CCNF_XENLA
ID CCNF_XENLA Reviewed; 761 AA.
AC Q7T0L6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Cyclin-F;
GN Name=ccnf;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2003) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC056134; AAH56134.1; -; mRNA.
DR RefSeq; NP_001079901.1; NM_001086432.1.
DR AlphaFoldDB; Q7T0L6; -.
DR SMR; Q7T0L6; -.
DR DNASU; 379591; -.
DR GeneID; 379591; -.
DR KEGG; xla:379591; -.
DR CTD; 379591; -.
DR Xenbase; XB-GENE-963734; ccnf.L.
DR OrthoDB; 607108at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 379591; Expressed in oocyte and 19 other tissues.
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: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..761
FT /note="Cyclin-F"
FT /id="PRO_0000398637"
FT DOMAIN 28..75
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT DOMAIN 300..411
FT /note="Cyclin N-terminal"
FT /evidence="ECO:0000255"
FT REGION 575..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..745
FT /note="PEST"
FT REGION 677..761
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 COMPBIAS 685..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 84500 MW; 8BFB3EA39C602A81 CRC64;
MKGGGLHCRC SKCFAAPPRR RIKRRPRVLT LLSLPEDVLL YVLECLPAVD ILSMREVHPH
LRSLVDSHSS VWARASFQDV WPSSENLNLF ERAAECGNFE ACVKLGIAYL YNEGLSVSDD
GRAEVNGLKA SRFFSLTERL NAGADPFVWL FIRPPWSSSG SCCKAVVFDS LNEECGTVTS
GEGATGALKG SIQYCLAKVL SLFEDDDKKR EALGMLESSA SNGCLHSAYL LWETKQKAAL
SDPGRYLQSF RQLRDYAARG CWDAQISLAK ACGHKNPLNQ EQRSAGELVN QVFQSSLPIN
KSSIFTTQKG MNDTMRYILI DWLVEVATMK DFSSLCLHMT VGLVDRYLKL RSVPRAKLQL
VGIACMVICT RFISKEILTI REAVWLTDNT YKYEDLVRMM GEIISALEGK IRMPTVVDYK
DVLSHLIPLD RNTLHLCSYI SELSLLYTEL SMYSPAQLAA GALLLARILH RQARPWPAQL
AETTGFTLEH LTPCVVLLHK KCFHDDAPRD YRQVSLTAVK QRFQDDLYDQ ISKEKVMDHT
HLCELLGVPC HDSESPATCP NAADFHQFLC SPSGNKTKRR REESIQEDRG SFVTTPTAEL
SNQEEDLLGD FLDWSLETSC SGYEGDRESE GEREGEVTAP SGVLDLSLLL TEHPQCQDST
TDDDSITLHP IPLLSKAENG TDSIEGCVEK SSGYSSVSSG GSPTSSSSPG LPFTPTPGLN
HSKLTPIPFP QPCSPLLKAS RRQVKRKNQA QHSEDNLSDE L
