ID M3VXM0_FELCA Unreviewed; 848 AA.
AC M3VXM0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 4.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Cyclin-F {ECO:0000256|ARBA:ARBA00019493};
GN Name=CCNF {ECO:0000313|Ensembl:ENSFCAP00000001809.6,
GN ECO:0000313|VGNC:VGNC:60559};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000001809.6, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000001809.6, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001809.6,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000001809.6, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001809.6,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000001809.6}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001809.6};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}.
CC Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000256|ARBA:ARBA00006955}.
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DR EMBL; AANG04001668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3VXM0; -.
DR STRING; 9685.ENSFCAP00000001809; -.
DR PaxDb; 9685-ENSFCAP00000001809; -.
DR Ensembl; ENSFCAT00000001956.6; ENSFCAP00000001809.6; ENSFCAG00000001956.6.
DR VGNC; VGNC:60559; CCNF.
DR eggNOG; KOG0654; Eukaryota.
DR GeneTree; ENSGT00810000125541; -.
DR HOGENOM; CLU_020348_0_0_1; -.
DR InParanoid; M3VXM0; -.
DR OMA; HQAKKSC; -.
DR Proteomes; UP000011712; Chromosome E3.
DR Bgee; ENSFCAG00000001956; Expressed in testis and 8 other cell types or tissues.
DR GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0010997; F:anaphase-promoting complex binding; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0001890; P:placenta development; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:Ensembl.
DR GO; GO:0000320; P:re-entry into mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR CDD; cd20521; CYCLIN_CCNF_rpt1; 1.
DR CDD; cd22082; F-box_FBXO1; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR048258; Cyclins_cyclin-box.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR PANTHER; PTHR10177:SF496; CYCLIN-F; 1.
DR PANTHER; PTHR10177; CYCLINS; 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; Cyclin-like; 2.
DR SUPFAM; SSF81383; F-box domain; 1.
DR PROSITE; PS00292; CYCLINS; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712}.
FT DOMAIN 65..112
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REGION 619..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 848 AA; 93828 MW; 8BA47F37A6F0CE72 CRC64;
MIPLMLGSRH VAGSFCGGGG TVTVSPLLSS PSPGPLCRFS SVIHCRCAKC FCYPTKRRIR
RRPRNLTILS LPEDVLFHIL KWLSVGDILA VRAVHSHLKN LVDGHASVWA CASFQELWPS
PKNLKLFERA AEKGNFEAAV KLGIAYLYNE GLSVSDEARA EVNGLKASRF FSLAEQLNAG
STPFIWLFIR PPWSVSGSCC KAVVHESLRA ECQLQGVNPV EEHAWGPHAG RSEPHRTHRA
SILHCLGRVL SLFEDAERKQ QARDLFEESA RQGCLASSYL LWERDRRTDM SDPGRCLHSF
RKLRDYAAKG CWEAQLSLAK ACANGGQLGL EGKVADGVAR RLFQASRAVS KQQVFSVQKG
LSDTMRYILI DWLVEVATMK DFTSLCLHLT VECVDRYLRR RLVPRYRLQL LGIACMVICT
RFISREILTI REAVWLTDNT YKYEDLVRMM GEIISALEGR IRVPTVVDYK DVLLTLVPEA
PRTQHLCGFL CELSLLHTSL AAYAPACLAA AALLLARLTH GQTQPWTTRL WDITGFSCED
LIPCVLSLHQ KCFHDDAPKD YRQVSLTAVK QRFEDKRYEE ISREEVLSYG QLCAALGVKQ
GSPEPTSFLS AGDIHTFLSS PSGRRTKRKR ENSLQEDRGS FVTTPTAELS SQEEVLLGSF
LDWSLDYCSG YEGDQESEGE KDGDVTAPSG VLDVTVVYLN PEQHCCQESS DDEACPEAGG
RQDVRAYVPG TQTPPSPGPQ PLLHGRREPG KDSVTSGYSS ICSASPTDSV DGVSGASPRS
TSVPSPGSDS GTQPCRQHAK KPCLQCHSPS PLESSTPQRQ VKRKNLSAHS EEEEEEDEDE
ERGLSPAC
//
