ID A0A3Q1HYL5_ANATE Unreviewed; 292 AA.
AC A0A3Q1HYL5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=G1/S-specific cyclin-D1 {ECO:0000256|ARBA:ARBA00039573};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000014187.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000014187.1}
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 {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily.
CC {ECO:0000256|ARBA:ARBA00009065}.
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DR AlphaFoldDB; A0A3Q1HYL5; -.
DR STRING; 64144.ENSATEP00000014187; -.
DR Ensembl; ENSATET00000014416.2; ENSATEP00000014187.1; ENSATEG00000009890.2.
DR GeneTree; ENSGT00940000157816; -.
DR InParanoid; A0A3Q1HYL5; -.
DR OrthoDB; 1077601at2759; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0005737; C: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; cd20573; CYCLIN_CCND1_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; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR048258; Cyclins_cyclin-box.
DR PANTHER; PTHR10177; CYCLINS; 1.
DR PANTHER; PTHR10177:SF67; G1_S-SPECIFIC CYCLIN-D1; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 62..146
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 155..284
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
SQ SEQUENCE 292 AA; 33062 MW; 56321C455B77406B CRC64;
MEDQLLCCEV DSIRRAYQDV NLLNDRVLHT MLKAEENYLP SPNYFKCVQK EIVPKMRKIV
ATWMLEVCEE QKCEEEVFPL AMNYLDRFLS VEATRKTRLQ LLGATCMFLA SKMKETVPLT
AEKLCIYTDN SVQPGELLQM ELLVLNKLKW DLASVTSHDF IEHFLSKLKI HPSTKQILRK
HAQTFVALCA TDVNFIASPP SMVAAGSVVA AVQGLYLKSQ DASLSSENLT NFLSQVIRSD
PDCLRSCQEQ IESLLESSLR QAQQHSSATE TKHVDEDVDL SCTPTDVRDI NI
//