ID   CCND2_XENLA             Reviewed;         291 AA.
AC   P53782;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=G1/S-specific cyclin-D2;
GN   Name=ccnd2;
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.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9237366; DOI=10.1111/j.1768-322x.1996.tb00984.x;
RA   Taieb F., Jessus C.;
RT   "Xenopus cyclin D2: cloning and expression in oocytes and during early
RT   development.";
RL   Biol. Cell 88:99-111(1996).
CC   -!- FUNCTION: Regulatory component of the cyclin D2-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:P30279}.
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. {ECO:0000250|UniProtKB:P30279}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P30279}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P30279}. Nucleus membrane
CC       {ECO:0000250|UniProtKB:P30279}. Note=Cyclin D-CDK4 complexes accumulate
CC       at the nuclear membrane and are then translocated into the nucleus
CC       through interaction with KIP/CIP family members.
CC       {ECO:0000250|UniProtKB:P30279}.
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: ubiquitination is
CC       dependent on Thr-282 phosphorylation. The DCX(AMBRA1) complex
CC       represents the major regulator of CCND2 stability during the G1/S
CC       transition. {ECO:0000250|UniProtKB:P30280}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X89476; CAA61665.1; -; mRNA.
DR   EMBL; X83503; CAA58493.1; -; mRNA.
DR   PIR; S57925; S57925.
DR   RefSeq; NP_001079130.1; NM_001085661.1.
DR   AlphaFoldDB; P53782; -.
DR   SMR; P53782; -.
DR   PRIDE; P53782; -.
DR   GeneID; 373667; -.
DR   KEGG; xla:373667; -.
DR   CTD; 373667; -.
DR   Xenbase; XB-GENE-6252872; ccnd2.L.
DR   OMA; CLEMDTN; -.
DR   OrthoDB; 1234739at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 373667; Expressed in gastrula and 18 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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:SF66; PTHR10177:SF66; 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; 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; Membrane; Nucleus;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..291
FT                   /note="G1/S-specific cyclin-D2"
FT                   /id="PRO_0000080441"
FT   REGION          261..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         282
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P30280"
SQ   SEQUENCE   291 AA;  32959 MW;  9A290F04F1531E89 CRC64;
     MELLCCEGDT VRRAQPDPAL LLDDRVLHNL LTVEERYLPQ CSYFKCVQKD IQPFMRRMVA
     TWMLEVCEEQ RCEEEVFPMA MNYLDRFLAV IPTRKCHLQL LGAVCMFLAS KLKETIPLTA
     EKLCIYTDNS IKPQELLEWE LVVLGKLKWN LAAVTPHDFI EHILRKLPLP KDKLLLIRKH
     AQTFIALCAT DFNFAMYPPS MIATGSVGAA ICGLQLDVGE TSLSGDSLTE HLAKITSTDV
     DCLKACQEQI ESVLVSSLRQ TRQQTQQRNS SKSVDELDQA STPTDVQDIN L