CC85C_MOUSE
ID CC85C_MOUSE Reviewed; 420 AA.
AC E9Q6B2;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Coiled-coil domain-containing protein 85C;
GN Name=Ccdc85c;
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).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22056358; DOI=10.1016/j.ajpath.2011.09.014;
RA Mori N., Kuwamura M., Tanaka N., Hirano R., Nabe M., Ibuki M., Yamate J.;
RT "Ccdc85c encoding a protein at apical junctions of radial glia is disrupted
RT in hemorrhagic hydrocephalus (hhy) mice.";
RL Am. J. Pathol. 180:314-327(2012).
CC -!- FUNCTION: May play a role in cell-cell adhesion and epithelium
CC development through its interaction with proteins of the beta-catenin
CC family (By similarity). May play an important role in cortical
CC development, especially in the maintenance of radial glia
CC (PubMed:22056358). {ECO:0000250|UniProtKB:A6NKD9,
CC ECO:0000269|PubMed:22056358}.
CC -!- SUBUNIT: May interact with ARVCF, CTNND1, CTNND2 and PKP4.
CC {ECO:0000250|UniProtKB:A6NKD9}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000269|PubMed:22056358}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:A6NKD9}. Note=Localizes to the apical junction
CC of radial glia in the wall of lateral ventricles of the developing
CC brain. Colocalizes with TJP1 on the meshwork-like structure of adherens
CC junctions on the lateral ventricles wall.
CC {ECO:0000269|PubMed:22056358}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed on the surface of the
CC lateral ventricular walls of the developing cerebral cortex.
CC {ECO:0000269|PubMed:22056358}.
CC -!- DISRUPTION PHENOTYPE: Disrupted in the hemorrhagic hydrocephalus (hhy)
CC mutant. The mutant animals shown sucortical heterotopia and non-
CC obstructive hydrocephalus with frequent brain hemorrhage.
CC {ECO:0000269|PubMed:22056358}.
CC -!- SIMILARITY: Belongs to the CCDC85 family. {ECO:0000305}.
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DR EMBL; AC122407; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC152059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49166.1; -.
DR RefSeq; NP_001153382.1; NM_001159910.1.
DR AlphaFoldDB; E9Q6B2; -.
DR SMR; E9Q6B2; -.
DR BioGRID; 579958; 2.
DR IntAct; E9Q6B2; 1.
DR STRING; 10090.ENSMUSP00000125757; -.
DR iPTMnet; E9Q6B2; -.
DR PhosphoSitePlus; E9Q6B2; -.
DR EPD; E9Q6B2; -.
DR MaxQB; E9Q6B2; -.
DR PaxDb; E9Q6B2; -.
DR PeptideAtlas; E9Q6B2; -.
DR PRIDE; E9Q6B2; -.
DR ProteomicsDB; 281492; -.
DR Antibodypedia; 54727; 80 antibodies from 15 providers.
DR Ensembl; ENSMUST00000222310; ENSMUSP00000152421; ENSMUSG00000084883.
DR GeneID; 668158; -.
DR KEGG; mmu:668158; -.
DR UCSC; uc011yrs.1; mouse.
DR CTD; 317762; -.
DR MGI; MGI:3644008; Ccdc85c.
DR VEuPathDB; HostDB:ENSMUSG00000084883; -.
DR eggNOG; KOG3819; Eukaryota.
DR GeneTree; ENSGT00940000159071; -.
DR HOGENOM; CLU_028762_0_0_1; -.
DR InParanoid; E9Q6B2; -.
DR OMA; NGLACPA; -.
DR PhylomeDB; E9Q6B2; -.
DR TreeFam; TF320243; -.
DR BioGRID-ORCS; 668158; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Ccdc85c; mouse.
DR PRO; PR:E9Q6B2; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; E9Q6B2; protein.
DR Bgee; ENSMUSG00000084883; Expressed in retinal neural layer and 93 other tissues.
DR ExpressionAtlas; E9Q6B2; baseline and differential.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0043296; C:apical junction complex; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0021987; P:cerebral cortex development; IMP: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; Developmental protein;
KW Phosphoprotein; Reference proteome; Tight junction.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:A6NKD9"
FT CHAIN 2..420
FT /note="Coiled-coil domain-containing protein 85C"
FT /id="PRO_0000415925"
FT REGION 165..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 26..92
FT /evidence="ECO:0000255"
FT COILED 122..165
FT /evidence="ECO:0000255"
FT COMPBIAS 177..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:A6NKD9"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6NKD9"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6NKD9"
SQ SEQUENCE 420 AA; 45334 MW; 89DB51260E57BEA1 CRC64;
MAKPPAVAAA AAAAASEELS QVPDEELLRW SKEELARRLR RAEGEKVGLM LEHGGLMRDV
NRRLQQHLLE IRGLKDVNQR LQDDNQELRE LCCFLDDDRQ KGRKLAREWQ RFGRHAAGAV
WHEVARSQQK LRELEARQEA LLRENLELKE LVLLLDEERA ALAAAGGAGG GGGGAGSRSS
IDSQASLSGP LAGSAAGSGA RDVGDGSSTS SAGSGGSPDH HHHVPAALLP PGPHKVPDGK
AGATRRSLDD LSAPPHHRSI PNGLHDPSST YIRPLETKVK LLDGDKLPPQ QAGSGEFRTL
RKGFSPYHSE SQLASLPPSY QEVLQNGPAC PVPELPSPPS TVYSSAGQKP EAVVHAMKVL
EVHENLDRQL QDSCEEDLSE KEKAIVREMC NVVWRKLGDA ASTKPSIRQH LSGNQFKGPL
