ID   CCNF_XENTR              Reviewed;         763 AA.
AC   Q5XGG5;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Cyclin-F;
GN   Name=ccnf;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Substrate recognition component of the SCF(CCNF) E3
CC       ubiquitin-protein ligase complex which mediates the ubiquitination and
CC       subsequent proteasomal degradation of target proteins (By similarity).
CC       The SCF(CCNF) E3 ubiquitin-protein ligase complex is an integral
CC       component of the ubiquitin proteasome system (UPS) and links proteasome
CC       degradation to the cell cycle (By similarity). Mediates the substrate
CC       recognition and the proteasomal degradation of various target proteins
CC       during G2 phase involved in the regulation of cell cycle progression
CC       and in the maintenance of genome stability (By similarity).
CC       {ECO:0000250|UniProtKB:P41002}.
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   -!- 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; BC084474; AAH84474.1; -; mRNA.
DR   RefSeq; NP_001011083.1; NM_001011083.1.
DR   AlphaFoldDB; Q5XGG5; -.
DR   SMR; Q5XGG5; -.
DR   STRING; 8364.ENSXETP00000027235; -.
DR   PaxDb; Q5XGG5; -.
DR   DNASU; 496496; -.
DR   Ensembl; ENSXETT00000027235; ENSXETP00000027235; ENSXETG00000012459.
DR   GeneID; 496496; -.
DR   KEGG; xtr:496496; -.
DR   CTD; 899; -.
DR   Xenbase; XB-GENE-963729; ccnf.
DR   eggNOG; KOG0654; Eukaryota.
DR   HOGENOM; CLU_020348_0_0_1; -.
DR   InParanoid; Q5XGG5; -.
DR   OMA; CHHQAKK; -.
DR   OrthoDB; 607108at2759; -.
DR   TreeFam; TF101006; -.
DR   Reactome; R-XTR-8951664; Neddylation.
DR   Reactome; R-XTR-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   Proteomes; UP000008143; Chromosome 9.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000012459; Expressed in gastrula and 14 other tissues.
DR   ExpressionAtlas; Q5XGG5; baseline.
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; 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; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..763
FT                   /note="Cyclin-F"
FT                   /id="PRO_0000398638"
FT   DOMAIN          28..75
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   DOMAIN          299..411
FT                   /note="Cyclin N-terminal"
FT                   /evidence="ECO:0000255"
FT   REGION          574..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..747
FT                   /note="PEST"
FT   REGION          677..763
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           316..319
FT                   /note="D box 1"
FT                   /evidence="ECO:0000250|UniProtKB:P41002"
FT   MOTIF           355..358
FT                   /note="D box 2"
FT                   /evidence="ECO:0000250|UniProtKB:P41002"
FT   MOTIF           575..581
FT                   /note="Nuclear localization signal 2"
FT                   /evidence="ECO:0000250|UniProtKB:P41002"
FT   COMPBIAS        678..709
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        749..763
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   763 AA;  84864 MW;  E9A52555CDDB22E5 CRC64;
     MKGGALHCRC SKCFAAPPKR RVKRRPRVLT LLSLPEDVLL YVLECLPAVD ILSMREVHPH
     LRSLVDSHSS VWARASFQDV WPSPENLNLF ERAAECGNFE ACVKLGIAYL YNEGLSLSDD
     GRAEVNGLKA SRFFSLTERL NSGADPFVWL FIRPPWSSSG SCCKAVVFDS LKEECGTVTS
     EEGATGALKG SIQYCLAKVL SLFEDDDKKR EALGMLESSA SHGCLHSSYL LWETKQKTAL
     SDPGRYLQSF RQLRDYAARG CWDAQISLAK ACGHKNQLSQ EQRSASELVN QVFQSSLPIN
     KTSIFTTQKG MNDTMRYILI DWLVEVATMK DFSSLCLHMT VGLVDRYLKL RSVPRAKLQL
     VGIACMVICT RFISKEILTI REAVWLTDNT YKYEDLVRMM GEIISALEGK IRMPTVVDYK
     DVLSHLIPLD RSTLHLCSYI SELSLLYTEL STYSPAQLAA GALLLARILH KQARPWPAQL
     AETTGFTLEH LTPCVVLLHK KCFHDDAPKD YRQVSLTAVK QRFQDDLYDQ ISKEKVMDHS
     HLCELLGVPC RDSESPASCP NAADFHQFLC SPSGSKTKRR REDSIQEDRG SFVTTPTAEL
     SNQEEDLLGD FLDWSLETSC SGYEGDRESE GEREGEVTAP SGVLDLSLLI TEHQQCQDTT
     SDDDSLVPLH PIPLLSKLEN GTHSTEGCAE KSSGYSSVSS GGSPTSSSSP PGLPFTPTPG
     LNHSKLMPIP FPQPCSPLFK ASRRQVKRKN QAQHSEDNLS DEL