ID   CCNE3_XENLA             Reviewed;         408 AA.
AC   O42575; Q5EAX0;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=G1/S-specific cyclin-E3;
GN   Name=cyce3;
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].
RC   TISSUE=Egg;
RX   PubMed=8799808; DOI=10.1242/jcs.109.6.1173;
RA   Chevalier S., Couturier A., Chartrain I., le Guellec R., Beckhelling C.,
RA   le Guellec K., Philippe M., Ford C.C.;
RT   "Xenopus cyclin E, a nuclear phosphoprotein, accumulates when oocytes gain
RT   the ability to initiate DNA replication.";
RL   J. Cell Sci. 109:1173-1184(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential for the control of the cell cycle at the G1/S
CC       (start) transition.
CC   -!- SUBUNIT: Interacts with CDK2 protein kinase to form a serine/threonine
CC       kinase holoenzyme complex. The cyclin subunit imparts substrate
CC       specificity to the complex. {ECO:0000250|UniProtKB:P24864}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P24864}.
CC   -!- PTM: Phosphorylation by CDK2 triggers its release from CDK2 and
CC       degradation via the ubiquitin proteasome pathway.
CC       {ECO:0000250|UniProtKB:P24864}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin E subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L43513; AAA99425.1; -; mRNA.
DR   EMBL; BC090214; AAH90214.1; -; mRNA.
DR   RefSeq; NP_001081446.1; NM_001087977.1.
DR   AlphaFoldDB; O42575; -.
DR   SMR; O42575; -.
DR   BioGRID; 99180; 7.
DR   GeneID; 397841; -.
DR   KEGG; xla:397841; -.
DR   CTD; 397841; -.
DR   Xenbase; XB-GENE-972047; ccne1.S.
DR   OrthoDB; 993640at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 397841; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:InterPro.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
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; IPR028858; Cyclin_E.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10177; PTHR10177; 1.
DR   PANTHER; PTHR10177:SF71; PTHR10177:SF71; 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; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..408
FT                   /note="G1/S-specific cyclin-E3"
FT                   /id="PRO_0000080456"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          66..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         394
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P24864"
SQ   SEQUENCE   408 AA;  47204 MW;  49F1E2868A9EAE1C CRC64;
     MPVIRNPAAE KSTKDERTAS CTVRSRKRKA DVAIFLQDPD DTLDCLEMTK KKQYQDRGQL
     SNEMTCKSPH KLIPTPEKEE HEPNPTSYPH FASLRFSPVS ASPLPRLGWA NQDDVWRNML
     NKDRIYLRDK NFFEKHPQLQ PNMRAILLDW LMEVCEVYKL HRETFYLAQD FFDRFMATQK
     NVIKSRLQLI GITSLFIAAK MEEIYPPKLH QFAFITDCAC TEDEITSMEL IIMKDLDWCL
     SPMTMVSWFN VFLQVAYIRE LQHFLRPQFP QEVYIQIVQL LDLCVLDICC LDYPYGVLAA
     SALYHFSCPE LMEKVSGFKL TELQGCIKWL VPFAMAIKDG GKSKLKFFKG VDIEDVHNIQ
     THTGCLELME KVHINRAVLE EQNRASPIPS GVLTPPQSDK KQKSDPAD