CCD13_MOUSE
ID CCD13_MOUSE Reviewed; 709 AA.
AC D3YV10;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Coiled-coil domain-containing protein 13 {ECO:0000305};
GN Name=Ccdc13 {ECO:0000312|MGI:MGI:1920144};
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-469 AND SER-532, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Required for primary cilia formation and promotes the
CC localization of the ciliopathy protein BBS4 to both centriolar
CC satellites and cilia. {ECO:0000250|UniProtKB:Q8IYE1}.
CC -!- SUBUNIT: Interacts with PCM1, CEP290 and PCNT.
CC {ECO:0000250|UniProtKB:Q8IYE1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriolar satellite
CC {ECO:0000250|UniProtKB:Q8IYE1}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q8IYE1}.
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DR EMBL; AC165080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS57717.1; -.
DR RefSeq; NP_082660.1; NM_028384.1.
DR RefSeq; XP_006511967.1; XM_006511904.2.
DR RefSeq; XP_011241227.1; XM_011242925.1.
DR AlphaFoldDB; D3YV10; -.
DR SMR; D3YV10; -.
DR IntAct; D3YV10; 1.
DR STRING; 10090.ENSMUSP00000114787; -.
DR iPTMnet; D3YV10; -.
DR PhosphoSitePlus; D3YV10; -.
DR MaxQB; D3YV10; -.
DR PaxDb; D3YV10; -.
DR PeptideAtlas; D3YV10; -.
DR PRIDE; D3YV10; -.
DR ProteomicsDB; 265589; -.
DR Ensembl; ENSMUST00000135986; ENSMUSP00000114787; ENSMUSG00000079235.
DR GeneID; 100502861; -.
DR KEGG; mmu:100502861; -.
DR UCSC; uc012hct.1; mouse.
DR CTD; 152206; -.
DR MGI; MGI:1920144; Ccdc13.
DR VEuPathDB; HostDB:ENSMUSG00000079235; -.
DR eggNOG; ENOG502QSV1; Eukaryota.
DR GeneTree; ENSGT00390000000596; -.
DR HOGENOM; CLU_026686_0_0_1; -.
DR InParanoid; D3YV10; -.
DR OMA; NINTMND; -.
DR OrthoDB; 1533296at2759; -.
DR PhylomeDB; D3YV10; -.
DR TreeFam; TF328506; -.
DR BioGRID-ORCS; 100502861; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Ccdc13; mouse.
DR PRO; PR:D3YV10; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; D3YV10; protein.
DR Bgee; ENSMUSG00000079235; Expressed in spermatid and 75 other tissues.
DR ExpressionAtlas; D3YV10; baseline and differential.
DR Genevisible; D3YV10; MM.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISO:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; ISO:MGI.
DR InterPro; IPR038929; CCDC13.
DR PANTHER; PTHR31935; PTHR31935; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium biogenesis/degradation; Coiled coil; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..709
FT /note="Coiled-coil domain-containing protein 13"
FT /id="PRO_0000431958"
FT REGION 281..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 70..97
FT /evidence="ECO:0000255"
FT COILED 139..178
FT /evidence="ECO:0000255"
FT COILED 206..288
FT /evidence="ECO:0000255"
FT COILED 323..457
FT /evidence="ECO:0000255"
FT COILED 539..604
FT /evidence="ECO:0000255"
FT COMPBIAS 286..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 709 AA; 79750 MW; D6286CA89E824418 CRC64;
MAADESSADT LRLQFKAMQE LQHRRLQKQM EKKREKELSC QSKADNQEGF MVIPDGLSLL
DTEEQNLKNI FEKRVLEDEI QHLRSELRET VDENGRLYKL LKERDFEIKH LKKKIEEDRF
AFTGASGMAG DLVATKIVEL SKKNRGLMAE SESAKVRIKQ LTNRIQELEH QLQMASAKPP
SKGATDAGAK PLKTQTGDRA LLETPEVKAL QDRLAATNLK MSDLRNQIQS AKQELRVAQK
VLANEVGEDV NIQQLLASPG TWRGRAQQIL VLQSRVRDLE KQLGQRQNKP AGSSSSEVPL
SSDSRKMTAQ EKNLLRIRSL ERDKQESWEK LASERDTLQT ELEELRKKFE GMRSRNKVLS
SEVKTLRSQM TTLVEKGRHD DELIDALMDQ LKQLQDILSS LSVQEESRRT SQQHLDQKVN
SEAQRSSSLV AQLRAMVADR EAKVRQLELE IGQLSVQYLH GKGGGEGASP ADARFPEDQT
PITNSPASAG DHVGRLGSSR SVTSLGHTLV ESALTRPSLP SPHGTSPRFS DSPEQKGWQA
QAAEMKALWQ AAEVERDRLN EFVTVLQKRV EESSSKLLEA ERRLQEERQR AVLLEQHLEK
MRLEPSRASV SQKTKNKPGP PAANTKPNSA GSAKKDSSST QLCDMPMESQ IQELNARLAI
QMEENGILRD ALGSALRGKE EDFRMYHQTL GQVKGVFLQA LRQQKANKQ
