ID F7DES9_ORNAN Unreviewed; 378 AA.
AC F7DES9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 3.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Hsp90 co-chaperone Cdc37 {ECO:0000256|RuleBase:RU369110};
DE AltName: Full=Hsp90 chaperone protein kinase-targeting subunit {ECO:0000256|RuleBase:RU369110};
DE Contains:
DE RecName: Full=Hsp90 co-chaperone Cdc37, N-terminally processed {ECO:0000256|RuleBase:RU369110};
GN Name=CDC37 {ECO:0000313|Ensembl:ENSOANP00000021135.3};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000021135.3, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000021135.3, ECO:0000313|Proteomes:UP000002279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000021135.3,
RC ECO:0000313|Proteomes:UP000002279};
RX PubMed=18464734; DOI=10.1038/nature06936;
RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT "Genome analysis of the platypus reveals unique signatures of evolution.";
RL Nature 453:175-183(2008).
RN [2] {ECO:0000313|Ensembl:ENSOANP00000021135.3}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000021135.3};
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 composed of chaperones HSP90 and HSP70, co-
CC chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein
CC TSC2. Forms a complex composed of chaperones HSP90 and HSP70, co-
CC chaperones CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1
CC and NR3C1; this complex does not contain co-chaperones STIP1/HOP and
CC PTGES3/p23. Forms a complex with Hsp90/HSP90AB1 and CDK6. Interacts
CC with HSP90AA1. Interacts with AR, CDK4, CDK6 and EIF2AK1. Interacts
CC with RB1. Interacts with KSR1. Interacts with FLCN, FNIP1 and FNIP2.
CC {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 AlphaFoldDB; F7DES9; -.
DR STRING; 9258.ENSOANP00000021135; -.
DR Ensembl; ENSOANT00000021138.3; ENSOANP00000021135.3; ENSOANG00000013393.3.
DR eggNOG; KOG2260; Eukaryota.
DR GeneTree; ENSGT00390000013443; -.
DR HOGENOM; CLU_046495_0_0_1; -.
DR InParanoid; F7DES9; -.
DR OMA; CINLEME; -.
DR OrthoDB; 297041at2759; -.
DR TreeFam; TF101059; -.
DR Proteomes; UP000002279; Chromosome X2.
DR Bgee; ENSOANG00000013393; Expressed in fibroblast and 8 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:1990565; C:HSP90-CDC37 chaperone complex; IEA:Ensembl.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0019887; F:protein kinase regulator activity; IEA:Ensembl.
DR GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central.
DR GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0098779; P:positive regulation of mitophagy in response to mitochondrial depolarization; IEA:Ensembl.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0060334; P:regulation of type II interferon-mediated signaling pathway; IEA:Ensembl.
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:UP000002279}.
FT DOMAIN 1..131
FT /note="Cdc37 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01071"
FT DOMAIN 124..285
FT /note="Cdc37 Hsp90 binding"
FT /evidence="ECO:0000259|SMART:SM01070"
FT DOMAIN 289..376
FT /note="Cdc37 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01069"
FT REGION 351..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 40..112
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 363..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 378 AA; 44546 MW; A6592AF24CA9C0D1 CRC64;
MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRDCQRK
VAECQQKLKA LEVADREGEG AQGEWQRLQA EAQELRKEEK TWERKLDELH RKEKSMPWNV
DTLSRDGFSK SVFNVKPDQE EESEEQKEQK HKTFVEKYEA QIKHFGMLRR WDDSQKYLSD
HTHLVCEETA NYLVIWCIDL EVEEKCALME QVAHQTIVMQ FILELAKSLK VDPRACFRQF
FTKIKTADQQ YMEGFNDELE SFKERVRGRA KVRVERALQE YEEEERRKRL GPGGLDPVEV
YEALPVKLQK CFDVKDVQML QDTISQMDPT EAKYHMQRCI DSGLWVPNAK PASSLDKGEE
EAALLSAAAK KAEDKEHP
//
