CCNOB_XENLA
ID CCNOB_XENLA Reviewed; 365 AA.
AC Q32NM1;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Cyclin-O protein B;
GN Name=ccno-b;
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).
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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localizes to the
CC apical part of cytoplasm. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclin family. {ECO:0000305}.
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DR EMBL; BC108565; AAI08566.1; -; mRNA.
DR RefSeq; NP_001089865.1; NM_001096396.1.
DR AlphaFoldDB; Q32NM1; -.
DR SMR; Q32NM1; -.
DR DNASU; 734931; -.
DR GeneID; 734931; -.
DR KEGG; xla:734931; -.
DR CTD; 734931; -.
DR Xenbase; XB-GENE-17332754; ccno.S.
DR OMA; EHFTHAR; -.
DR OrthoDB; 752095at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 734931; Expressed in egg cell and 16 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 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cilium biogenesis/degradation; Cyclin;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..365
FT /note="Cyclin-O protein B"
FT /id="PRO_0000430435"
FT REGION 22..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 365 AA; 40662 MW; E491E3C8C7177718 CRC64;
MVTCSMRCTE EGLLGATLAF SSGKRKRDSV YSPGDATPGD RGEGEPKCPS VGTKKRAKYS
RHRKQSLELR SCDSGVADLY ETPSPSPVAP SPTHEPWDTC TPMYDGLGLQ NFRDYGQDCY
TFNKSLEDKF LAVNCLKNQP QIQAESRCKL ISWLIPVHRH LNLGFESLCL TVNILDRFLA
CTPVASDCFQ LVGVTSLLIA SKQVETRPPR VKQLLALCCD AFSREQLCNL ECIILLKLHF
RLGAPTINFF LQHFSLLRVT NEESSDTELS ETTKSVTVAR GIAELSLADY AFNSYSPSLM
AVCCLEIADR MLCHRNPIRA RVSDYHESLI QECVGKIDLL VSLNQDSLHR LLPSQFAVKS
INVDN