ID A0A3Q3X452_MOLML Unreviewed; 394 AA.
AC A0A3Q3X452;
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=G2/mitotic-specific cyclin-B2 {ECO:0000256|ARBA:ARBA00040980};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000022835.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000022835.1}
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 -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000256|ARBA:ARBA00006955}.
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DR AlphaFoldDB; A0A3Q3X452; -.
DR STRING; 94237.ENSMMOP00000022835; -.
DR Ensembl; ENSMMOT00000023214.1; ENSMMOP00000022835.1; ENSMMOG00000017358.1.
DR Proteomes; UP000261620; Unplaced.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:InterPro.
DR CDD; cd20507; CYCLIN_CCNB1-like_rpt1; 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; IPR046965; Cyclin_A/B-like.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR048258; Cyclins_cyclin-box.
DR PANTHER; PTHR10177; CYCLINS; 1.
DR PANTHER; PTHR10177:SF184; G2_MITOTIC-SPECIFIC CYCLIN-B2; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF001771; Cyclin_A_B_D_E; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
DR PROSITE; PS00292; CYCLINS; 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 Reference proteome {ECO:0000313|Proteomes:UP000261620}.
FT DOMAIN 168..252
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 261..379
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 265..346
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 36..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 394 AA; 44056 MW; 3C4FF3BDF9E2DCB2 CRC64;
PEWVETITNH QQRGPAENPL RMGKSTAAGQ RRAALGEITN SKAPAKAPAK APAKAPAKPS
CAQEAVPVQV VHPVVQVEAP ADPLPLPSEE PADASMKEEE EQLCQAFSDA LLTVQDVDEQ
DADLPQLCSQ YVKDIYNYLH VLEVQQAVRA NYMQGYEITE RMRALLVDWL VQVHSRFQLL
QETLYLTVAI LDRFLQVQPV SRRKLQLVGV TAMLVASKYE EMYAPEVGDF AYITDNAFTK
CQILEMEQVV LRGLNFQLGR PLPLHFLRRA SKVSNADVER HTLAKYLMEL TLVDYNMVHY
RPSEIAAASL CLSQLLLAGL PWSPTQRHYS TYDEAHLKPI MQHMAKNVVT VNEGKTKFLA
VKNKYSSSKL QKISLIPQLK SAVVKNMAAA LLNS
//
