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Database: UniProt
Entry: A0A3Q3GMM2_9LABR
LinkDB: A0A3Q3GMM2_9LABR
Original site: A0A3Q3GMM2_9LABR 
ID   A0A3Q3GMM2_9LABR        Unreviewed;       778 AA.
AC   A0A3Q3GMM2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Cyclin-F {ECO:0000256|ARBA:ARBA00019493};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000035132.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000035132.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Essential for the control of the cell cycle at the G2/M
CC       (mitosis) transition. {ECO:0000256|ARBA:ARBA00003222}.
CC   -!- SUBUNIT: Interacts with the CDK1 protein kinase to form a
CC       serine/threonine kinase holoenzyme complex also known as maturation
CC       promoting factor (MPF). The cyclin subunit imparts substrate
CC       specificity to the complex. {ECO:0000256|ARBA:ARBA00025821}.
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   AlphaFoldDB; A0A3Q3GMM2; -.
DR   STRING; 56723.ENSLBEP00000035132; -.
DR   Ensembl; ENSLBET00000036628.1; ENSLBEP00000035132.1; ENSLBEG00000026388.1.
DR   GeneTree; ENSGT00810000125541; -.
DR   InParanoid; A0A3Q3GMM2; -.
DR   OrthoDB; 3020936at2759; -.
DR   Proteomes; UP000261660; Unplaced.
DR   GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   CDD; cd20521; CYCLIN_CCNF_rpt1; 1.
DR   CDD; cd22082; F-box_FBXO1; 1.
DR   Gene3D; 1.20.1280.50; -; 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; PF12937; F-box-like; 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:UP000261660}.
FT   DOMAIN          28..75
FT                   /note="F-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50181"
FT   REGION          613..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          662..706
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          737..778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..706
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        754..768
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   778 AA;  86241 MW;  D4AB14724154BEFD CRC64;
     MKAGVVHCRC SKCYSIPARK RVRKRTPALT LLSLPEEVLL CVLQCLSAED LLSVRAVHSQ
     LRDIVDNHSS VWARVSFRDT WPSPKTLWLF ERAAEKGNFE AAVKLGIAYL YNEGPLLSDE
     GRADVCGRKA SHFFSLAESL HSPLTDPFIW VFIRPPWSPT GSCCKAVVFD RLKAECDSNV
     EKRGPLLHCL ARVLQLFEGD ERRSDAISML KESSQAGCLQ SSYMLWEHNR KAAMADPGRY
     LQCVRTLRDY AGKGCWEAQV SLAKVCSSGN PLGLESKACS DLVAQLFSCN PASGHCTQGI
     LKRGIKDTMR YILVDWLVEV TTMKDFSSLT LHVTVGCVDR YLALRSVPKA RLQLLGIACM
     VVCTRYISKE ILTIREAVWL TDNTYKYEDL VRMMGEVVAV LEGKIRSPTL LDYGEVLLSL
     LPLERRTTHL FSYICELSLL YSALSSPPPA KLACAALLLT RALHHYAPLW PSQLVDYTGF
     SKQDLVSLAV LLFVKCFSQD VPKDYRHVSL TGVKQRFEDE AYRSISKERV MDYKELCQLL
     EIPEVEPQME PPSPTGQPAD IHTFLASPSS TSKRKRDDAM QAHRACFMAT PTAELSNQEE
     TLLGDIMDWS LDTSCSGYEG DQEEESEGEK DSDASMISIK LSPLTEDEKI LEHCRALSSD
     EDSFCEAEKD ESKDGQAPNP MSFPADLHTS GYSSIQSVSP SSTCSSSSLM PCTFKTLTTS
     LGAASANATP GFRLLVPMQR PRGTSGKQVK RKNSAAHSGG EVEREGDEYS ANAGFLSL
//
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