ID G1PKD5_MYOLU Unreviewed; 378 AA.
AC G1PKD5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:ENSMLUP00000011253.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000011253.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000011253.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000011253.2}
RP IDENTIFICATION.
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 EMBL; AAPE02048874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006104110.2; XM_006104048.2.
DR AlphaFoldDB; G1PKD5; -.
DR STRING; 59463.ENSMLUP00000011253; -.
DR Ensembl; ENSMLUT00000012360.2; ENSMLUP00000011253.2; ENSMLUG00000012357.2.
DR GeneID; 102433533; -.
DR KEGG; mlf:102433533; -.
DR CTD; 11140; -.
DR eggNOG; KOG2260; Eukaryota.
DR GeneTree; ENSGT00390000013443; -.
DR HOGENOM; CLU_046495_0_0_1; -.
DR InParanoid; G1PKD5; -.
DR OMA; CINLEME; -.
DR OrthoDB; 297041at2759; -.
DR TreeFam; TF101059; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:1990565; C:HSP90-CDC37 chaperone complex; IEA:Ensembl.
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:0097110; F:scaffold protein binding; IEA:Ensembl.
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: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:UP000001074}.
FT DOMAIN 1..129
FT /note="Cdc37 N-terminal"
FT /evidence="ECO:0000259|SMART:SM01071"
FT DOMAIN 122..284
FT /note="Cdc37 Hsp90 binding"
FT /evidence="ECO:0000259|SMART:SM01070"
FT DOMAIN 288..378
FT /note="Cdc37 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01069"
FT REGION 125..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 40..110
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 351..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 378 AA; 44609 MW; EE34EAD49CD4BB59 CRC64;
MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRSCRECKRK
VVECQRKLKE LEVAEDEGSK VELERLQAEA QQLRKEERSW EQKLEEMRKK EKSMPWNVDT
LSKDGFSKSM VNTKPEQVEE ESEEVREQKH KTFVEKYEKQ IKHFGMLHRW DDSQKYLSDN
AHLVCEETAN YLVIWCIDLE VEEKCALMEQ VAHQTIVMQF ILELAKSLKV DPRACFRQFF
TKIKTADRQY MEGFNDELEA FKERVRGRAK LRIEKAMKEY EEEERKKRLG PGGLDPVEVY
ESLPEELQKC FDVKDVQMLQ DAISKMDPSD AKYHMQRCID SGLWVPNSKS SEAKEGEEAG
PGDPLLEAVK PDEKDVSA
//
