ID Q9PVT7_CARAU Unreviewed; 410 AA.
AC Q9PVT7;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Cyclin E {ECO:0000313|EMBL:BAA85846.1};
OS Carassius auratus (Goldfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Carassius.
OX NCBI_TaxID=7957 {ECO:0000313|EMBL:BAA85846.1};
RN [1] {ECO:0000313|EMBL:BAA85846.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10910135; DOI=10.1046/j.1440-169x.2000.00506.x;
RA Yoshida N., Yamashita M.;
RT "Non-dependence of cyclin E/Cdk2 kinase activity on the initiation of
RT oocyte maturation in goldfish.";
RL Dev. Growth Differ. 42:285-294(2000).
CC -!- FUNCTION: Essential for the control of the cell cycle at the G1/S
CC (start) transition. {ECO:0000256|ARBA:ARBA00037610}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin E subfamily.
CC {ECO:0000256|ARBA:ARBA00007143}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB026627; BAA85846.1; -; mRNA.
DR AlphaFoldDB; Q9PVT7; -.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd20579; CYCLIN_CCNE1_rpt1; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR048258; Cyclins_cyclin-box.
DR PANTHER; PTHR10177; CYCLINS; 1.
DR PANTHER; PTHR10177:SF71; G1_S-SPECIFIC CYCLIN-E1; 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; Cyclin-like; 2.
DR PROSITE; PS00292; CYCLINS; 1.
PE 2: Evidence at transcript level;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383}.
FT DOMAIN 152..237
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 246..368
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 410 AA; 46655 MW; 6D847CD93B15E663 CRC64;
MPSKKVLRTE QFNTTDEAPK TMSVRPRKRK ADVAIHLQDP DEEISEMTRK KPCASQACWN
PDTGYTSPCR RIPTPDEVEE PVAVGSVGFA QYASENIFVT PTRSTPLPAL CWASRDDVWN
NLLRKDKLYL RDTHVMERHP HLQPKMRAIL LDWLIEVCEV YKLHRETFYL GQDYFDRFMA
TQENVLKTTL QLIGISCLFI AAKMEEIYPP KVHQFAYVTD GACTEDDILS MEIIIMKELD
WSLSPLTPVA WLNIYMQMAY LKETAQVLVA QYPQATFVQI AELLDLCILD ARSLEFSYSL
LAASALFHFS SLELVMKVSG LKWCDLEECV RWMVPFAMSI REAGSSSLKT FKGIAADDLH
NIQTHVPYME WLGRVNSYQP VDIESSQTSP VPSGVLTPPP SSEKPESEVS
//