ID A0A3Q3BR62_KRYMA Unreviewed; 340 AA.
AC A0A3Q3BR62;
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=G1/S-specific cyclin-D2 {ECO:0000256|ARBA:ARBA00039574};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000029094.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000029094.1}
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: Membrane {ECO:0000256|ARBA:ARBA00004370}. Nucleus
CC membrane {ECO:0000256|ARBA:ARBA00004126}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily.
CC {ECO:0000256|ARBA:ARBA00009065}.
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DR RefSeq; XP_017274530.1; XM_017419041.1.
DR AlphaFoldDB; A0A3Q3BR62; -.
DR STRING; 37003.ENSKMAP00000029094; -.
DR Ensembl; ENSKMAT00000029458.1; ENSKMAP00000029094.1; ENSKMAG00000021573.1.
DR GeneID; 108237544; -.
DR KEGG; kmr:108237544; -.
DR CTD; 799608; -.
DR GeneTree; ENSGT00940000155180; -.
DR OMA; CLEMDTN; -.
DR OrthoDB; 1077601at2759; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0031965; C:nuclear membrane; 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; cd20577; CYCLIN_CCND2_rpt2; 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 PANTHER; PTHR10177; CYCLINS; 1.
DR PANTHER; PTHR10177:SF66; G1_S-SPECIFIC CYCLIN-D2; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 1.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 104..188
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 197..335
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT REGION 300..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 340 AA; 39552 MW; 3BB425375FD4927F CRC64;
MFCPATLFLR FREENYYFFL SSFFFFFFFF FFFFFYLSES PSTMELLCLE MDTNIRARPD
PNLLCDDRVL QSLLTIEERF LPQYSYFKGV QKDIQPFMRR MVATWMLEVC EEQKCEEEVF
PLAMNYLDRF LAMVPIKKCN LQLLGAVCMF LASKLKETRP LTAEKLCIYT DNSIRPQELL
EWELVVLGKL KWNLAAVTPN DFIEHIVRRL PLPEDKLALI RKHVQTFIAL CATDFRFAMY
PPSMIATGSV GAAICGLQLD SPDQSQWGDS LTDLLAKITN TEVDVLKECQ EQIERVLESS
LREGRQQQQQ QQQTQRGPSG KGLDELDQSS TPTDVRDVNL
//
