CCNF_RAT
ID CCNF_RAT Reviewed; 780 AA.
AC Q8K4F8; D3ZCW7;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Cyclin-F;
GN Name=Ccnf;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-747.
RC STRAIN=Brown Norway;
RA Behboudi A., Medin C., Levan G.;
RT "Rat Cyclin F.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
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 involved in the regulation of
CC cell cycle progression and in the maintenance of genome stability (By
CC similarity). Mediates the ubiquitination and subsequent proteasomal
CC degradation of CP110 during G2 phase, thereby acting as an inhibitor of
CC centrosome reduplication (By similarity). In G2, mediates the
CC ubiquitination and proteasomal degradation of CDC6, thereby suppressing
CC DNA re-replication and preventing genome instability (By similarity).
CC Involved in the ubiquitination and degradation of the substrate adapter
CC CDH1 of the anaphase-promoting complex (APC/C), thereby acting as an
CC antagonist of APC/C in regulating G1 progression and S phase entry (By
CC similarity). May play a role in the G2 cell cycle checkpoint control
CC after DNA damage, possibly by promoting the ubiquitination of
CC MYBL2/BMYB (By similarity). {ECO:0000250|UniProtKB:P41002}.
CC -!- SUBUNIT: Component of the SCF(CCNF) complex consisting of CUL1, RBX1,
CC SKP1 and CCNF (By similarity). Interacts with SKP1 (By similarity).
CC Interacts with CUL1 (By similarity). Interacts with CCNB1; interaction
CC is required for nuclear localization of CCNB1 (By similarity).
CC Interacts with CCP110; this interaction leads to CCP110 ubiquitination
CC and degradation via the proteasome pathway (By similarity). Interacts
CC (via the Cyclin N-terminal domain) with MYBL2/BMYB (By similarity).
CC Interacts with FZR1/CDH1 (via N-terminus) (By similarity). Interacts
CC with RRM2 (via Cy motif and when phosphorylated at 'Thr-33'); the
CC interaction occurs exclusively in G2 and early M (By similarity).
CC Interacts with CDC6 (via Cy motif); the interaction takes place during
CC G2 and M phase (By similarity). {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. Localization to
CC centrosomes is not dependent on CP110. Localizes to the nucleus in G2
CC phase. {ECO:0000250|UniProtKB:P41002}.
CC -!- DOMAIN: The nuclear localization signals mediate the localization to
CC the nucleus and are required for CCNB1 localization to the nucleus.
CC {ECO:0000250|UniProtKB:P41002}.
CC -!- DOMAIN: The D box motifs 1-4 (amino acid sequence RxxL) are involved in
CC substrate binding, such as FZR1/CDH1, and may be ubiquitinated.
CC {ECO:0000250|UniProtKB:P41002}.
CC -!- PTM: Degraded when the spindle assembly checkpoint is activated during
CC the G2-M transition. Degradation is not dependent on the proteasome or
CC ubiquitin and depends on the C-terminal PEST sequence.
CC {ECO:0000250|UniProtKB:P41002}.
CC -!- PTM: Phosphorylated just before cells enter into mitosis.
CC {ECO:0000250|UniProtKB:P41002}.
CC -!- PTM: Ubiquitinated by the anaphase-promoting complex (APC/C); leading
CC to its degradation by the proteasome. {ECO:0000250|UniProtKB:P41002}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
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DR EMBL; AF410816; AAM46626.1; -; mRNA.
DR RefSeq; NP_001093944.1; NM_001100474.1.
DR AlphaFoldDB; Q8K4F8; -.
DR SMR; Q8K4F8; -.
DR STRING; 10116.ENSRNOP00000060445; -.
DR iPTMnet; Q8K4F8; -.
DR PhosphoSitePlus; Q8K4F8; -.
DR PaxDb; Q8K4F8; -.
DR Ensembl; ENSRNOT00000064392; ENSRNOP00000060445; ENSRNOG00000007483.
DR GeneID; 117524; -.
DR KEGG; rno:117524; -.
DR UCSC; RGD:67401; rat.
