CDC37_BOVIN
ID CDC37_BOVIN Reviewed; 380 AA.
AC Q5EAC6;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Hsp90 co-chaperone Cdc37;
DE AltName: Full=Hsp90 chaperone protein kinase-targeting subunit;
DE AltName: Full=p50Cdc37;
DE Contains:
DE RecName: Full=Hsp90 co-chaperone Cdc37, N-terminally processed;
GN Name=CDC37;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. Inhibits HSP90AA1 ATPase activity.
CC {ECO:0000250|UniProtKB:Q16543}.
CC -!- SUBUNIT: Probably forms a complex composed of chaperones HSP90 and
CC HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and
CC client protein TSC2. Probably forms a complex composed of chaperones
CC HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client protein
CC TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain co-
CC chaperones STIP1/HOP and PTGES3/p23. Forms a complex with
CC Hsp90/HSP90AB1 and CDK6 (By similarity). Interacts with HSP90AA1.
CC Interacts with AR, CDK4, CDK6 and EIF2AK1. Interacts with RB1.
CC Interacts with KSR1. Interacts with FLCN, FNIP1 and FNIP2.
CC {ECO:0000250|UniProtKB:Q16543, ECO:0000250|UniProtKB:Q63692}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16543}.
CC -!- PTM: Constitutively sumoylated by UBE2I.
CC {ECO:0000250|UniProtKB:Q16543}.
CC -!- SIMILARITY: Belongs to the CDC37 family. {ECO:0000305}.
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DR EMBL; BT020643; AAX08660.1; -; mRNA.
DR EMBL; BC102043; AAI02044.1; -; mRNA.
DR RefSeq; NP_001030415.1; NM_001035338.1.
DR AlphaFoldDB; Q5EAC6; -.
DR BMRB; Q5EAC6; -.
DR SMR; Q5EAC6; -.
DR STRING; 9913.ENSBTAP00000036036; -.
DR PeptideAtlas; Q5EAC6; -.
DR PRIDE; Q5EAC6; -.
DR Ensembl; ENSBTAT00000036173; ENSBTAP00000036036; ENSBTAG00000011699.
DR GeneID; 520883; -.
DR KEGG; bta:520883; -.
DR CTD; 11140; -.
DR VEuPathDB; HostDB:ENSBTAG00000011699; -.
DR VGNC; VGNC:106679; CDC37.
DR GeneTree; ENSGT00390000013443; -.
DR InParanoid; Q5EAC6; -.
DR OMA; IWCINLE; -.
DR OrthoDB; 786744at2759; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000011699; Expressed in vas deferens and 106 other 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
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: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:0060334; P:regulation of interferon-gamma-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0045859; P:regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
DR Gene3D; 1.20.58.610; -; 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; PTHR12800; 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.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..380
FT /note="Hsp90 co-chaperone Cdc37"
FT /id="PRO_0000423196"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16543"
FT CHAIN 2..380
FT /note="Hsp90 co-chaperone Cdc37, N-terminally processed"
FT /id="PRO_0000283717"
FT REGION 124..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q16543"
FT MOD_RES 2
FT /note="N-acetylvaline; in Hsp90 co-chaperone Cdc37, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:Q16543"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16543"
FT MOD_RES 80
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16543"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16543"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16543"
FT MOD_RES 156
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16543"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16543"
SQ SEQUENCE 380 AA; 44580 MW; BD690D918E73975D CRC64;
MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK
VAECQRKLKE LEVAEGEGGK AELERLQAEA QQLRKEERSW EQKLEEMRKK EKSMPWNVDT
LSKDGFSKSM VNTKPEQAEE ESEEVREQKH KTFVEKYEKQ IKHFGMLRRW DDSQKYLSDN
VHLVCEETAN YLVIWCIDLE VEEKCALMEQ VAHQTIVMQF ILELAKSLKV DPRACFRQFF
TKIKTADRQY MEGFNDELEA FKDRVRGRAK LRIEKAMKEY EEEERKKRLG PGGLDPVEVY
ESLPEELQKC FDAKDVQMLQ DAISKMDPTD AKYHMQRCID SGLWVPNSKS SEAKDGEEAG
TGDPLLEATS KSGDEKDVSV
