DTX4_MOUSE
ID DTX4_MOUSE Reviewed; 616 AA.
AC Q6PDK8; Q6IS30; Q8BID3;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=E3 ubiquitin-protein ligase DTX4;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q61010};
DE AltName: Full=Protein deltex-4;
DE Short=Deltex4;
DE AltName: Full=RING-type E3 ubiquitin transferase DTX4 {ECO:0000305};
GN Name=Dtx4;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 219-616.
RC STRAIN=C57BL/6J; TISSUE=Head;
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 PROTEIN SEQUENCE OF 365-374, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=15684394; DOI=10.1128/mcb.25.4.1437-1445.2005;
RA Storck S., Delbos F., Stadler N., Thirion-Delalande C., Bernex F.,
RA Verthuy C., Ferrier P., Weill J.-C., Reynaud C.-A.;
RT "Normal immune system development in mice lacking the Deltex-1 RING finger
RT domain.";
RL Mol. Cell. Biol. 25:1437-1445(2005).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16923970; DOI=10.1128/mcb.00149-06;
RA Lehar S.M., Bevan M.J.;
RT "T cells develop normally in the absence of both Deltex1 and Deltex2.";
RL Mol. Cell. Biol. 26:7358-7371(2006).
CC -!- FUNCTION: Functions as a ubiquitin ligase protein in vivo, mediating
CC 'Lys48'-linked polyubiquitination and promoting degradation of TBK1,
CC targeting to TBK1 requires interaction with NLRP4 (By similarity).
CC Regulator of Notch signaling, a signaling pathway involved in cell-cell
CC communications that regulates a broad spectrum of cell-fate
CC determinations. {ECO:0000250, ECO:0000269|PubMed:16923970}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q61010};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with NLRP4. {ECO:0000250|UniProtKB:Q9Y2E6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, testis, embryonic fibroblasts
CC and thymocytes. {ECO:0000269|PubMed:15684394,
CC ECO:0000269|PubMed:16923970}.
CC -!- DOMAIN: The WWE domains are thought to mediate some protein-protein
CC interaction, and are frequently found in ubiquitin ligases.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Deltex family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39704.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC058647; AAH58647.1; -; mRNA.
DR EMBL; BC069975; AAH69975.1; -; mRNA.
DR EMBL; AK086624; BAC39704.1; ALT_FRAME; mRNA.
DR CCDS; CCDS29631.1; -.
DR RefSeq; NP_766030.3; NM_172442.3.
DR AlphaFoldDB; Q6PDK8; -.
DR SMR; Q6PDK8; -.
DR BioGRID; 228902; 2.
DR STRING; 10090.ENSMUSP00000040229; -.
DR iPTMnet; Q6PDK8; -.
DR PhosphoSitePlus; Q6PDK8; -.
DR MaxQB; Q6PDK8; -.
DR PaxDb; Q6PDK8; -.
DR PRIDE; Q6PDK8; -.
DR ProteomicsDB; 277527; -.
DR Antibodypedia; 52744; 136 antibodies from 23 providers.
DR DNASU; 207521; -.
DR Ensembl; ENSMUST00000045521; ENSMUSP00000040229; ENSMUSG00000039982.
DR GeneID; 207521; -.
DR KEGG; mmu:207521; -.
DR UCSC; uc008guc.2; mouse.
DR CTD; 23220; -.
DR MGI; MGI:2672905; Dtx4.
DR VEuPathDB; HostDB:ENSMUSG00000039982; -.
DR eggNOG; ENOG502QQ9M; Eukaryota.
DR GeneTree; ENSGT00940000157122; -.
DR HOGENOM; CLU_030422_4_0_1; -.
DR InParanoid; Q6PDK8; -.
DR OMA; EKQHPWV; -.
DR OrthoDB; 600021at2759; -.
DR PhylomeDB; Q6PDK8; -.
DR TreeFam; TF325526; -.
DR Reactome; R-MMU-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
DR Reactome; R-MMU-3134975; Regulation of innate immune responses to cytosolic DNA.
DR Reactome; R-MMU-3270619; IRF3-mediated induction of type I IFN.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 207521; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q6PDK8; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q6PDK8; protein.
DR Bgee; ENSMUSG00000039982; Expressed in floor plate of midbrain and 219 other tissues.
DR Genevisible; Q6PDK8; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007219; P:Notch signaling pathway; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd09633; Deltex_C; 1.
DR Gene3D; 3.30.390.130; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.720.50; -; 2.
DR InterPro; IPR039396; Deltex_C.
DR InterPro; IPR039399; Deltex_C_sf.
DR InterPro; IPR039398; Deltex_fam.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR018123; WWE-dom_subgr.
DR InterPro; IPR037197; WWE_dom_sf.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12622; PTHR12622; 1.
DR Pfam; PF18102; DTC; 1.
DR Pfam; PF02825; WWE; 2.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00678; WWE; 2.
DR SUPFAM; SSF117839; SSF117839; 2.
DR PROSITE; PS50918; WWE; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Metal-binding;
KW Notch signaling pathway; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..616
FT /note="E3 ubiquitin-protein ligase DTX4"
FT /id="PRO_0000280556"
FT DOMAIN 1..78
FT /note="WWE 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT DOMAIN 79..155
FT /note="WWE 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT ZN_FING 406..465
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 223..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 272
FT /note="A -> T (in Ref. 1; AAH58647)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 616 AA; 66821 MW; 84361BC9A52F6D69 CRC64;
MLLASAVVVW EWLNEHGRWR PYSPAVSHHI EAVVRAGPRA GGSVVLGQVD SRLAPYIIDL
QSMNQFRQDT GTLRPVRRNY YDPSSAPGKG VVWEWENDNG SWTPYDMEVG ITIQYAYEKQ
HPWIDLTSIG FSYIIDFSTM GQINRQTQRQ RRVRRRLDLI YPMVTGTMPK TQSWPVSPGP
ATSSPAPPCS CPQCVLVMSV KAAVVHGGTG PPAVRKNMAL SGVGKLPQPP GPGAKPLDTT
GTIRGPGKTA PSQVIRRQVS NAPAGATVGS PASPQGSNRK TGRVALATLN RSNLQRLAIA
QSRVLIASGV PTVPVKNLNG SSPVNPALAG ITGILMSAAG LPVCLTRPPK LVLHPPPVSK
SEIKSIPGVS NTSRKTTKKQ AKKGKTPEEV LKKYLQKVRH PPEEDCTICM ERLTAPSGYK
GPQPTVKPDL VGKLSRCGHI YHIYCLVAMY NNGNKDGSLQ CPTCKTIYGV KTGTQPPGKM
EYHLIPHSLP GHPDCKTIRI IYSIPPGIQG PEHPNPGKSF SARGFPRHCY LPDSEKGRKV
LKLLLVAWDR RLIFAIGTSS TTGESDTVIW NEVHHKTEFG SNLTGHGYPD ANYLDNVLAE
LAAQGISEDS TSHEKD
