ID A0A3Q1GJA5_9TELE Unreviewed; 743 AA.
AC A0A3Q1GJA5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Cyclin-F {ECO:0000256|ARBA:ARBA00019493};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000030731.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000030731.1}
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; A0A3Q1GJA5; -.
DR Ensembl; ENSAPOT00000032888.1; ENSAPOP00000030731.1; ENSAPOG00000017707.1.
DR GeneTree; ENSGT00810000125541; -.
DR Proteomes; UP000257200; 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:UP000257200}.
FT DOMAIN 28..75
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REGION 544..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 82866 MW; 56F58E241EDE0162 CRC64;
MKAGVVHCRC SKCYSVPARK RVRKRTPGLS LLSLPEEIVL YVLQCLSAED LLSVRAVHSQ
LRDVVDNHSS VWARVSFRDT WPSPSTLWLF ERAAEKGNFE AAVKLGIAYL YNEGPLLSDE
GRADVCGRKA SHFFSLAESL RSPTADPFIW VFIRPPWSPT GSCCKAVVFD RLKAECDDNV
VGRGPLLHCL ARVLQLFEDE RRSDAVSLLE ESSQAGCLQS SYLLWEHRRK AAMADPGRFL
QCVRTLRDYA GKGCWEAQLS LAKVCISGNP LGLEAKACSD LVSQLFTSSS PSLCLLMIRW
TLLRYILVDW LVEVTTMKDF SSLTLHVTVS CVDRYLALRS VPKARLQLLG IACMVVCTRY
ISKEILTIRE AVWLTDNTYK YEDLVRMMGE VVSVLWGRIR NPSLLDYGEV LLALVPLERR
SSHLFSYICE LSLLYSALAS PPPARLACAA LLLTRALHHH APLWPTLLAD HTGFSKEDLV
PLCVLLYVNC FSQDVPKDHR HVCLTGVKQR FEDENFQQIS REKVMDFKEL CQILEVPEVE
PQVELQVEPP SPAGQPTDLH TFLASPSSTS KRRRDDSMQT HRGSFVATPT AELSNQEETL
LGEILDWSLD TSCSGYEGDQ EESEEEKDGD ASMTSINLQP LSSADQRLEN CRAQSSDEDS
FCEADGKVKD DQGQENLTFS TDLHSSGYSS VQSVSPSSSS SLMLLVPMQR PRGSKQVKRK
NVAAHSGGEV EEERSANAGF LSL
//
