CCDC6_MOUSE
ID CCDC6_MOUSE Reviewed; 469 AA.
AC D3YZP9;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Coiled-coil domain-containing protein 6;
GN Name=Ccdc6;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233 AND SER-237, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-233; SER-237 AND
RP SER-316, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-380, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=May be a cytoskeletal protein. {ECO:0000250}.
CC -!- DOMAIN: The protein has mostly an alpha helical conformation similar to
CC myosin heavy-chain tail that might adopt a coiled-coil conformation.
CC {ECO:0000250}.
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; AC132435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466553; EDL31982.1; -; Genomic_DNA.
DR CCDS; CCDS48591.1; -.
DR RefSeq; NP_001104591.1; NM_001111121.1.
DR AlphaFoldDB; D3YZP9; -.
DR SMR; D3YZP9; -.
DR BioGRID; 218173; 10.
DR IntAct; D3YZP9; 1.
DR STRING; 10090.ENSMUSP00000123374; -.
DR iPTMnet; D3YZP9; -.
DR PhosphoSitePlus; D3YZP9; -.
DR EPD; D3YZP9; -.
DR jPOST; D3YZP9; -.
DR MaxQB; D3YZP9; -.
DR PaxDb; D3YZP9; -.
DR PeptideAtlas; D3YZP9; -.
DR PRIDE; D3YZP9; -.
DR ProteomicsDB; 265369; -.
DR Antibodypedia; 14268; 230 antibodies from 29 providers.
DR Ensembl; ENSMUST00000147545; ENSMUSP00000123374; ENSMUSG00000048701.
DR GeneID; 76551; -.
DR KEGG; mmu:76551; -.
DR UCSC; uc011xfv.1; mouse.
DR CTD; 8030; -.
DR MGI; MGI:1923801; Ccdc6.
DR VEuPathDB; HostDB:ENSMUSG00000048701; -.
DR eggNOG; KOG2129; Eukaryota.
DR GeneTree; ENSGT00390000013594; -.
DR HOGENOM; CLU_033433_2_0_1; -.
DR InParanoid; D3YZP9; -.
DR OMA; NLSAHIQ; -.
DR OrthoDB; 1142037at2759; -.
DR PhylomeDB; D3YZP9; -.
DR TreeFam; TF321211; -.
DR BioGRID-ORCS; 76551; 8 hits in 75 CRISPR screens.
DR ChiTaRS; Ccdc6; mouse.
DR PRO; PR:D3YZP9; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; D3YZP9; protein.
DR Bgee; ENSMUSG00000048701; Expressed in animal zygote and 255 other tissues.
DR ExpressionAtlas; D3YZP9; baseline and differential.
DR Genevisible; D3YZP9; MM.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR InterPro; IPR019152; DUF2046.
DR PANTHER; PTHR15276; PTHR15276; 1.
DR Pfam; PF09755; DUF2046; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosomal rearrangement; Coiled coil; Cytoplasm;
KW Cytoskeleton; Methylation; Phosphoprotein; Reference proteome; Repeat;
KW SH3-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q16204"
FT CHAIN 2..469
FT /note="Coiled-coil domain-containing protein 6"
FT /id="PRO_0000415808"
FT REPEAT 99..127
FT /note="1"
FT REPEAT 128..156
FT /note="2"
FT REPEAT 157..185
FT /note="3"
FT REPEAT 186..199
FT /note="4; approximate"
FT REPEAT 200..228
FT /note="5"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..228
FT /note="5 X 29 AA tandem repeats"
FT REGION 335..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 47..320
FT /evidence="ECO:0000255"
FT MOTIF 435..444
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 337..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..463
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q16204"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16204"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16204"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16204"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 342
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16204"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16204"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16204"
FT MOD_RES 380
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16204"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16204"
SQ SEQUENCE 469 AA; 52939 MW; 708882EB2F131354 CRC64;
MADSASESDT DAAGGGPAAM QSSCSATSGG SGGGGGGKSG GIVISPFRLE ELTNRLASLQ
QENKVLKIEL ETYKLKCKAL QEENRDLRKA SVTIQARAEQ EEEFISNTLF KKIQALQKEK
ETLAVNYEKE EEFLTNELSR KLMQLQHEKA ELEQHLEQEQ EFQVNKLMKK IKKLENDTIS
KQLTLEQLRR EKIDLENTLE QEQEALVNRL WKRMDKLEAE KRILQEKLDQ PVSAPPSPRD
ISMEIDSPEN MMRHIRFLKN EVERLKKQLR AAQLQHSEKM AQYLEEERHM REENLRLQRK
LQREMERREA LCRQLSESES SLEMDDERYF NEMSAQGLRP RTVSSPIPYT PSPSSSRPIS
PGLSYASHTV GFTPPTSLTR AGMSYYNSPG LHVQHMGASH GITRPSPRRS SSPDKFKRPT
PPPSPNTQSP VQPPPPPPPP PMQPAVPSAA PTQPAPTQPQ HPVHPSSQP