ID   CD37L_PONAB             Reviewed;         337 AA.
AC   Q5RA87;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Hsp90 co-chaperone Cdc37-like 1;
GN   Name=CDC37L1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR859131; CAH91323.1; -; mRNA.
DR   RefSeq; NP_001125782.1; NM_001132310.1.
DR   AlphaFoldDB; Q5RA87; -.
DR   SMR; Q5RA87; -.
DR   STRING; 9601.ENSPPYP00000021554; -.
DR   Ensembl; ENSPPYT00000057629; ENSPPYP00000040429; ENSPPYG00000019246.
DR   GeneID; 100172709; -.
DR   KEGG; pon:100172709; -.
DR   CTD; 55664; -.
DR   eggNOG; KOG2260; Eukaryota.
DR   GeneTree; ENSGT00390000013443; -.
DR   HOGENOM; CLU_046495_1_0_1; -.
DR   InParanoid; Q5RA87; -.
DR   OrthoDB; 786744at2759; -.
DR   Proteomes; UP000001595; Chromosome 9.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
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..337
FT                   /note="Hsp90 co-chaperone Cdc37-like 1"
FT                   /id="PRO_0000318523"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2..171
FT                   /note="Self-association"
FT                   /evidence="ECO:0000250"
FT   REGION          147..277
FT                   /note="Self-association and interaction with Hsp90"
FT                   /evidence="ECO:0000250"
FT   REGION          267..337
FT                   /note="Interaction with Hsp70"
FT                   /evidence="ECO:0000250"
FT   REGION          278..337
FT                   /note="Required for interaction with STIP1"
FT                   /evidence="ECO:0000250"
FT   COILED          85..122
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   337 AA;  38927 MW;  5881A1032ED41D51 CRC64;
     MEQPWPPPGP WSLPRAEGEA EEENDLDVFP SSPRCPQLPG GSAQMYSHGI ELACQKQKEF
     VKSSVACKWN LAEAQQKLGS LALHNSESLD QEHAKAQIAV SELRQREEEW RQKEEALVQR
     EKMCLWSMDA ISKDVFNKSF INQDKRKDTE DEDKSESFMQ KYEQKIRHFG MLSRWDDSQR
     FLSDHPYLVC EETAKYLILW CFHLEAEKKG ALMEQIAHQA VVMQFIMEMA KNCNVDPRGC
     FRLFFQKAKA EEEGYFEAFK NELEAFKSRV RLYSQSQSFQ PMTVQNHVPH SGVGSIGLLE
     SLPQNPDYLQ YSINTALCSL NSVVHKEDDE PKMMDTV