CDCA3_XENLA
ID CDCA3_XENLA Reviewed; 363 AA.
AC P0C2X8;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Cell division cycle-associated protein 3;
DE AltName: Full=Trigger of mitotic entry protein 1;
DE Short=TOME-1;
GN Name=cdca3; Synonyms=tome1;
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], FUNCTION, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION, UBIQUITINATION, DEVELOPMENTAL STAGE, AND INTERACTION WITH
RP WEE1.
RX PubMed=12679038; DOI=10.1016/s0092-8674(03)00232-0;
RA Ayad N.G., Rankin S., Murakami M., Jebanathirajah J., Gygi S.P.,
RA Kirschner M.W.;
RT "Tome-1, a trigger of mitotic entry, is degraded during G1 via the APC.";
RL Cell 113:101-113(2003).
CC -!- FUNCTION: F-box-like protein which is required for entry into mitosis.
CC Acts by participating in E3 ligase complexes that mediate the
CC ubiquitination and degradation of WEE1 kinase at G2/M phase.
CC {ECO:0000269|PubMed:12679038}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with wee1, when wee1 is phosphorylated at 'Ser-38'.
CC {ECO:0000269|PubMed:12679038}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12679038}.
CC -!- DEVELOPMENTAL STAGE: Present at high level in G2 and M phases but
CC declines rapidly in G2 phase (at protein level).
CC {ECO:0000269|PubMed:12679038}.
CC -!- DOMAIN: The KEN box is required for the association with the APC/C-Cdh1
CC complex.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:12679038}.
CC -!- PTM: Ubiquitinated and degraded by the APC/C-Cdh1 complex during G1
CC phase. {ECO:0000269|PubMed:12679038}.
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DR AlphaFoldDB; P0C2X8; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR InterPro; IPR038832; CDCA3.
DR PANTHER; PTHR34756; PTHR34756; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Mitosis; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..363
FT /note="Cell division cycle-associated protein 3"
FT /id="PRO_0000287711"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..152
FT /note="F-box-like"
FT REGION 126..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 353..355
FT /note="KEN box"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 363 AA; 39702 MW; 9BE5780A53A622FD CRC64;
MGSAESKAQV TPSRPLRNHL LSRVNDPRSP TSGIPRTPIE VGESPRNTPQ TVKEEEEEIP
DSPEIFDPRS PTNGITRTPL RPPIHAVLNN LAKQLSEVFV AEDSSTEGGP LGFTGPEATN
LERQVVESQT APPAGEHVND HEVEPSVEKA ETQIDLEVCP GVEKVKSPIA EMLETLNDQE
ESPIAETLET MNDQEESPIA ETMNDQEESP IAETLENLND QAESPIAETL ENLNDQAESP
IAEMLDTLND QEPVAVAQSV VSTESTQATG QQQKTRGKSP RSSGVKNVRQ RPRKALLSSS
SGRSPLRILQ EDNSPNTNTQ HRQAKKLSFQ SEPALPHRAL KISHPNWESS LNKENAEYGH
SNS