DR CTD; 899; -.
DR RGD; 67401; Ccnf.
DR eggNOG; KOG0654; Eukaryota.
DR GeneTree; ENSGT00810000125541; -.
DR HOGENOM; CLU_020348_0_0_1; -.
DR InParanoid; Q8K4F8; -.
DR OMA; CHHQAKK; -.
DR OrthoDB; 607108at2759; -.
DR PhylomeDB; Q8K4F8; -.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q8K4F8; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000007483; Expressed in thymus and 19 other tissues.
DR Genevisible; Q8K4F8; RN.
DR GO; GO:0030054; C:cell junction; IEA:Ensembl.
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:0010997; F:anaphase-promoting complex binding; ISO:RGD.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:UniProt.
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:0001890; P:placenta development; ISO:RGD.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0000320; P:re-entry into mitotic cell cycle; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0010033; P:response to organic substance; IEA:UniProt.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd00043; CYCLIN; 1.
DR Gene3D; 1.25.40.10; -; 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 InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR Pfam; PF00646; F-box; 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; Phosphoprotein; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..780
FT /note="Cyclin-F"
FT /id="PRO_0000398635"
FT DOMAIN 29..76
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT DOMAIN 288..405
FT /note="Cyclin N-terminal"
FT /evidence="ECO:0000255"
FT REGION 544..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..761
FT /note="PEST"
FT REGION 651..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 20..28
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000250|UniProtKB:P41002"
FT MOTIF 310..313
FT /note="D box 1"
FT /evidence="ECO:0000250|UniProtKB:P41002"
FT MOTIF 343..346
FT /note="D box 2"
FT /evidence="ECO:0000250|UniProtKB:P41002"
FT MOTIF 349..352
FT /note="D box 3"
FT /evidence="ECO:0000250|UniProtKB:P41002"
FT MOTIF 568..574
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000250|UniProtKB:P41002"
FT MOTIF 762..765
FT /note="D box 4"
FT /evidence="ECO:0000250|UniProtKB:P41002"
FT COMPBIAS 548..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 780 AA; 86790 MW; 9E3BC35E7C35AF07 CRC64;
MGSGGVIHCR CAKCFCYPTK RRIKRRPRNL TILSLPEDVL FHILKWLSVG DILAVRAVHS
HLKYLVDNHA SVWASASFQE LWPSPQNLKL FERAAEKGNF EAAVKLGIAY LYNEGLSVSD
EACAEVNGLK ASRFFSMAER LNTGSDPFIW LFIRPPWSVS GSCCKAVVHD SLRAECQLQR
SHKASILHCL GRVLNLFEDE EKRKQAHNLF EESAHQGCLA SSYLLWESDR KVDMSDPGRC
LHSFRKLRDY AAKGCWEAQL ALAKACAGGS QLGLEGKACS ESVCQLFQAS QAVNKQQIFS
VQKGLSDTMR YILIDWLVEV ATMKDFTSLC LHLTVECVDR YLRRRLVPRY KLQLLGIACM
VICTRFISKE ILTIREAVWL TDNTYKYEDL VRVMGEIISA LEGKIRIPTV VDYKEVLLTL
VPVAPRTQHL CSFLCELTLL HTSLSVYAPA RLASAALLLA RLMHGHTQPW TTQLWDLTGF
SYSDLTPCVL SLHKKCFHDD APKDYRQVSL TAVKQRFEDK CYEEISQEEV LSYAELCSAL
GVKQESPEPP SFPSSGEIHT FLSSPSGRRS KRKRENSLQE DRGSFVTTPT AELSNQEETL
LGSLLDWSLD CCSGYEGDQE SEGEKEGDVT APSGLLDVTV VYLNPEEHCC QESSDEEVWP
EDKSHPTPGT QAPPASAPWP LPCNRGDPGK DVTTSGYSSV SSSSPISSLD GGMVGSPRST
SVLSVGSHSS TKPCYHQAKK SCLQCRPPNP PESGAHQQPV KRQNLSVHSD EDTNLGFLKL
