CCNF_BOVIN
ID CCNF_BOVIN Reviewed; 788 AA.
AC A5PK16;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Cyclin-F;
GN Name=CCNF;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) 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 1-5 (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; BC142318; AAI42319.1; -; mRNA.
DR RefSeq; NP_001092340.1; NM_001098870.2.
DR AlphaFoldDB; A5PK16; -.
DR SMR; A5PK16; -.
DR STRING; 9913.ENSBTAP00000034530; -.
DR PaxDb; A5PK16; -.
DR PRIDE; A5PK16; -.
DR GeneID; 505200; -.
DR KEGG; bta:505200; -.
DR CTD; 899; -.
DR eggNOG; KOG0654; Eukaryota.
DR HOGENOM; CLU_020348_0_0_1; -.
DR InParanoid; A5PK16; -.
DR OrthoDB; 607108at2759; -.
DR TreeFam; TF101006; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010826; P:negative regulation of centrosome duplication; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
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..788
FT /note="Cyclin-F"
FT /id="PRO_0000398634"
FT DOMAIN 29..76
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT DOMAIN 291..405
FT /note="Cyclin N-terminal"
FT /evidence="ECO:0000255"
FT REGION 566..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..766
FT /note="PEST"
FT REGION 700..788
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 351..354
FT /note="D box 4"
FT /evidence="ECO:0000250|UniProtKB:P41002"
FT MOTIF 568..574
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000250|UniProtKB:P41002"
FT MOTIF 767..770
FT /note="D box 5"
FT /evidence="ECO:0000250|UniProtKB:P41002"
FT COMPBIAS 700..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 788 AA; 87898 MW; 44621CC1B81BC5CE CRC64;
MGSGGVIHCR CAKCFCYPSK RRIRRRPRNL TILNLPEDAL FHILKWLSVG DILAVRAVHS
HLKYLVDNHA SVWACASFQE LWPSPGNLKL FERAAEKGNF EAAVKLGIAY LYNEGLSVSD
EARAEVNGLR ASRYFSLAER LNVGAAPFIW LFIRPPWSVS GSCCKAVVHE SLRAECQLQK
THRASILHCL GRVLSLFEDE EKQKQARKLF EESANQGCLT SSYLLWESDR RMDMLDPGRC
LHSFRKLRDF AAKGCWEAQL SLAKACAHGH QLGLEAKASS EIVCQLFQAS HAVNKQRVFS
VQKGLNDTMR YILIDWLVEV ATMKDFSSLC LHLTVECVDR YLRRRLVPRY RLQLLGIACM
VICTRFISKE ILTIREAVWL TDNTYKYEDL VRMMGEVVSA LDGKIRVPTV VDYKDVLLTL
VPMAPRTQHL CSFLCELSLL HTSLAAYAPA HLAAAALLLA RLTHGQTQPW TTQLWDLTGF
SCEDLIPCVL SLHQKCFHDD APKDYRQVSL TAVKQRFEDK RYEEISLEEV LSYGQLCAAL
GVKQESLEPA PFLSAGDIHA FLSSPSARRT KRKRENSLQE DRGSFVTTPT AELSSQEETL
LGSFLDWSLD YCSGYEGDQE SEGEKEGDVT APSGVLDVTV VYLSPEEHCC QESSDEEACP
EEACGAQDTQ ALVPGHQALR TPGPEPPLCS RWGLGKDVTT SGYSSVNSAS PTDSGRTSGG
PPRSTSELPT GSSLNTQPCH HHARKSCLQC RPPSPPESCA PQQQVKRKNL SAHSEEEEED
MNLGFLKL
