CD37L_XENTR
ID CD37L_XENTR Reviewed; 285 AA.
AC Q28HY7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Hsp90 co-chaperone Cdc37-like 1;
GN Name=cdc37l1; ORFNames=TEgg077n10.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) 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: Forms complexes with Hsp70 and Hsp90. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CDC37 family. {ECO:0000305}.
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DR EMBL; CR760680; CAJ82202.1; -; mRNA.
DR RefSeq; NP_001037905.1; NM_001044440.1.
DR AlphaFoldDB; Q28HY7; -.
DR SMR; Q28HY7; -.
DR PaxDb; Q28HY7; -.
DR GeneID; 733511; -.
DR KEGG; xtr:733511; -.
DR CTD; 55664; -.
DR Xenbase; XB-GENE-984706; cdc37l1.
DR eggNOG; KOG2260; Eukaryota.
DR InParanoid; Q28HY7; -.
DR OrthoDB; 786744at2759; -.
DR Reactome; R-XTR-114608; Platelet degranulation.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..285
FT /note="Hsp90 co-chaperone Cdc37-like 1"
FT /id="PRO_0000318526"
FT REGION 34..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 35..73
FT /evidence="ECO:0000255"
FT COMPBIAS 34..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 285 AA; 32880 MW; D72A0B3CFC261AA5 CRC64;
MDFSHSQQNE CARSSVACKW SLAEAQQKLN SLALHNSESM DQEQAMAQAE LSELQRSEEE
WRRKEAALSQ GENWGLPTTD GLNQDVFNKS FINQVKKSID GEDQSISFIQ KYEAKIRHFG
MLSRWNDSQH FLSEYPDLVS EETAKYLLLW CSHLESEQKT ALMEQVAHQA VVMQFIIEMA
KSCNMDPRGC FRLFFQKAKE EKEGYFEAFK SELEILKSKV RQHAECQRYE AAILRKPAFP
PDLGHMGTQQ CHQKDVLQSH PNAAVCHLNP MEHAEDEDLK MMDTL