ID   CCD62_MOUSE             Reviewed;         701 AA.
AC   E9PVD1; F6WEA5;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Coiled-coil domain-containing protein 62;
GN   Name=Ccdc62;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: Nuclear receptor coactivator that can enhance preferentially
CC       estrogen receptors ESR1 and ESR2 transactivation. Modulates also
CC       progesterone/PGR, glucocorticoid/NR3C1 and androgen/AR receptors
CC       transactivation, although at lower level; little effect on vitamin D
CC       receptor/VDR (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ESR1 and ESR2 in the presence of estradiol/E2.
CC       The interaction with ESR2 recruits CCDC62 to ER target genes, including
CC       cyclin-D1/CCND1 AP-1 promoter (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus. Note=Mainly
CC       nuclear. {ECO:0000250}.
CC   -!- DOMAIN: Contains 2 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. The first one is
CC       essential for the association with ESR1 and ESR2 (By similarity).
CC       {ECO:0000250}.
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DR   EMBL; AC122753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS51646.1; -.
DR   RefSeq; NP_001128239.1; NM_001134767.1.
DR   RefSeq; XP_006530318.1; XM_006530255.3.
DR   AlphaFoldDB; E9PVD1; -.
DR   SMR; E9PVD1; -.
DR   BioGRID; 229023; 1.
DR   STRING; 10090.ENSMUSP00000127483; -.
DR   iPTMnet; E9PVD1; -.
DR   PhosphoSitePlus; E9PVD1; -.
DR   MaxQB; E9PVD1; -.
DR   PaxDb; E9PVD1; -.
DR   PRIDE; E9PVD1; -.
DR   ProteomicsDB; 283733; -.
DR   Antibodypedia; 52252; 70 antibodies from 17 providers.
DR   Ensembl; ENSMUST00000094320; ENSMUSP00000091878; ENSMUSG00000061882.
DR   Ensembl; ENSMUST00000165148; ENSMUSP00000127483; ENSMUSG00000061882.
DR   GeneID; 208908; -.
DR   KEGG; mmu:208908; -.
DR   UCSC; uc012edk.1; mouse.
DR   CTD; 84660; -.
DR   MGI; MGI:2684996; Ccdc62.
DR   VEuPathDB; HostDB:ENSMUSG00000061882; -.
DR   eggNOG; ENOG502RHSF; Eukaryota.
DR   GeneTree; ENSGT00400000022269; -.
DR   HOGENOM; CLU_025504_0_0_1; -.
DR   InParanoid; E9PVD1; -.
DR   OMA; PGHMSDA; -.
DR   OrthoDB; 397822at2759; -.
DR   PhylomeDB; E9PVD1; -.
DR   TreeFam; TF329149; -.
DR   BioGRID-ORCS; 208908; 4 hits in 72 CRISPR screens.
DR   PRO; PR:E9PVD1; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; E9PVD1; protein.
DR   Bgee; ENSMUSG00000061882; Expressed in spermatid and 110 other tissues.
DR   Genevisible; E9PVD1; MM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR   GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:MGI.
DR   GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR   GO; GO:0071392; P:cellular response to estradiol stimulus; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Nucleus; Reference proteome; Repeat.
FT   CHAIN           1..701
FT                   /note="Coiled-coil domain-containing protein 62"
FT                   /id="PRO_0000415823"
FT   REGION          624..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          61..197
FT                   /evidence="ECO:0000255"
FT   COILED          241..342
FT                   /evidence="ECO:0000255"
FT   MOTIF           654..658
FT                   /note="LXXLL motif 1"
FT   MOTIF           670..674
FT                   /note="LXXLL motif 2"
FT   COMPBIAS        624..651
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   701 AA;  79317 MW;  57B3D241A8965D35 CRC64;
     MRSSEGAPSW AVALPPPLRP CAYGVSEVTR CWHQLSLGAG ESSMNPSATL YRRQNIGSEV
     ETSTIEKQRK ELQLLIGELK DRDKELNDMV AVHQRQLLSW EEDRQKVLTL EERCSKLEGE
     LHKRTDIIKS LMKKVKTLES NQAECQTALQ KTQQQLQEMA QKATHSTLLS EDLEARNENL
     SSTLVDLSAQ VGQLQAREQA LTTMIKLKDK DIIEAVNHIS DCSGKFKLLE HALRDAKMAE
     TCVVREKQDY KQKLKALRIE VNKLKEDLNE KTTENNEQRE EIIRLKQEKS CLHDELIFTV
     EREKRKDELL DIAKSKQDRT NSELQNLRQI YVKQQSDLQF LNFNIESSQE LIQIHGLKME
     EPKALECSKD MCLSDLDNNY PKIDIKRERN QKSLVKDQTF EVMLAQHNGS DKSSCDACRE
     KKLQVNTALG EKSVIALSSL FTKDLLDKQK SWSLGGKIQT EPENKVTLCK VHAKSPKCDG
     VGLPTEEKQL SETSVSLSDE KQWHDINVYL GLSSCSKQPD RLDGDGHDRT GTSEVSCCTP
     NVVCIGDNDL SESKCCHPSN IIIEAPGHMT DTEWMNIFKP SRAQRIVRHK TMCTCSRSVS
     AMKYNSSASE LIGMQPSQCV GSLKSAEREE ESAALPDRRT SANEKDDFSP TSKLQRLLAE
     SRQMVTDLEL STLLPISCEN LNRSKLEVSE EPDEKTTLVS H