CDC37_CAEEL
ID CDC37_CAEEL Reviewed; 370 AA.
AC O02108;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Probable Hsp90 co-chaperone cdc37;
DE AltName: Full=Cell division cycle-related protein 37;
DE AltName: Full=Hsp90 chaperone protein kinase-targeting subunit;
GN Name=cdc-37; ORFNames=W08F4.8;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, INTERACTION WITH DAF-21, PHOSPHORYLATION, AND DEPHOSPHORYLATION
RP BY PPH-5.
RX PubMed=23569206; DOI=10.1074/jbc.m112.439257;
RA Eckl J.M., Rutz D.A., Haslbeck V., Zierer B.K., Reinstein J., Richter K.;
RT "Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90)
RT motility by interaction with N-terminal and middle domain binding sites.";
RL J. Biol. Chem. 288:16032-16042(2013).
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 (By similarity). Inhibits daf-21/Hsp90
CC ATPase activity (PubMed:23569206). {ECO:0000250|UniProtKB:Q16543,
CC ECO:0000269|PubMed:23569206}.
CC -!- SUBUNIT: Forms a complex with daf-21/Hsp90 (PubMed:23569206). Interacts
CC with a number of kinases (By similarity).
CC {ECO:0000250|UniProtKB:Q16543, ECO:0000269|PubMed:23569206}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Phosphorylated. Dephosphorylated by pph-5.
CC {ECO:0000269|PubMed:23569206}.
CC -!- SIMILARITY: Belongs to the CDC37 family. {ECO:0000305}.
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DR EMBL; FO080468; CCD63937.1; -; Genomic_DNA.
DR PIR; T34050; T34050.
DR RefSeq; NP_001040820.1; NM_001047355.3.
DR AlphaFoldDB; O02108; -.
DR SMR; O02108; -.
DR BioGRID; 38826; 15.
DR ComplexPortal; CPX-3983; Hsp90-cdc-37-pph-5 phosphatase complex.
DR ComplexPortal; CPX-3984; Hsp90-Cdc37 chaperone complex.
DR ComplexPortal; CPX-4002; Hsp90-cdc-37-aha-1 complex.
DR DIP; DIP-25193N; -.
DR IntAct; O02108; 8.
DR STRING; 6239.W08F4.8b; -.
DR EPD; O02108; -.
DR PaxDb; O02108; -.
DR PeptideAtlas; O02108; -.
DR EnsemblMetazoa; W08F4.8a.1; W08F4.8a.1; WBGene00021097.
DR EnsemblMetazoa; W08F4.8a.2; W08F4.8a.2; WBGene00021097.
DR UCSC; W08F4.8b; c. elegans.
DR WormBase; W08F4.8a; CE14726; WBGene00021097; cdc-37.
DR eggNOG; KOG2260; Eukaryota.
DR HOGENOM; CLU_046495_0_0_1; -.
DR InParanoid; O02108; -.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR Reactome; R-CEL-1227986; Signaling by ERBB2.
DR Reactome; R-CEL-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-CEL-9652282; Drug-mediated inhibition of ERBB2 signaling.
DR PRO; PR:O02108; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00021097; Expressed in adult organism and 4 other tissues.
DR ExpressionAtlas; O02108; baseline and differential.
DR GO; GO:0101031; C:chaperone complex; IDA:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:1990565; C:HSP90-CDC37 chaperone complex; IDA:ComplexPortal.
DR GO; GO:0008287; C:protein serine/threonine phosphatase complex; IC:ComplexPortal.
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:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0022417; P:protein maturation by protein folding; IC:ComplexPortal.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0045859; P:regulation of protein kinase activity; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..370
FT /note="Probable Hsp90 co-chaperone cdc37"
FT /id="PRO_0000195062"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 370 AA; 42706 MW; A53FB7BD49905BF4 CRC64;
MPIDYSKWKD IEVSDDEDDT HPNIDTPSLF RWRHQARLER MAEKKMEQEK IDKEKGTTSK
KMEELEKKLA AADVTDKSDI QKQIDEVKAQ EEAWRKKEAE LEEKERLEPW NVDTIGHEAF
STSRINKITE KKPQAPKTDE EDTHAMSTFF ETHESLLEKM AVLKNGAKST ELFLAEHPHM
ASEYTANWLT IEALNAAIDF NEEKMKTMAE QCIIIQYLLE LSKSLNAVAT NTTVQKQFFK
KFEAAEPVYM KHYQDEVKAF EDRLRTRAQT KRDAAMEEAE AEEKAERMKS APGGIDPQEV
FEQLPEEMRK CFEAHDIEAL KGVAQKMDEE VFKYHFDRCI ASGLWVPGKA DDDDDDEEAA
PAEEEPTTSS
