ID   CCNOA_XENLA             Reviewed;         366 AA.
AC   Q32NJ2;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Cyclin-O protein A;
GN   Name=ccno-a; Synonyms=ccno;
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 (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RX   PubMed=24747639; DOI=10.1038/ng.2961;
RA   Wallmeier J., Al-Mutairi D.A., Chen C.T., Loges N.T., Pennekamp P.,
RA   Menchen T., Ma L., Shamseldin H.E., Olbrich H., Dougherty G.W., Werner C.,
RA   Alsabah B.H., Koehler G., Jaspers M., Boon M., Griese M., Schmitt-Grohe S.,
RA   Zimmermann T., Koerner-Rettberg C., Horak E., Kintner C., Alkuraya F.S.,
RA   Omran H.;
RT   "Mutations in CCNO result in congenital mucociliary clearance disorder with
RT   reduced generation of multiple motile cilia.";
RL   Nat. Genet. 46:646-651(2014).
RN   [3]
RP   FUNCTION, AND MUTAGENESIS OF LEU-228.
RX   PubMed=26777464; DOI=10.1002/humu.22957;
RG   Israeli PCD Consortium Investigators;
RA   Amirav I., Wallmeier J., Loges N.T., Menchen T., Pennekamp P., Mussaffi H.,
RA   Abitbul R., Avital A., Bentur L., Dougherty G.W., Nael E., Lavie M.,
RA   Olbrich H., Werner C., Kintner C., Omran H.;
RT   "Systematic analysis of CCNO variants in a defined population: implications
RT   for clinical phenotype and differential diagnosis.";
RL   Hum. Mutat. 37:396-405(2016).
CC   -!- FUNCTION: Specifically required for generation of multiciliated cells,
CC       possibly by promoting a cell cycle state compatible with centriole
CC       amplification and maturation. Acts downstream of mcidas to promote
CC       mother centriole amplification and maturation in preparation for apical
CC       docking. {ECO:0000269|PubMed:24747639, ECO:0000269|PubMed:26777464}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0C242}.
CC       Note=Localizes to the apical part of cytoplasm.
CC       {ECO:0000250|UniProtKB:P0C242}.
CC   -!- SIMILARITY: Belongs to the cyclin family. {ECO:0000305}.
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DR   EMBL; BC108598; AAI08599.1; -; mRNA.
DR   RefSeq; NP_001089879.1; NM_001096410.1.
DR   AlphaFoldDB; Q32NJ2; -.
DR   SMR; Q32NJ2; -.
DR   DNASU; 734946; -.
DR   GeneID; 734946; -.
DR   KEGG; xla:734946; -.
DR   CTD; 734946; -.
DR   Xenbase; XB-GENE-979551; ccno.L.
DR   OMA; CNLECLV; -.
DR   OrthoDB; 752095at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 734946; Expressed in egg cell and 13 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR   GO; GO:1903251; P:multi-ciliated epithelial cell differentiation; IMP:UniProtKB.
DR   CDD; cd00043; CYCLIN; 2.
DR   InterPro; IPR028864; Ccno.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10177; PTHR10177; 1.
DR   PANTHER; PTHR10177:SF401; PTHR10177:SF401; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SMART; SM01332; Cyclin_C; 1.
DR   SUPFAM; SSF47954; SSF47954; 2.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cilium biogenesis/degradation; Cyclin;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..366
FT                   /note="Cyclin-O protein A"
FT                   /id="PRO_0000430434"
FT   REGION          18..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          80..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         228
FT                   /note="L->P: Decreased formation of basal bodies in
FT                   multiciliated cells."
FT                   /evidence="ECO:0000269|PubMed:26777464"
SQ   SEQUENCE   366 AA;  40469 MW;  E1A2CF658AD7D2FB CRC64;
     MVTCSMRCTE EHLLGAPAAF SSGKRKRDSG YSPGDATPGD RGEGGPDWPS AGIKKRVKYS
     RHRKQRLELR SCDSGVADLY ETPSPSPVAP TPTNEPYDSP CTSMPDRLGL QSFSDYGHDC
     YLFNKSLEDK FLTVNCLKNQ PQIKAESRCK LISWLIPVHK HLKLGFESLC LTVNILDRFL
     ACTPVASDCF QLVGVTSLLI ACKQVESRPP RVKQLLALCC DAFSREQLCN LECIILLKLC
     FRIGAPTINF FLQHFSLLRV TSVESPDTEL IEATKSMTVA RGIAELSLAD YAFNAYSPSL
     VAACCLELAD RMLCLRNPIG VRVSGYHQSL IKECVGKIDL LVSLNQDSLH RLLPSQFSVK
     SIKADN