ID   CD37L_RAT               Reviewed;         335 AA.
AC   Q5XIC3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Hsp90 co-chaperone Cdc37-like 1;
GN   Name=Cdc37l1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Co-chaperone that binds to numerous proteins and promotes
CC       their interaction with Hsp70 and Hsp90. {ECO:0000250}.
CC   -!- SUBUNIT: Self-associates. Forms complexes with Hsp70 and Hsp90.
CC       Interacts with CDC37, FKBP4, PPID and STIP1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CDC37 family. {ECO:0000305}.
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DR   EMBL; BC083761; AAH83761.1; -; mRNA.
DR   RefSeq; NP_001011941.1; NM_001011941.1.
DR   AlphaFoldDB; Q5XIC3; -.
DR   SMR; Q5XIC3; -.
DR   STRING; 10116.ENSRNOP00000016000; -.
DR   PaxDb; Q5XIC3; -.
DR   Ensembl; ENSRNOT00000016000; ENSRNOP00000016000; ENSRNOG00000010967.
DR   GeneID; 293886; -.
DR   KEGG; rno:293886; -.
DR   CTD; 55664; -.
DR   RGD; 1309295; Cdc37l1.
DR   eggNOG; KOG2260; Eukaryota.
DR   GeneTree; ENSGT00390000013443; -.
DR   InParanoid; Q5XIC3; -.
DR   OMA; GKWTKDD; -.
DR   OrthoDB; 786744at2759; -.
DR   PhylomeDB; Q5XIC3; -.
DR   TreeFam; TF101059; -.
DR   Reactome; R-RNO-114608; Platelet degranulation.
DR   PRO; PR:Q5XIC3; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000010967; Expressed in quadriceps femoris and 19 other tissues.
DR   ExpressionAtlas; Q5XIC3; baseline and differential.
DR   Genevisible; Q5XIC3; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR   Gene3D; 1.20.58.610; -; 1.
DR   InterPro; IPR004918; Cdc37.
DR   InterPro; IPR013874; Cdc37_Hsp90-bd.
DR   InterPro; IPR038189; Cdc37_Hsp90-bd_sf.
DR   PANTHER; PTHR12800; PTHR12800; 1.
DR   Pfam; PF08565; CDC37_M; 1.
DR   SMART; SM01070; CDC37_M; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..335
FT                   /note="Hsp90 co-chaperone Cdc37-like 1"
FT                   /id="PRO_0000318524"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2..170
FT                   /note="Self-association"
FT                   /evidence="ECO:0000250"
FT   REGION          147..276
FT                   /note="Self-association and interaction with Hsp90"
FT                   /evidence="ECO:0000250"
FT   REGION          266..335
FT                   /note="Interaction with Hsp70"
FT                   /evidence="ECO:0000250"
FT   REGION          277..335
FT                   /note="Required for interaction with STIP1"
FT                   /evidence="ECO:0000250"
FT   COILED          84..120
FT                   /evidence="ECO:0000255"
FT   MOD_RES         32
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L3B6"
FT   MOD_RES         88
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L3B6"
SQ   SEQUENCE   335 AA;  38315 MW;  8D14DE43F9FEC937 CRC64;
     MEQPWPPPGP WSFPRTGGET EEESDLDVSP SSSHYSPVPD GGAQMYSHGI ELACQRQKEF
     VKSSVACKWN LAEAQQKLGS LALHNSESLD QEHAKAQTAV SELRQREEEW RQKEEALVQR
     ERTCLWNVDA ISKDVFNKSF INQDKRKTED EDKSQSFMQK YEQKIRHFGM LSRWDDSQRF
     LSDHPYLVCE ETAKYLILWC FHLEAEQKGA LMEQIAHQAV VMQFIMEMAK NCNVDPRGCF
     RLFFQKAKAE EEGYFEAFKN ELEAFKARVR LYAQSQSFAP VTVENHAPHS GVGCIGSAEP
     LPQNPDSLQC CPPAPLCSVD SVVHKEDDDR MMDTV