CCD50_MOUSE
ID CCD50_MOUSE Reviewed; 305 AA.
AC Q810U5; A6X929; Q3TRW1; Q8BP82; Q9CZT1; Q9D436;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Coiled-coil domain-containing protein 50;
DE AltName: Full=Protein Ymer;
GN Name=Ccdc50;
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 [MRNA] (ISOFORM 1).
RC STRAIN=CD-1; TISSUE=Liver;
RX PubMed=14527723; DOI=10.1016/s0378-1119(03)00710-8;
RA Vazza G., Picelli S., Bozzato A., Mostacciuolo M.L.;
RT "Identification and characterization of C3orf6, a new conserved human gene
RT mapping to chromosome 3q28.";
RL Gene 314:113-120(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17503326; DOI=10.1086/518311;
RA Modamio-Hoeybjoer S., Mencia A., Goodyear R., del Castillo I.,
RA Richardson G., Moreno F., Moreno-Pelayo M.A.;
RT "A mutation in CCDC50, a gene encoding an effector of epidermal growth
RT factor-mediated cell signaling, causes progressive hearing loss.";
RL Am. J. Hum. Genet. 80:1076-1089(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, 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 [6]
RP INTERACTION WITH RNF126.
RX PubMed=23418353; DOI=10.1242/jcs.116129;
RA Smith C.J., Berry D.M., McGlade C.J.;
RT "The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of
RT the epidermal growth factor receptor.";
RL J. Cell Sci. 126:1366-1380(2013).
CC -!- FUNCTION: Involved in EGFR signaling. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RNF126. {ECO:0000269|PubMed:23418353}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17503326}.
CC Note=Associated with microtubules of the cytoskeleton and mitotic
CC apparatus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q810U5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q810U5-2; Sequence=VSP_014986;
CC Name=3;
CC IsoId=Q810U5-3; Sequence=VSP_014987;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17503326}.
CC -!- DEVELOPMENTAL STAGE: At 14.5 dpc, strong punctate expression in the
CC otic mesenchyme. Detected in the cells lining the lumen of the
CC primitive cochlear duct and in the nerve fibers of the spiral ganglion,
CC as well as in the nerve fibers invading the cochlear epithelium. At
CC 17.5 dpc, detected only in the mesenchyme around the cochlear duct. 2
CC days after birth (P2), the mesenchymal expression becomes weaker,
CC except in the region of the spiral limbus, while expression is observed
CC for the first time in the apical region of the developing pillar cells
CC (PCs). Also observed in the cytoplasm of outer hair cells, in their
CC innervating nerve fibers and in the marginal cells of stria vascularis.
CC At P9 and P12, detected in the stria vascularis and strongly through
CC the entire length of the inner and outer PCs. At these stages, in
CC tissues of mesenchymal origin, restricted to the spiral limbus and the
CC spiral ligament. At P14 and P16, strong expression is maintained in the
CC PCs and in the marginal cells of the stria vascularis, weak expression
CC in the spiral limbus and ligament. Also detected in Deiter's cells. At
CC P19 and P22, intense expression in the PCs and stria vascularis, as
CC well as in the cell bodies and processes of Deiter's cells. Weak
CC expression in the spiral limbus and ligament. At P31, when the inner
CC ear is functionally mature, expressed only in the PCs and stria
CC vascularis. At P69, strong expression in the PCs and less intense in
CC stria vascularis. In the vestibular maculae and the cristae ampullaris,
CC expression similar to that observed in the cochlea: strong signal in
CC the mesenchyme at the initial embryonic stages that progressively
CC becomes weaker and is less prominent in the adult (P33). At 17.5 dpc
CC and P2, observed in nerve fibers innervating the sensory epithelia.
CC Expression in the vestibular epithelium starts at 17.5 dpc and is
CC readily detected at P2. Later expression increases and persists in
CC adult stages in which it is restricted to the apical cytoplasm of the
CC epithelial cells (at protein level). {ECO:0000269|PubMed:17503326}.
CC -!- PTM: Phosphorylated on tyrosine residues. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB28089.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ534985; CAD59434.1; -; mRNA.
DR EMBL; AK012190; BAB28089.1; ALT_FRAME; mRNA.
DR EMBL; AK016827; BAB30453.1; -; mRNA.
DR EMBL; AK077557; BAC36861.1; -; mRNA.
