CCNF_DANRE
ID CCNF_DANRE Reviewed; 764 AA.
AC Q6NYX6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cyclin-F;
GN Name=ccnf;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=28444311; DOI=10.1093/hmg/ddx136;
RA Hogan A.L., Don E.K., Rayner S.L., Lee A., Laird A.S., Watchon M.,
RA Winnick C., Tarr I.S., Morsch M., Fifita J.A., Gwee S.S.L., Formella I.,
RA Hortle E., Yuan K.C., Molloy M.P., Williams K.L., Nicholson G.A.,
RA Chung R.S., Blair I.P., Cole N.J.;
RT "Expression of ALS/FTD-linked mutant CCNF in zebrafish leads to increased
RT cell death in the spinal cord and an aberrant motor phenotype.";
RL Hum. Mol. Genet. 26:2616-2626(2017).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins (By similarity). The SCF(CCNF) E3 ubiquitin-protein ligase
CC complex is an integral component of the ubiquitin proteasome system
CC (UPS) and links proteasome degradation to the cell cycle (By
CC similarity). Mediates the substrate recognition and the proteasomal
CC degradation of various target proteins during G2 phase involved in the
CC regulation of cell cycle progression and in the maintenance of genome
CC stability (By similarity). May play a role in motor neuron development
CC and axonal outgrowth (PubMed:28444311). {ECO:0000250|UniProtKB:P41002,
CC ECO:0000269|PubMed:28444311}.
CC -!- SUBUNIT: Component of the SCF(CCNF) complex.
CC {ECO:0000250|UniProtKB:P41002}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P41002}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41002}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriole {ECO:0000250|UniProtKB:P41002}. Note=Localization in the
CC centrosome is rare in S phase cells and increases in G2 cells,
CC Localizes on both the mother and daughter centrioles. Localizes to the
CC nucleus in G2 phase. {ECO:0000250|UniProtKB:P41002}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain.
CC {ECO:0000269|PubMed:28444311}.
CC -!- DEVELOPMENTAL STAGE: Initially ubiquitous expression at 12 hours post-
CC fertilization (hpf), then strongly expressed in the central nervous
CC system by 48 hpf (PubMed:28444311). Strongly expressed in the brain up
CC to 5 days post-fertilization (dpf) (PubMed:28444311). Ongoing
CC expression in whole brain tissue beyond 5 dpf into adulthood
CC (PubMed:28444311). {ECO:0000269|PubMed:28444311}.
CC -!- DOMAIN: The nuclear localization signals mediate the localization to
CC the nucleus. {ECO:0000250|UniProtKB:P41002}.
CC -!- DOMAIN: The D box motifs (amino acid sequence RxxL) are involved in
CC substrate binding, and may be ubiquitinated.
CC {ECO:0000250|UniProtKB:P41002}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
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DR EMBL; BC066425; AAH66425.1; -; mRNA.
DR RefSeq; NP_996931.1; NM_207048.1.
DR AlphaFoldDB; Q6NYX6; -.
DR SMR; Q6NYX6; -.
DR STRING; 7955.ENSDARP00000043143; -.
DR PaxDb; Q6NYX6; -.
DR Ensembl; ENSDART00000167177; ENSDARP00000141877; ENSDARG00000105046.
DR GeneID; 266981; -.
DR KEGG; dre:266981; -.
DR CTD; 899; -.
DR ZFIN; ZDB-GENE-021030-2; ccnf.
DR eggNOG; KOG0654; Eukaryota.
DR GeneTree; ENSGT00810000125541; -.
DR HOGENOM; CLU_020348_0_0_1; -.
DR InParanoid; Q6NYX6; -.
DR OMA; CHHQAKK; -.
DR OrthoDB; 607108at2759; -.
DR PhylomeDB; Q6NYX6; -.
DR TreeFam; TF101006; -.
DR Reactome; R-DRE-8951664; Neddylation.
DR Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q6NYX6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000105046; Expressed in testis and 39 other tissues.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
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:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0010826; P:negative regulation of centrosome duplication; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd00043; CYCLIN; 1.
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 InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR Pfam; PF12937; F-box-like; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS00292; CYCLINS; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cyclin; Cytoplasm; Cytoskeleton; Mitosis;
KW Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..764
FT /note="Cyclin-F"
FT /id="PRO_0000398636"
FT DOMAIN 28..75
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT DOMAIN 307..404
FT /note="Cyclin N-terminal"
FT /evidence="ECO:0000255"
FT REGION 583..738
FT /note="PEST"
FT REGION 662..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 19..27
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000250|UniProtKB:P41002"
FT MOTIF 309..312
FT /note="D box 1"
FT /evidence="ECO:0000250|UniProtKB:P41002"
FT MOTIF 570..575
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000250|UniProtKB:P41002"
FT COMPBIAS 676..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 764 AA; 84906 MW; A1C5F9B0E29ADC3E CRC64;
MKAGALHCRC AKCFSLPVRK RVRKRASAVS LLSLPEELLV FVLQCLSAED LLSVRAVHSH
LCDIIDTNAS IWARVSFKDR WPAPDTVWLF ERAAEKGNFE AAVKLGIAYL YNEGPLLSEE
GRADLCGRMA SRYLSLSESL RSPQAEPFIW LFIRPPWSVS GSCCKAVVFD RLQAECQTSP
GRKGTLLYCL ARVLQLFDDE EKRDEAELML KESSRCGSLQ SSYLLWAISR ASSTADPGRY
LQCMRTLRDY AARGCWEAQL AFVKSCGSAN PLGLEPRACS ELVSQFFQTG PSALRYQPHL
QGQDITTKRY ILVDWLVEVT TTKDFSSQVL HVTISCVDRY LHLRSVPKAQ LQLLGIACMV
ICTRFISKEI LTIREAVWLT DNTYQYEDLV HMMGEVISVL DGKIRTPTVL DYGEVLLSLL
PVERRTAHLF SYICELSLLC SPATVPGPAR LASAILLLTR ALHNYVPVWP VQLEENTGFS
KQDLVSCALT LYIKCFGQDV PKDYRHVSLT GVKQRFEDDS YQQISKDTVM GFKELCHVLE
VPEVEPQVEV SSTSGQITEM HTFLSSPTSS SKRRRADSMQ AHRGAFVATP TAELSNQEET
LLGDFLDWSL DTSCSGYEGD RESEGEKDGE ISTMEVQMEL PLDCADRQTH CCLLSSDDTS
LCEEDEQEPP TGGSKPWTRH LSSSSTSSSS SSCGFCTDRH SSGYSSIQSF PSPTGSSALV
SPQNPPGVPS QRIRRQVKRK NTAAHSAGEA EQEDDAANLA FLSF
