CCD78_XENLA
ID CCD78_XENLA Reviewed; 559 AA.
AC Q66KE8;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Coiled-coil domain-containing protein 78;
DE AltName: Full=xCCDC78;
GN Name=ccdc78;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=24075808; DOI=10.1016/j.devcel.2013.08.021;
RA Klos Dehring D.A., Vladar E.K., Werner M.E., Mitchell J.W., Hwang P.,
RA Mitchell B.J.;
RT "Deuterosome-mediated centriole biogenesis.";
RL Dev. Cell 27:103-112(2013).
CC -!- FUNCTION: Component of the deuterosome, a structure that promotes de
CC novo centriole amplification in multiciliated cells that can generate
CC more than 100 centrioles. Deuterosome-mediated centriole amplification
CC occurs in terminally differentiated multiciliated cells (G1/0) and not
CC in S phase. Essential for centriole amplification and is required for
CC cep152 localization to the deuterosome. {ECO:0000269|PubMed:24075808}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:24075808}.
CC Note=Localizes to centrioles and deuterosome.
CC -!- TISSUE SPECIFICITY: Restricted to multiciliated cells.
CC {ECO:0000269|PubMed:24075808}.
CC -!- INDUCTION: Highly up-regulated in the ciliated epithelia of embryonic
CC skin during the developmental window of centriole biogenesis.
CC Expression is probably activated by mcidas/mcin.
CC {ECO:0000269|PubMed:24075808}.
CC -!- SIMILARITY: Belongs to the CCDC78 family. {ECO:0000305}.
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DR EMBL; BC080433; AAH80433.1; -; mRNA.
DR RefSeq; NP_001087605.1; NM_001094136.1.
DR AlphaFoldDB; Q66KE8; -.
DR SMR; Q66KE8; -.
DR DNASU; 447429; -.
DR GeneID; 447429; -.
DR KEGG; xla:447429; -.
DR CTD; 447429; -.
DR Xenbase; XB-GENE-5895378; ccdc78.S.
DR OrthoDB; 773737at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 447429; Expressed in brain and 9 other tissues.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0098536; C:deuterosome; IDA:UniProtKB.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0098535; P:de novo centriole assembly involved in multi-ciliated epithelial cell differentiation; IDA:UniProtKB.
DR InterPro; IPR039873; CCDC78.
DR InterPro; IPR029329; DUF4472.
DR PANTHER; PTHR22106; PTHR22106; 1.
DR Pfam; PF14739; DUF4472; 1.
PE 2: Evidence at transcript level;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT CHAIN 1..559
FT /note="Coiled-coil domain-containing protein 78"
FT /id="PRO_0000424819"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 9..327
FT /evidence="ECO:0000255"
FT COILED 419..541
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 559 AA; 65184 MW; 6E2662AF000A086D CRC64;
MDSTEDRETP LKDQIRRLTN ENVQLQDRNE RLYAKLGELQ DKMGKLAGSK TDLSSKLVLS
EEEKLKISKE LIELQIETNK IREHYEAETF ELKNTILTLE NRLMSLELQK EKLAGEHESV
KERLQAVDAN RKELADEYIV LKSNYLALSK EHEKEVAKND ELSMELLNLA SRRGQDETYS
QSRALVNEAT AELDRVKAMV NRLSARNIKP EDLVATEYER QKLERNLLGN QDHIREEIEN
MKKIHETQQQ RLEERIIAMG KELQEAKRAI RNTQHKMAEQ SAVLLTSQSQ LQETEAQNSH
LQLQLKELNE EYRSRLNRYI QDLADYVDGT ARSKGDGTRM KHFVDNMLSD IKASHRSREE
QLAGAARQYK KRMQNLIKKH QSLLIAYRMQ REQLLASGNQ DVEPGPPEHH FTITDPELQS
QVGLELNRLR EDKARLETQI HDLKEKKRLS DAGTSNQHVE HGGKLQEESW AEIRKQLREF
THNTQEELER ERSQLLSRAL VAEEQVAELQ DYVDKHLARY KQEILRLRKL LGNEEQRAVS
ADAPQSLLIR ALRRNSHEM