CC85B_DANRE
ID CC85B_DANRE Reviewed; 200 AA.
AC A2CEM9;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Coiled-coil domain-containing protein 85B;
GN Name=ccdc85b;
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 GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25009281; DOI=10.1091/mbc.e13-08-0492;
RA Markham N.O., Doll C.A., Dohn M.R., Miller R.K., Yu H., Coffey R.J.,
RA McCrea P.D., Gamse J.T., Reynolds A.B.;
RT "DIPA-family coiled-coils bind conserved isoform-specific head domain of
RT p120-catenin family: potential roles in hydrocephalus and heterotopia.";
RL Mol. Biol. Cell 25:2592-2603(2014).
CC -!- FUNCTION: Functions as a transcriptional repressor. May inhibit the
CC activity of CTNNB1 in a TP53-dependent manner and thus regulate cell
CC growth (By similarity). May function in adipocyte differentiation,
CC negatively regulating mitotic clonal expansion (By similarity). Plays a
CC role in cell-cell adhesion and epithelium development through its
CC interaction with proteins of the beta-catenin family (Probable).
CC {ECO:0000250|UniProtKB:Q15834, ECO:0000250|UniProtKB:Q6PDY0,
CC ECO:0000305|PubMed:25009281}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15834}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q15834}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q15834}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein results in
CC neural tube closure defects and a disorganization of the
CC neuroepithelium (PubMed:25009281). This developmental phenotype is
CC associated with an alteration of cell-cell junctions (PubMed:25009281).
CC {ECO:0000269|PubMed:25009281}.
CC -!- SIMILARITY: Belongs to the CCDC85 family. {ECO:0000305}.
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DR EMBL; CR626869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001159626.1; NM_001166154.1.
DR AlphaFoldDB; A2CEM9; -.
DR SMR; A2CEM9; -.
DR STRING; 7955.ENSDARP00000118959; -.
DR PaxDb; A2CEM9; -.
DR Ensembl; ENSDART00000087884; ENSDARP00000082317; ENSDARG00000061543.
DR GeneID; 564324; -.
DR KEGG; dre:564324; -.
DR CTD; 11007; -.
DR ZFIN; ZDB-GENE-060130-56; ccdc85b.
DR eggNOG; KOG3819; Eukaryota.
DR GeneTree; ENSGT00940000162317; -.
DR HOGENOM; CLU_117450_0_0_1; -.
DR InParanoid; A2CEM9; -.
DR OMA; IQGVNRQ; -.
DR OrthoDB; 1393196at2759; -.
DR PhylomeDB; A2CEM9; -.
DR TreeFam; TF320243; -.
DR PRO; PR:A2CEM9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 14.
DR Bgee; ENSDARG00000061543; Expressed in brain and 29 other tissues.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0001843; P:neural tube closure; IMP:ZFIN.
DR InterPro; IPR019359; CCDC85.
DR PANTHER; PTHR13546; PTHR13546; 1.
DR Pfam; PF10226; CCDC85; 1.
PE 3: Inferred from homology;
KW Cell junction; Coiled coil; Cytoplasm; Cytoskeleton; Nucleus;
KW Reference proteome.
FT CHAIN 1..200
FT /note="Coiled-coil domain-containing protein 85B"
FT /id="PRO_0000448224"
FT REGION 178..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 57..84
FT /evidence="ECO:0000255"
SQ SEQUENCE 200 AA; 22562 MW; A1C2D03215E07ED9 CRC64;
MGSDSEILNR ELSKLSDEDL LACTKEELVN RLRKEESDKM SALIQRGRLI KEVNKQLQGH
LLEIRELKVI NQRLQEENQE LRDLCCFLDD DRLKVKKLAR EWQLFGHHAA KVMREDLGGY
LKKLADLERM QDGLVKENLD LKELCLVLEE ECVSRSDSSP GGSTDLNIPC MVARDVGDGS
SSTGSVGSPD QLHLVCSPDD