ID Q684M6_PIG Unreviewed; 380 AA.
AC Q684M6; A0A4X1V502;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 124.
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|EMBL:CAG15149.1,
GN ECO:0000313|Ensembl:ENSSSCP00000050349.1,
GN ECO:0000313|VGNC:VGNC:86450};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:CAG15149.1};
RN [1] {ECO:0000313|EMBL:CAG15149.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9677330;
RA Sullivan M., Rena G., Begg F., Gordon L., Olsen A.S., Houslay M.D.;
RT "Identification and characterization of the human homologue of the short
RT PDE4A cAMP-specific phosphodiesterase 4A variant RD1 (PDE4A1) by analysis
RT of the human HSPDE4A gene locus located at chromosome 19p13.2.";
RL Biochem. J. 333:693-703(1998).
RN [2] {ECO:0000313|EMBL:CAG15149.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11306681;
RA Rena G., Begg F., Ross A., MacKenzie C., McPhee I., Campbell L., Huston E.,
RA Sullivan M., Houslay M.D.;
RT "Molecular cloning, genomic positioning, promoter identification, and
RT characterization of the novel cyclic AMP-specific phosphodiesterase
RT PDE4A10.";
RL Mol. Pharmacol. 59:996-1011(2001).
RN [3] {ECO:0000313|EMBL:CAG15149.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15305063; DOI=10.1159/000079578;
RA Leeb T., Martins-Wess F., Kuiper H., Distl O., Muller M.;
RT "Molecular characterization of the porcine TYK2 gene on SSC 2q1.3 ->
RT q2.1.";
RL Cytogenet. Genome Res. 107:103-107(2004).
RN [4] {ECO:0000313|Ensembl:ENSSSCP00000050349.1, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000050349.1,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|Ensembl:ENSSSCP00005033454.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; AJ632303; CAG15149.1; -; Genomic_DNA.
DR RefSeq; NP_001116568.1; NM_001123096.1.
DR STRING; 9823.ENSSSCP00000050349; -.
DR PaxDb; 9823-ENSSSCP00000014507; -.
DR Ensembl; ENSSSCT00000045428.3; ENSSSCP00000050349.1; ENSSSCG00000013647.4.
DR Ensembl; ENSSSCT00005054264.1; ENSSSCP00005033454.1; ENSSSCG00005033812.1.
DR GeneID; 100141402; -.
DR KEGG; ssc:100141402; -.
DR CTD; 11140; -.
DR VGNC; VGNC:86450; CDC37.
DR eggNOG; KOG2260; Eukaryota.
DR GeneTree; ENSGT00390000013443; -.
DR HOGENOM; CLU_046495_0_0_1; -.
DR OrthoDB; 297041at2759; -.
DR TreeFam; TF101059; -.
DR Reactome; R-SSC-1227986; Signaling by ERBB2.
DR Reactome; R-SSC-5675482; Regulation of necroptotic cell death.
DR Reactome; R-SSC-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-SSC-9652282; Drug-mediated inhibition of ERBB2 signaling.
DR Proteomes; UP000008227; Chromosome 2.
DR Bgee; ENSSSCG00000013647; Expressed in forelimb bud and 43 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:0051301; P:cell division; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Cell cycle {ECO:0000313|EMBL:CAG15149.1};
KW Cell division {ECO:0000313|EMBL:CAG15149.1};
KW Chaperone {ECO:0000256|RuleBase:RU369110};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU369110};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q684M6};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227}.
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..380
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 344..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 40..110
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 380 AA; 44490 MW; B91BB7F98976261D CRC64;
MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK
VAECQRKLKE LEVAEGEGGE AELERLQAEA QQLLKEERSW 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 SEAKEGEEAG
PGDPLLEAAS KSGDEKDVSA
//
