CD37L_DANRE
ID CD37L_DANRE Reviewed; 313 AA.
AC A7YY97;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Hsp90 co-chaperone Cdc37-like 1;
GN Name=cdc37l1; ORFNames=zgc:171475;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2007) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC152570; AAI52571.1; -; mRNA.
DR RefSeq; NP_001103296.2; NM_001109826.2.
DR AlphaFoldDB; A7YY97; -.
DR SMR; A7YY97; -.
DR STRING; 7955.ENSDARP00000110971; -.
DR PaxDb; A7YY97; -.
DR PeptideAtlas; A7YY97; -.
DR GeneID; 569357; -.
DR KEGG; dre:569357; -.
DR CTD; 55664; -.
DR ZFIN; ZDB-GENE-030131-8865; cdc37l1.
DR eggNOG; KOG2260; Eukaryota.
DR InParanoid; A7YY97; -.
DR OrthoDB; 786744at2759; -.
DR PhylomeDB; A7YY97; -.
DR Reactome; R-DRE-114608; Platelet degranulation.
DR PRO; PR:A7YY97; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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; IPR013873; Cdc37_C.
DR InterPro; IPR013874; Cdc37_Hsp90-bd.
DR InterPro; IPR038189; Cdc37_Hsp90-bd_sf.
DR PANTHER; PTHR12800; PTHR12800; 1.
DR Pfam; PF08564; CDC37_C; 1.
DR Pfam; PF08565; CDC37_M; 1.
DR SMART; SM01069; CDC37_C; 1.
DR SMART; SM01070; CDC37_M; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Cytoplasm; Reference proteome.
FT CHAIN 1..313
FT /note="Hsp90 co-chaperone Cdc37-like 1"
FT /id="PRO_0000318525"
SQ SEQUENCE 313 AA; 36371 MW; E7D1FABEABB92C4B CRC64;
MASLCQRQQH CVKASIASEW QLAEAQDQLC GLELHSSESV EQERARALAS STELSHTEHQ
WRLKERMLGT LCPEANRDVF DKSIINITQS WPNESDPDKS LNFVQRNEEL LKHFGMLGRW
DDSQRFLAEY HHLICEETAN YLILWCFRLQ AEKKEALMEQ VAHQAVVMQF ILEMARNTQQ
DPRGCFRHFF QKAKAGQEGY LDVFHTELQA FKDRVKEYTM KSTGETPKDT VHQNTPPACC
LDPKEVFESL PQELKTCIQM QDMQILQNVL SSMNPQVAEY HVKRCLEAGL WTNIPRTSKD
ESSEVDEWKM MET