ID F1NH83_CHICK Unreviewed; 310 AA.
AC F1NH83;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 3.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Hsp90 co-chaperone Cdc37-like 1 {ECO:0000256|ARBA:ARBA00040086};
GN Name=CDC37L1 {ECO:0000313|Ensembl:ENSGALP00010015187.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00010015187.1, ECO:0000313|Proteomes:UP000000539};
RN [1] {ECO:0000313|Ensembl:ENSGALP00010015187.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010015187.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Co-chaperone that binds to numerous proteins and promotes
CC their interaction with Hsp70 and Hsp90.
CC {ECO:0000256|ARBA:ARBA00037145}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the CDC37 family.
CC {ECO:0000256|ARBA:ARBA00006222}.
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DR RefSeq; XP_015135675.1; XM_015280189.1.
DR AlphaFoldDB; F1NH83; -.
DR SMR; F1NH83; -.
DR STRING; 9031.ENSGALP00000023285; -.
DR PaxDb; 9031-ENSGALP00000023285; -.
DR Ensembl; ENSGALT00010026632.1; ENSGALP00010015187.1; ENSGALG00010011133.1.
DR GeneID; 426535; -.
DR KEGG; gga:426535; -.
DR CTD; 55664; -.
DR VEuPathDB; HostDB:geneid_426535; -.
DR GeneTree; ENSGT00390000013443; -.
DR InParanoid; F1NH83; -.
DR OMA; GKWTKDD; -.
DR OrthoDB; 297041at2759; -.
DR Reactome; R-GGA-114608; Platelet degranulation.
DR Proteomes; UP000000539; Chromosome Z.
DR Bgee; ENSGALG00000014448; Expressed in spermatocyte and 14 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051087; F:protein-folding chaperone 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; Cdc37, Hsp90 binding domain; 1.
DR InterPro; IPR004918; Cdc37.
DR InterPro; IPR013874; Cdc37_Hsp90-bd.
DR InterPro; IPR038189; Cdc37_Hsp90-bd_sf.
DR PANTHER; PTHR12800; CDC37-RELATED; 1.
DR PANTHER; PTHR12800:SF2; HSP90 CO-CHAPERONE CDC37-LIKE 1; 1.
DR Pfam; PF08565; CDC37_M; 1.
DR SMART; SM01070; CDC37_M; 1.
DR SUPFAM; SSF101391; Hsp90 co-chaperone CDC37; 1.
PE 1: Evidence at protein level;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1NH83};
KW Reference proteome {ECO:0000313|Proteomes:UP000000539}.
FT DOMAIN 120..275
FT /note="Cdc37 Hsp90 binding"
FT /evidence="ECO:0000259|SMART:SM01070"
SQ SEQUENCE 310 AA; 36499 MW; 58EE0C6F03F5183C CRC64;
MALWFPRYRD GSPAVEEDEQ RELSPGSRQR LQTYSQEIEL ACQKEKEFVK HSVECTWNLA
EAQQKLGSLA LHNAESFDQE HAQAKTEVAE LRWREEEWRR KEEALNQGER QDLWNTDLVS
KEVFNKSFIN QKRKETEDED AAESFMKKHE QKIRHFGMMR RWDDSQRFLS DHPYLVSEET
SKYLMLWCFH LEAEQKRALM EQVAHQAVVM QFIIEIAKNC NVDPRGCFRL FFQKAKTGEG
YFEAFKSELE AFKTRVRIWS QSDSFQAILL YNPTVNPSLV EQLTSLSQNT GDLQGSTNTN
EEESKMMDTV
//