DR EMBL; AK151672; BAE30598.1; -; mRNA.
DR EMBL; AK162434; BAE36915.1; -; mRNA.
DR EMBL; CT010568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS37305.1; -. [Q810U5-1]
DR CCDS; CCDS37306.1; -. [Q810U5-2]
DR RefSeq; NP_001020786.1; NM_001025615.3. [Q810U5-2]
DR RefSeq; NP_001276365.1; NM_001289436.1.
DR RefSeq; NP_080478.2; NM_026202.4. [Q810U5-1]
DR AlphaFoldDB; Q810U5; -.
DR BioGRID; 212232; 5.
DR STRING; 10090.ENSMUSP00000097604; -.
DR iPTMnet; Q810U5; -.
DR PhosphoSitePlus; Q810U5; -.
DR EPD; Q810U5; -.
DR MaxQB; Q810U5; -.
DR PaxDb; Q810U5; -.
DR PRIDE; Q810U5; -.
DR ProteomicsDB; 281308; -. [Q810U5-1]
DR ProteomicsDB; 281309; -. [Q810U5-2]
DR ProteomicsDB; 281310; -. [Q810U5-3]
DR Antibodypedia; 722; 237 antibodies from 30 providers.
DR DNASU; 67501; -.
DR Ensembl; ENSMUST00000039443; ENSMUSP00000038509; ENSMUSG00000038127. [Q810U5-3]
DR Ensembl; ENSMUST00000096127; ENSMUSP00000093841; ENSMUSG00000038127. [Q810U5-2]
DR Ensembl; ENSMUST00000100026; ENSMUSP00000097604; ENSMUSG00000038127. [Q810U5-1]
DR GeneID; 67501; -.
DR KEGG; mmu:67501; -.
DR UCSC; uc007yvn.3; mouse. [Q810U5-1]
DR CTD; 152137; -.
DR MGI; MGI:1914751; Ccdc50.
DR VEuPathDB; HostDB:ENSMUSG00000038127; -.
DR eggNOG; ENOG502S0GI; Eukaryota.
DR GeneTree; ENSGT00390000011058; -.
DR HOGENOM; CLU_032371_0_0_1; -.
DR InParanoid; Q810U5; -.
DR OrthoDB; 1110962at2759; -.
DR PhylomeDB; Q810U5; -.
DR TreeFam; TF325391; -.
DR BioGRID-ORCS; 67501; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Ccdc50; mouse.
DR PRO; PR:Q810U5; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q810U5; protein.
DR Bgee; ENSMUSG00000038127; Expressed in embryonic post-anal tail and 250 other tissues.
DR ExpressionAtlas; Q810U5; baseline and differential.
DR Genevisible; Q810U5; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
DR InterPro; IPR039303; CCDC50.
DR InterPro; IPR029311; CCDC50_N.
DR PANTHER; PTHR22115; PTHR22115; 2.
DR Pfam; PF15295; CCDC50_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8IVM0"
FT CHAIN 2..305
FT /note="Coiled-coil domain-containing protein 50"
FT /id="PRO_0000066308"
FT REGION 122..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 86..130
FT /evidence="ECO:0000255"
FT COMPBIAS 218..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVM0"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVM0"
FT VAR_SEQ 189..203
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014986"
FT VAR_SEQ 265..305
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014987"
FT CONFLICT 75
FT /note="K -> N (in Ref. 2; BAC36861)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="P -> Q (in Ref. 2; BAC36861)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="I -> N (in Ref. 2; BAC36861)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="G -> C (in Ref. 2; BAB30453)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 305 AA; 35321 MW; A49B28050941D82F CRC64;
MADVSVDQSK LPGVKEVCRD FAVLEDHTLA HSLQEQEIEH HLASNIQRNR LVQHDLQVAK
QLQEEDLKAQ AQLQKRYKAL EQHDCEIAQE IQEKLTIEAE RRRIQEKKDE DIARLLQEKE
LQEEKRRKKH TPEFSGGSVF GDNYYHEDGG MKPRGIKEAV STPARASHRD QEWYDAEIAR
KLQEEELLAT HVDMRAAQVA QDEEIARLLM AEEKKAYKKA KEREKSSLDK RKHDPECKLK
AKSAHSKSKE GDEAHRSKID RPSRPPPPTM MGLEDTDPTH FTNQHSTTWH LPKSESSQKG
FHNKQ
