CC120_MOUSE
ID CC120_MOUSE Reviewed; 629 AA.
AC A2AEV7; A2AEV8;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Coiled-coil domain-containing protein 120 {ECO:0000305};
GN Name=Ccdc120 {ECO:0000312|MGI:MGI:1859619};
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 MRNA].
RC TISSUE=Testis;
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 [3]
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-357, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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-432, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
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).
RN [6]
RP FUNCTION.
RX PubMed=28422092; DOI=10.1038/ncomms15057;
RA Huang N., Xia Y., Zhang D., Wang S., Bao Y., He R., Teng J., Chen J.;
RT "Hierarchical assembly of centriole subdistal appendages via centrosome
RT binding proteins CCDC120 and CCDC68.";
RL Nat. Commun. 8:15057-15057(2017).
CC -!- FUNCTION: Centriolar protein required for centriole subdistal appendage
CC assembly and microtubule anchoring in interphase cells
CC (PubMed:28422092). Together with CCDC68, cooperate with subdistal
CC appendage components ODF2, NIN and CEP170 for hierarchical subdistal
CC appendage assembly (PubMed:28422092). Recruits NIN and CEP170 to
CC centrosomes (PubMed:28422092). Also required for neurite growth (By
CC similarity). Localizes CYTH2 to vesicles to allow its transport along
CC neurites, and subsequent ARF6 activation and neurite growth (By
CC similarity). {ECO:0000250|UniProtKB:Q96HB5,
CC ECO:0000269|PubMed:28422092}.
CC -!- SUBUNIT: Interacts with NIN and CEP170; leading to recruit them to
CC centrosomes (By similarity). Interacts with CYTH2; this interaction is
CC direct and stabilizes CCDC120, possibly by preventing ubiquitination
CC (By similarity). {ECO:0000250|UniProtKB:Q96HB5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250|UniProtKB:Q96HB5}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96HB5}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:Q96HB5}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q96HB5}. Endosome
CC {ECO:0000250|UniProtKB:Q96HB5}. Note=Localizes to the subdistal
CC appendages of mother centrioles and proximal ends of both centrioles in
CC interphase cells (By similarity). Recruited to subdistal appendages by
CC ODF2 (By similarity). In differentiating neuroblastoma cells,
CC colocalizes with CYTH2 in both neurite shaft and growth cone areas (By
CC similarity). Partially colocalizes with endosomes along neurites in
CC differentiating neuroblastoma cells (By similarity).
CC {ECO:0000250|UniProtKB:Q96HB5}.
CC -!- PTM: Ubiquitinated; interaction with CYTH2 may prevent ubiquitination.
CC {ECO:0000250|UniProtKB:Q96HB5}.
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DR EMBL; AL671995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC139064; AAI39065.1; -; mRNA.
DR CCDS; CCDS29972.1; -.
DR RefSeq; NP_997085.2; NM_207202.2.
DR AlphaFoldDB; A2AEV7; -.
DR SMR; A2AEV7; -.
DR STRING; 10090.ENSMUSP00000033490; -.
DR iPTMnet; A2AEV7; -.
DR PhosphoSitePlus; A2AEV7; -.
DR MaxQB; A2AEV7; -.
DR PaxDb; A2AEV7; -.
DR PeptideAtlas; A2AEV7; -.
DR PRIDE; A2AEV7; -.
DR ProteomicsDB; 279939; -.
DR Antibodypedia; 347; 118 antibodies from 21 providers.
DR Ensembl; ENSMUST00000033490; ENSMUSP00000033490; ENSMUSG00000031150.
DR GeneID; 54648; -.
DR KEGG; mmu:54648; -.
DR UCSC; uc009smf.1; mouse.
DR CTD; 90060; -.
DR MGI; MGI:1859619; Ccdc120.
DR VEuPathDB; HostDB:ENSMUSG00000031150; -.
DR eggNOG; KOG3529; Eukaryota.
DR GeneTree; ENSGT00940000154102; -.
DR HOGENOM; CLU_029533_0_0_1; -.
DR InParanoid; A2AEV7; -.
DR OMA; PDVQGCQ; -.
DR OrthoDB; 595503at2759; -.
DR PhylomeDB; A2AEV7; -.
DR TreeFam; TF328984; -.
DR BioGRID-ORCS; 54648; 3 hits in 76 CRISPR screens.
DR PRO; PR:A2AEV7; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; A2AEV7; protein.
DR Bgee; ENSMUSG00000031150; Expressed in lip and 152 other tissues.
DR ExpressionAtlas; A2AEV7; baseline and differential.
DR GO; GO:0120103; C:centriolar subdistal appendage; ISO:MGI.
DR GO; GO:0005814; C:centriole; ISO:MGI.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; ISO:MGI.
DR GO; GO:0008104; P:protein localization; ISO:MGI.
DR InterPro; IPR039108; CCDC120.
DR InterPro; IPR043447; CCDC120/INAVA.
DR InterPro; IPR021774; DUF3338.
DR PANTHER; PTHR16093; PTHR16093; 1.
DR PANTHER; PTHR16093:SF5; PTHR16093:SF5; 1.
DR Pfam; PF11819; CUPID; 1.
PE 1: Evidence at protein level;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Endosome; Methylation; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..629
FT /note="Coiled-coil domain-containing protein 120"
FT /id="PRO_0000442769"
FT REGION 31..70
FT /note="Involved in CYTH2-binding"
FT /evidence="ECO:0000250|UniProtKB:Q96HB5"
FT REGION 209..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 109..173
FT /evidence="ECO:0000255"
FT COMPBIAS 275..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..419
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HB5"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 432
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 629 AA; 67407 MW; 277CF22B3D090564 CRC64;
MEVKGQLISS PTFTAPAALF GEAAPLVKSD RLRGLLDRQR ALQEALSVKL QELRKVCLQE
AELTGQLPPE CPLEPGERPQ LVRRRPPAAR AYPPPHPNPA HHSLCPAEEL ALEALEREVS
VQQQIAAAAR RLALAPDLNG EQRRRRRQVQ VDALRRLHEL EEQLRDFRAR LGLPVLQPLP
LSAGALVNAQ GVCLGTRLAQ LSQEDVVLHS ESSSLSESGA SHDNEEPHSC FPLTERPSPP
KAWDQFRAVS GGSPERRAPW KPPPSDIYGD LKSRRNSVAS PTSPTRSLPR SASSFEGRSV
PATPVLTRGS GPRLCKPEGL HSRQWSGSQD SQMGFPRPDP ASDRASLFAA RTRRSNSSEA
LLVDRAAAGG AGSPPAPLAP PAAGPPVCKS SEVLYERPQP VPSFSSRTTG PPDPPRAARP
SSAAPASRGA PRLPTVCGDF LLDYPLDRGL PRGSGGAGWG ELLPAPEVPG PLSRRDGLLA
MLPGPPPIYA ADGSSPLLRS KDPNTRAIRS KPSGLPPEAV EGLEVHPNPL LWMPPPTRIP
PAGERGGHKN LALEGLRDWY IRNSGLAVGP QRRPMLPHVG PTHTPFLHAR CYEVGQSLYG
PPSQAPLPHS RSFTAPPVSG RYGGAFTDG
