ID   CCND3_BOVIN             Reviewed;         292 AA.
AC   Q3MHH5;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=G1/S-specific cyclin-D3;
GN   Name=CCND3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulatory component of the cyclin D3-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. Component of the ternary
CC       complex, cyclin D3/CDK4/CDKN1B, required for nuclear translocation and
CC       activity of the cyclin D-CDK4 complex. Shows transcriptional
CC       coactivator activity with ATF5 independently of CDK4.
CC       {ECO:0000250|UniProtKB:P30281}.
CC   -!- SUBUNIT: Interacts with the CDK4 and CDK6 protein kinases to form a
CC       serine/threonine kinase holoenzyme complex. The cyclin subunit imparts
CC       substrate specificity to the complex. Interacts with ATF5. Interacts
CC       with EIF3K. Component of the ternary complex cyclin D/CDK4/CDKN1B
CC       required for nuclear translocation and modulation of CDK4-mediated
CC       kinase activity. Can form similar complexes with either CDKN1A or
CC       CDKN2A. {ECO:0000250|UniProtKB:P30281}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P30281}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P30281}.
CC   -!- PTM: Phosphorylation at Thr-283 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: ubiquitination is
CC       dependent on Thr-283 phosphorylation. The DCX(AMBRA1) complex
CC       represents the major regulator of CCND3 stability during the G1/S
CC       transition (By similarity). Polyubiquitinated by the SCF(FBXL2)
CC       complex, leading to proteasomal degradation (By similarity).
CC       {ECO:0000250|UniProtKB:P30281, ECO:0000250|UniProtKB:P30282}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC105236; AAI05237.1; -; mRNA.
DR   RefSeq; NP_001029881.1; NM_001034709.2.
DR   AlphaFoldDB; Q3MHH5; -.
DR   SMR; Q3MHH5; -.
DR   STRING; 9913.ENSBTAP00000035894; -.
DR   PaxDb; Q3MHH5; -.
DR   PRIDE; Q3MHH5; -.
DR   GeneID; 540547; -.
DR   KEGG; bta:540547; -.
DR   CTD; 896; -.
DR   eggNOG; KOG0656; Eukaryota.
DR   InParanoid; Q3MHH5; -.
DR   OrthoDB; 1234739at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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; 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:SF65; PTHR10177:SF65; 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   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cyclin; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..292
FT                   /note="G1/S-specific cyclin-D3"
FT                   /id="PRO_0000236254"
FT   DOMAIN          27..152
FT                   /note="Cyclin N-terminal"
FT   REGION          255..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..292
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         264
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P30282"
FT   MOD_RES         279
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P30281"
FT   MOD_RES         283
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P24385"
SQ   SEQUENCE   292 AA;  32436 MW;  0D0F02A6054B4518 CRC64;
     MELLCCEGTR HAPRAGPDPR LLGDQRVLQS LLRLEERYVP RASYFQCVQR EIKPHMRKML
     AYWMLEVCEE QRCEEEVFPL AMNYLDRYLS CVPTRKAQLQ LLGAVCMLLA SKLRETTPLT
     IEKLCIYTDH SVSPRQLRDW EVLVLGKLKW DLAAVIAHDF LALILHRLSL PRDRQALVKK
     HAQTFLALCA TDYTFAMYPP SMIATGSIGA AVQGLGACST SGDELTELLA GIAGTEVDCL
     RACQEQIEAA LRESLREAAQ TSPSPAPKAP RGSSSQGPSQ TSTPTDVTAI HL