CDCA3_MOUSE
ID CDCA3_MOUSE Reviewed; 266 AA.
AC Q99M54; O88837; Q8R2V1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Cell division cycle-associated protein 3;
DE AltName: Full=Gene-rich cluster protein C8;
DE AltName: Full=Trigger of mitotic entry protein 1;
DE Short=TOME-1;
GN Name=Cdca3; Synonyms=C8, Grcc8, Tome1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9445485;
RA Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M., Lu J.,
RA Gorrell J.H., Chinault A.C., Belmont J.W., Miller W., Gibbs R.A.;
RT "Comparative sequence analysis of a gene-rich cluster at human chromosome
RT 12p13 and its syntenic region in mouse chromosome 6.";
RL Genome Res. 8:29-40(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Small intestine, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 [5]
RP INTERACTION WITH SKP1.
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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-67, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-207 AND THR-210, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. {ECO:0000269|PubMed:12679038}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99M54-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99M54-2; Sequence=VSP_025606, VSP_025607;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27172.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK008606; BAB25773.1; -; mRNA.
DR EMBL; AK010409; BAB26916.1; -; mRNA.
DR EMBL; AK011313; BAB27539.1; -; mRNA.
DR EMBL; AK028159; BAC25785.1; -; mRNA.
DR EMBL; AK145537; BAE26492.1; -; mRNA.
DR EMBL; AK169792; BAE41370.1; -; mRNA.
DR EMBL; AC002397; AAC36014.1; -; Genomic_DNA.
DR EMBL; BC002006; AAH02006.1; -; mRNA.
DR EMBL; BC027172; AAH27172.1; ALT_INIT; mRNA.
DR CCDS; CCDS39629.1; -. [Q99M54-1]
DR RefSeq; NP_038566.1; NM_013538.5. [Q99M54-1]
DR RefSeq; XP_006505627.1; XM_006505564.3. [Q99M54-1]
DR RefSeq; XP_017176884.1; XM_017321395.1.
DR AlphaFoldDB; Q99M54; -.
DR STRING; 10090.ENSMUSP00000024270; -.
DR iPTMnet; Q99M54; -.
DR PhosphoSitePlus; Q99M54; -.
DR EPD; Q99M54; -.
DR jPOST; Q99M54; -.
DR MaxQB; Q99M54; -.
DR PaxDb; Q99M54; -.
DR PeptideAtlas; Q99M54; -.
DR PRIDE; Q99M54; -.
DR ProteomicsDB; 281141; -. [Q99M54-1]
DR ProteomicsDB; 281142; -. [Q99M54-2]
DR Antibodypedia; 11223; 202 antibodies from 33 providers.
DR DNASU; 14793; -.
DR Ensembl; ENSMUST00000024270; ENSMUSP00000024270; ENSMUSG00000023505. [Q99M54-1]
DR GeneID; 14793; -.
DR KEGG; mmu:14793; -.
DR UCSC; uc009dsc.2; mouse. [Q99M54-1]
DR CTD; 83461; -.
DR MGI; MGI:1315198; Cdca3.
DR VEuPathDB; HostDB:ENSMUSG00000023505; -.
DR eggNOG; ENOG502S7V2; Eukaryota.
DR GeneTree; ENSGT00390000017343; -.
DR HOGENOM; CLU_091723_0_0_1; -.
DR InParanoid; Q99M54; -.
DR OMA; GHNKENQ; -.
DR OrthoDB; 1398970at2759; -.
DR PhylomeDB; Q99M54; -.
DR TreeFam; TF101068; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 14793; 10 hits in 74 CRISPR screens.
DR ChiTaRS; Cdca3; mouse.
DR PRO; PR:Q99M54; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q99M54; protein.
DR Bgee; ENSMUSG00000023505; Expressed in ventricular zone and 198 other tissues.
DR ExpressionAtlas; Q99M54; baseline and differential.
DR Genevisible; Q99M54; MM.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
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 Alternative splicing; Cell cycle; Cell division; Cytoplasm; Mitosis;
KW Phosphoprotein; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..266
FT /note="Cell division cycle-associated protein 3"
FT /id="PRO_0000287709"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..119
FT /note="F-box-like"
FT REGION 120..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 256..258
FT /note="KEN box"
FT COMPBIAS 33..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
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:0007744|PubMed:19144319"
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 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 200
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99618"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 210
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 83..84
FT /note="DP -> GK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025606"
FT VAR_SEQ 85..266
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025607"
FT CONFLICT 119
FT /note="Y -> S (in Ref. 4; AAH02006)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="D -> G (in Ref. 4; AAH02006)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 266 AA; 28708 MW; 8E02E77ACAAAC2F8 CRC64;
MGSTQSVSGT PARPLPRNKQ VARVADPRSP SAGIQRTPIQ VESSPQPSLP AEQLNGLKQA
QDPDPRSPTL GIARTPMKIS GPDPQCSLVK ELSEVLETEA SESISSPELA LPRETPLFYD
LDLSSDPQLS PEDQLLPWSQ AELDPKQVFT KEEAKQSAET IAASQNSDKP SRDPETPQSS
GSKRSRRKAN SKVLGRSPLT ILQDDNSPGT LTLRQGKRPS ALSENVKDLK EGVVLGTGRF
LKAGGGAREP NQDHDKENQH FALLES
