ID   CCNE_HEMPU              Reviewed;         424 AA.
AC   O15995;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=G1/S-specific cyclin-E;
GN   Name=CYCE;
OS   Hemicentrotus pulcherrimus (Sea urchin) (Strongylocentrotus pulcherrimus).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC   Hemicentrotus.
OX   NCBI_TaxID=7650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9450391; DOI=10.2108/zsj.14.791;
RA   Kurokawa D., Akasaka K., Mitsunaga-Nakatsubo K., Shimada H.;
RT   "Cloning of cyclin E cDNA of the sea urchin, Hemicentrotus pulcherrimus.";
RL   Zool. Sci. 14:791-794(1997).
CC   -!- FUNCTION: Essential for the control of the cell cycle at the G1/S
CC       (start) transition.
CC   -!- SUBUNIT: Interacts with a member of the CDK2/CDK protein kinases to
CC       form a serine/threonine kinase holoenzyme complex. The cyclin subunit
CC       imparts substrate specificity to the complex (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin E subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB008363; BAA22990.1; -; mRNA.
DR   AlphaFoldDB; O15995; -.
DR   SMR; O15995; -.
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; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10177; PTHR10177; 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.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cyclin; Nucleus; Phosphoprotein.
FT   CHAIN           1..424
FT                   /note="G1/S-specific cyclin-E"
FT                   /id="PRO_0000080460"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         411
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   424 AA;  48417 MW;  02A90E8B50727F64 CRC64;
     MSRRSGRLQS RQDNQPLTEC ISDENNLPMC TRKRKTREQD TTGVSKAEEV QRRRQQFTIE
     NRWVPISESS SIETSLLVPM QTKEPSTPSE ELMDTANWVT FRNLFPAHVS DRASPIPLLH
     WDDLPEVWTI MTRKEALCPR KHDCLKSHPS LGERMRAILL DWLIEVCEVY RLHRESFYLA
     ADFVDRYLAA KENVPKTKLQ LIGITSLFVA AKLEEIYPPK LHEFAYVTDG ACTDDQILDQ
     ELIMLMTLNW DLTPITVNTW LNAFMQICNA EEIANRKTNF HFPSYSSTEF VQVAQLLDVC
     TLDIGSMDFD YSILAASALY HVTNEEVTLS VTGLKWDDIA ACVQWMSTFA MTIREVGVAQ
     LKNFKNIYAG DAHNIQTHCS SLELLDKSHE KQRLLREASC CSPVQVPGVL TPPQSDKKSK
     KGVL