQFI LELAKSLKVD PRGCFRQFFA
KIKTADQQYQ DAFNDELEAF KERVRGRAKI RIEKALKEYE EEERQKRLGP GGLDPVEVYE
SLPAEMQKCF DEKDIQMLQE VISKMDPTEA KHHMKRCIDS GLWVPNSGEG KEEEGTYEEV
KREPEETKE
//
