ID   CCND1_XENLA             Reviewed;         291 AA.
AC   P50755;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=G1/S-specific cyclin-D1;
GN   Name=ccnd1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Cockerill M.J., Hunt T.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulatory component of the cyclin D1-CDK4 (DC) complex that
CC       phosphorylates and inhibits members of the retinoblastoma (RB) protein
CC       family including RB1 and regulates the cell-cycle during G(1)/S
CC       transition. Phosphorylation of RB1 allows dissociation of the
CC       transcription factor E2F from the RB/E2F complex and the subsequent
CC       transcription of E2F target genes which are responsible for the
CC       progression through the G(1) phase. Hypophosphorylates RB1 in early
CC       G(1) phase. Cyclin D-CDK4 complexes are major integrators of various
CC       mitogenenic and antimitogenic signals. {ECO:0000250|UniProtKB:P24385}.
CC   -!- SUBUNIT: Interacts with the cdk4 and cdk6 protein kinases to form a
CC       serine/threonine kinase holoenzyme complex (By similarity). The cyclin
CC       subunit imparts substrate specificity to the complex (By similarity).
CC       {ECO:0000250|UniProtKB:P24385}.
CC   -!- INTERACTION:
CC       P50755; Q91727: cdk4; NbExp=2; IntAct=EBI-7270567, EBI-7270544;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P24385}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P24385}.
CC   -!- PTM: Phosphorylation at Thr-282 by MAP kinases is required for
CC       ubiquitination and degradation by the DCX(AMBRA1) complex.
CC       {ECO:0000250|UniProtKB:P24385}.
CC   -!- PTM: Ubiquitinated by the DCX(AMBRA1) complex during the transition
CC       from G1 to S cell phase, leading to its degradation. The DCX(AMBRA1)
CC       complex represents the major regulator of CCND1 stability during the
CC       G1/S transition. {ECO:0000250|UniProtKB:P24385}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X89475; CAA61664.1; -; mRNA.
DR   PIR; S57922; S57922.
DR   AlphaFoldDB; P50755; -.
DR   SMR; P50755; -.
DR   IntAct; P50755; 1.
DR   MINT; P50755; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0017053; C:transcription repressor complex; ISS:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR   CDD; cd00043; CYCLIN; 1.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR015451; Cyclin_D.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10177; PTHR10177; 1.
DR   PANTHER; PTHR10177:SF67; PTHR10177:SF67; 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; SSF47954; 2.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cyclin; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..291
FT                   /note="G1/S-specific cyclin-D1"
FT                   /id="PRO_0000080436"
FT   MOD_RES         282
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   291 AA;  32953 MW;  A4747C5BD1679087 CRC64;
     MELLCCEVDT IGRAHLDRNL ITDRVLQTML KAEETSCPSM SYFKCVQKEI LPNMRKIVAT
     WMLEVCEEQK CEEEVFPLAM NYLDRFLSVE PLRKSWLQLL GATCMFLASK MKETIPLTAE
     KLCIYTDNSI RPDELLIMEL RVLNKLKWDL ASVTPHDFIE HFLNKMPLTE DTKQIIRKHA
     QTFVALCATD VNFISNPPSM IAAGSVAAAV QGLNLGNADS VFSTQRLTLF LSQVIKCDPD
     CLRACQEQIE SLLESSLRQA QQQHNASSDT KNMVDEVDIS CTPTDVRDVN I