ID   CD37L_BOVIN             Reviewed;         337 AA.
AC   A6H754;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Hsp90 co-chaperone Cdc37-like 1;
GN   Name=CDC37L1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19390049; DOI=10.1126/science.1169588;
RG   The bovine genome sequencing and analysis consortium;
RT   "The genome sequence of taurine cattle: a window to ruminant biology and
RT   evolution.";
RL   Science 324:522-528(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 116-337 (ISOFORM 1).
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-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: 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A6H754-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A6H754-2; Sequence=VSP_031211, VSP_031212;
CC   -!- SIMILARITY: Belongs to the CDC37 family. {ECO:0000305}.
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DR   EMBL; AAFC03000142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAFC03117968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC146118; AAI46119.1; -; mRNA.
DR   EMBL; DT850745; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001092401.1; NM_001098931.1. [A6H754-2]
DR   RefSeq; XP_005210020.1; XM_005209963.3. [A6H754-1]
DR   AlphaFoldDB; A6H754; -.
DR   SMR; A6H754; -.
DR   STRING; 9913.ENSBTAP00000022777; -.
DR   PaxDb; A6H754; -.
DR   PRIDE; A6H754; -.
DR   Ensembl; ENSBTAT00000022777; ENSBTAP00000022777; ENSBTAG00000017137. [A6H754-1]
DR   GeneID; 510572; -.
DR   KEGG; bta:510572; -.
DR   CTD; 55664; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017137; -.
DR   eggNOG; KOG2260; Eukaryota.
DR   GeneTree; ENSGT00530000063861; -.
DR   HOGENOM; CLU_046495_1_0_1; -.
DR   InParanoid; A6H754; -.
DR   OMA; GKWTKDD; -.
DR   OrthoDB; 786744at2759; -.
DR   TreeFam; TF101059; -.
DR   Reactome; R-BTA-114608; Platelet degranulation.
DR   Proteomes; UP000009136; Chromosome 8.
DR   Bgee; ENSBTAG00000017137; Expressed in oocyte and 104 other tissues.
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   Alternative splicing; Chaperone; Coiled coil; Cytoplasm; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..337
FT                   /note="Hsp90 co-chaperone Cdc37-like 1"
FT                   /id="PRO_0000318520"
FT   REGION          1..43
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          84..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"
FT   VAR_SEQ         305..306
FT                   /note="NP -> VS (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_031211"
FT   VAR_SEQ         307..337
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_031212"
SQ   SEQUENCE   337 AA;  38850 MW;  166A2FA829FAFF0F CRC64;
     MEQPWPPPGP WSLPRAEGEA EEESDLDLSP GSPRCPQLPG GGTQMYSHGI EMACQKQKEF
     VKSSVACKWN LAEAQQKLGS LALHNSESLD QEHAKAQTAI SELRQREEEW RQKEEALVQR
     ERMCLWNMDA ISKDVFNKSF INQDKRKETE DEDKSKSFMQ KHEQKIRHFG MLSRWDDSQR
     FLSDHPYLVC EETAKYLILW CFHLEAEQKG ALMEQIAHQA VVMQFIMEMA KNCNVDPRGC
     FRLFFQKAKA EEEGYFEAFK NELEAFKSRV RLYSQSPNFQ PVTVQNHVPH SGVGSIGLLE
     SLPQNPDYLQ YSINTALCSL NSVVHKEDDE PKMMDTV