CDCA3_RAT
ID CDCA3_RAT Reviewed; 273 AA.
AC Q68FW2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with SKP1. Part of a SCF (SKP1-cullin-F-box) protein
CC ligase complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC -!- DOMAIN: The KEN box is required for the association with the APC/C-Cdh1
CC complex. {ECO:0000250}.
CC -!- PTM: Ubiquitinated and degraded by the APC/C-Cdh1 complex.
CC {ECO:0000250}.
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DR EMBL; BC079204; AAH79204.1; -; mRNA.
DR RefSeq; NP_001007649.1; NM_001007648.1.
DR RefSeq; XP_006237403.1; XM_006237341.2.
DR RefSeq; XP_017448079.1; XM_017592590.1.
DR AlphaFoldDB; Q68FW2; -.
DR STRING; 10116.ENSRNOP00000020803; -.
DR iPTMnet; Q68FW2; -.
DR PhosphoSitePlus; Q68FW2; -.
DR PaxDb; Q68FW2; -.
DR PRIDE; Q68FW2; -.
DR Ensembl; ENSRNOT00000020803; ENSRNOP00000020803; ENSRNOG00000015529.
DR GeneID; 297594; -.
DR KEGG; rno:297594; -.
DR UCSC; RGD:1359093; rat.
DR CTD; 83461; -.
DR RGD; 1359093; Cdca3.
DR eggNOG; ENOG502S7V2; Eukaryota.
DR GeneTree; ENSGT00390000017343; -.
DR HOGENOM; CLU_091723_0_0_1; -.
DR InParanoid; Q68FW2; -.
DR OMA; GHNKENQ; -.
DR OrthoDB; 1398970at2759; -.
DR PhylomeDB; Q68FW2; -.
DR TreeFam; TF101068; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q68FW2; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000015529; Expressed in testis and 17 other tissues.
DR Genevisible; Q68FW2; RN.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
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..273
FT /note="Cell division cycle-associated protein 3"
FT /id="PRO_0000287710"
FT REGION 1..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..124
FT /note="F-box-like"
FT REGION 251..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 263..265
FT /note="KEN box"
FT COMPBIAS 33..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99618"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99618"
FT MOD_RES 37
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99618"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99618"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99618"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99618"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99618"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99618"
FT MOD_RES 207
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99618"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 217
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99M54"
SQ SEQUENCE 273 AA; 29611 MW; 2EB02AE5CFDFBDE1 CRC64;
MGSTQSVSGT PARPLPRNKH VSRVADPRSP SAGIQRTPIQ VESSPQPNPP AEQLNSLKQA
QDPDPRSPTL GIARTPMKIS GPDSQCPLVK ELSEVFETEV SETEVSESIS SPVLGLPQET
PLSSELDLPP DPDPQVSLED QLLPWSQTEL NSKQVFAKEE AKQSTETMVS GQTSDKPSRD
PETPQSSGSK RSRRKTNNKV LGRSPLTILQ DDNSPGTLTL RQGKRPSALS ENVKDLKEGV
ILGTGRFLKA GGGAWEQNED HDKENQHFAL MES
