CCNO_MOUSE
ID CCNO_MOUSE Reviewed; 352 AA.
AC P0C242;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cyclin-O {ECO:0000305};
GN Name=Ccno {ECO:0000312|MGI:MGI:2145534};
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].
RC STRAIN=C57BL/6 X CBA/Ca; TISSUE=Oocyte;
RX PubMed=16697536; DOI=10.1016/j.gene.2006.02.030;
RA Hirst R., Gosden R., Miller D.;
RT "The cyclin-like uracil DNA glycosylase (UDG) of murine oocytes and its
RT relationship to human and chimpanzee homologues.";
RL Gene 375:95-102(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic head;
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 TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=19609756; DOI=10.1007/978-1-60327-017-5_12;
RA Roset R., Gil-Gomez G.;
RT "Measurement of changes in Cdk2 and cyclin o-associated kinase activity in
RT apoptosis.";
RL Methods Mol. Biol. 559:161-172(2009).
RN [4]
RP FUNCTION.
RX PubMed=18927588; DOI=10.1038/cdd.2008.145;
RA Roig M.B., Roset R., Ortet L., Balsiger N.A., Anfosso A., Cabellos L.,
RA Garrido M., Alameda F., Brady H.J., Gil-Gomez G.;
RT "Identification of a novel cyclin required for the intrinsic apoptosis
RT pathway in lymphoid cells.";
RL Cell Death Differ. 16:230-243(2009).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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 (By similarity). May be involved in apoptosis in lymphoid
CC cells; however, this result requires additional evidences in vivo. May
CC be involved in oocyte meiotic resumption in oocytes. {ECO:0000250,
CC ECO:0000269|PubMed:18927588, ECO:0000269|PubMed:19609756,
CC ECO:0000269|PubMed:26777464}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24747639,
CC ECO:0000269|PubMed:26777464}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P22674}. Note=Localizes to the apical part of
CC cytoplasm. {ECO:0000269|PubMed:24747639}.
CC -!- TISSUE SPECIFICITY: Present in respiratory cells (at protein level).
CC Expressed in multiciliated tissue in brain and fallopian tube (at
CC protein level) (PubMed:26777464). Highly expressed in oocytes.
CC {ECO:0000269|PubMed:19609756, ECO:0000269|PubMed:24747639,
CC ECO:0000269|PubMed:26777464}.
CC -!- DEVELOPMENTAL STAGE: Expressed in ependymal cells of the embryonic
CC brain, but almost absent in the adult brain.
CC {ECO:0000269|PubMed:26777464}.
CC -!- SIMILARITY: Belongs to the cyclin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK086507; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK086507; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS36782.1; -.
DR RefSeq; NP_001074531.1; NM_001081062.1.
DR AlphaFoldDB; P0C242; -.
DR SMR; P0C242; -.
DR STRING; 10090.ENSMUSP00000040083; -.
DR PhosphoSitePlus; P0C242; -.
DR PaxDb; P0C242; -.
DR PRIDE; P0C242; -.
DR ProteomicsDB; 281341; -.
DR Antibodypedia; 11078; 220 antibodies from 26 providers.
DR DNASU; 218630; -.
DR Ensembl; ENSMUST00000038404; ENSMUSP00000040083; ENSMUSG00000042417.
DR GeneID; 218630; -.
DR KEGG; mmu:218630; -.
DR UCSC; uc007rwz.1; mouse.
DR CTD; 10309; -.
DR MGI; MGI:2145534; Ccno.
DR VEuPathDB; HostDB:ENSMUSG00000042417; -.
DR eggNOG; KOG0653; Eukaryota.
DR GeneTree; ENSGT00940000155998; -.
DR HOGENOM; CLU_020695_1_0_1; -.
DR InParanoid; P0C242; -.
DR OMA; EHFTHAR; -.
DR OrthoDB; 752095at2759; -.
DR PhylomeDB; P0C242; -.
DR TreeFam; TF332057; -.
DR BioGRID-ORCS; 218630; 2 hits in 111 CRISPR screens.
DR PRO; PR:P0C242; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P0C242; protein.
DR Bgee; ENSMUSG00000042417; Expressed in primary oocyte and 48 other tissues.
DR ExpressionAtlas; P0C242; baseline and differential.
DR Genevisible; P0C242; MM.
DR GO; GO:0097124; C:cyclin A2-CDK2 complex; IBA:GO_Central.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISO:MGI.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:1903251; P:multi-ciliated epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
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.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cilium biogenesis/degradation; Cyclin;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..352
FT /note="Cyclin-O"
FT /id="PRO_0000261156"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22674"
SQ SEQUENCE 352 AA; 38822 MW; 001F10138A890719 CRC64;
MVTPCPASPG SPAAGAGRRD SHQNLRAPVK KSRRPCLRRK KPLRPLNACS LPGDSGVCDL
FESPSSSSDG ADSPAVSAAR DCSSLLNPAQ PLTALDLQTF REYGQSCYDF RKAQENLFHP
RESLARQPQV TAESRCKLLS WLLQVHRQFG LSFESLCLTV NTLDRFLLTT PVAADCFQLL
GVTCLLIACK QVEVHPPRLK QLLALCGGAF SRQQLCNLEC IVLHKLHFSL GAPTINFFLE
HFTQWRMEAG QAEVTEALEA QTLARGVAEL SLTDYAFTTY TPSLMAICCL ALADGLLQHQ
HEMDLRLGEH PEATLQDCLG KLQTLVSINS SSLPRILPPQ IWERCSLPQS WQ
