CC85B_MOUSE
ID CC85B_MOUSE Reviewed; 202 AA.
AC Q6PDY0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Coiled-coil domain-containing protein 85B;
DE AltName: Full=Hepatitis delta antigen-interacting protein A homolog;
DE Short=Delta-interacting protein A homolog;
GN Name=Ccdc85b; Synonyms=Dipa;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION, INTERACTION WITH CEBPB AND CEBPD, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=15644333; DOI=10.1074/jbc.m411741200;
RA Bezy O., Elabd C., Cochet O., Petersen R.K., Kristiansen K., Dani C.,
RA Ailhaud G., Amri E.-Z.;
RT "Delta-interacting protein A, a new inhibitory partner of CCAAT/enhancer-
RT binding protein beta, implicated in adipocyte differentiation.";
RL J. Biol. Chem. 280:11432-11438(2005).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22666460; DOI=10.1371/journal.pone.0038130;
RA Liu X.F., Bera T.K., Kahue C., Escobar T., Fei Z., Raciti G.A., Pastan I.;
RT "ANKRD26 and its interacting partners TRIO, GPS2, HMMR and DIPA regulate
RT adipogenesis in 3T3-L1 cells.";
RL PLoS ONE 7:E38130-E38130(2012).
RN [4]
RP INTERACTION WITH EURL.
RX PubMed=27404227; DOI=10.1038/srep29514;
RA Li S.S., Qu Z., Haas M., Ngo L., Heo Y.J., Kang H.J., Britto J.M.,
RA Cullen H.D., Vanyai H.K., Tan S.S., Chan-Ling T., Gunnersen J.M.,
RA Heng J.I.;
RT "The HSA21 gene EURL/C21ORF91 controls neurogenesis within the cerebral
RT cortex and is implicated in the pathogenesis of Down Syndrome.";
RL Sci. Rep. 6:29514-29514(2016).
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. May function in adipocyte differentiation, negatively
CC regulating mitotic clonal expansion (PubMed:15644333, PubMed:22666460).
CC Plays a role in cell-cell adhesion and epithelium development through
CC its interaction with proteins of the beta-catenin family (By
CC similarity). {ECO:0000250|UniProtKB:A2CEM9,
CC ECO:0000269|PubMed:15644333, ECO:0000269|PubMed:22666460}.
CC -!- SUBUNIT: Interacts with CEBPB (PubMed:15644333). May interact with
CC CEBPD (Probable). Interacts with EURL (PubMed:27404227). Interacts with
CC MCRS1 (By similarity). Interacts with TCF7L2; competes with CTNNB1 (By
CC similarity). Interacts with ANKRD26 (By similarity). Interacts with the
CC beta-catenin family proteins ARVCF, CTNND1, CTNND2 AND PKP4 (By
CC similarity). {ECO:0000250|UniProtKB:Q15834,
CC ECO:0000269|PubMed:15644333, ECO:0000269|PubMed:27404227,
CC ECO:0000305|PubMed:15644333}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15644333,
CC ECO:0000269|PubMed:22666460}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q15834}. Cell
CC junction, adherens junction {ECO:0000250|UniProtKB:Q15834}.
CC -!- TISSUE SPECIFICITY: Expressed in white and brown adipose tissue.
CC {ECO:0000269|PubMed:15644333}.
CC -!- SIMILARITY: Belongs to the CCDC85 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; BC058411; AAH58411.1; -; mRNA.
DR CCDS; CCDS50357.1; -.
DR RefSeq; NP_941018.1; NM_198616.4.
DR AlphaFoldDB; Q6PDY0; -.
DR SMR; Q6PDY0; -.
DR STRING; 10090.ENSMUSP00000137537; -.
DR PhosphoSitePlus; Q6PDY0; -.
DR MaxQB; Q6PDY0; -.
DR PaxDb; Q6PDY0; -.
DR PRIDE; Q6PDY0; -.
DR ProteomicsDB; 281248; -.
DR Antibodypedia; 55944; 56 antibodies from 21 providers.
DR Ensembl; ENSMUST00000179549; ENSMUSP00000137537; ENSMUSG00000095098.
DR GeneID; 240514; -.
DR KEGG; mmu:240514; -.
DR UCSC; uc012bgx.2; mouse.
DR CTD; 11007; -.
DR MGI; MGI:2147607; Ccdc85b.
DR VEuPathDB; HostDB:ENSMUSG00000095098; -.
DR eggNOG; KOG3819; Eukaryota.
DR GeneTree; ENSGT00940000162317; -.
DR HOGENOM; CLU_117450_0_0_1; -.
DR InParanoid; Q6PDY0; -.
DR OMA; IQGVNRQ; -.
DR OrthoDB; 1393196at2759; -.
DR PhylomeDB; Q6PDY0; -.
DR TreeFam; TF320243; -.
DR BioGRID-ORCS; 240514; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Ccdc85b; mouse.
DR PRO; PR:Q6PDY0; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q6PDY0; protein.
DR Bgee; ENSMUSG00000095098; Expressed in ventral horn of spinal cord and 206 other tissues.
DR ExpressionAtlas; Q6PDY0; baseline and differential.
DR Genevisible; Q6PDY0; MM.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070097; F:delta-catenin binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR InterPro; IPR019359; CCDC85.
DR PANTHER; PTHR13546; PTHR13546; 1.
DR Pfam; PF10226; CCDC85; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell junction; Coiled coil; Cytoplasm; Cytoskeleton;
KW Differentiation; Growth regulation; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..202
FT /note="Coiled-coil domain-containing protein 85B"
FT /id="PRO_0000079909"
FT REGION 152..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 44..82
FT /evidence="ECO:0000255"
FT COILED 118..141
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q15834"
SQ SEQUENCE 202 AA; 22133 MW; DD49A77706FDE2C9 CRC64;
MEAEAGGLEE LTDEEMAALG KEELVRRLRR EEAARLAALV QRGRLMQEVN RQLQGHLGEI
RELKQLNRRL QAENRELRDL CCFLDSERQR GRRAARQWQL FGTQASRAVR EDLGGCWQKL
AELEGRQEEL LRENLALKEL CLALGEEWGP RGGPGGAVGS GAGPTPELAL PPCGPRDLGD
GSSSTGSVGS PDQLPLACSP DD
