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 28-MAR-2018, entry version 118.
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;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC Muroidea; Muridae; 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
RT project: 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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA 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
RT finger 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
RT Deltex2.";
RL Mol. Cell. Biol. 26:7358-7371(2006).
CC -!- FUNCTION: Functions as a ubiquitin ligase protein in vivo,
CC mediating 'Lys48'-linked polyubiquitination and promoting
CC degradation of TBK1, targeting to TBK1 requires interaction with
CC NLRP4 (By similarity). Regulator of Notch signaling, a signaling
CC pathway involved in cell-cell communications that regulates a
CC broad spectrum of cell-fate determinations. {ECO:0000250,
CC ECO:0000269|PubMed:16923970}.
CC -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
CC enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
CC conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
CC protein]-L-lysine. {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
CC fibroblasts and thymocytes. {ECO:0000269|PubMed:15684394,
CC ECO:0000269|PubMed:16923970}.
CC -!- DOMAIN: The WWE domains are thought to mediate some protein-
CC protein interaction, and are frequently found in ubiquitin
CC ligases. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Deltex family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39704.1; Type=Frameshift; Positions=266; Evidence={ECO:0000305};
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 UniGene; Mm.247695; -.
DR ProteinModelPortal; Q6PDK8; -.
DR SMR; Q6PDK8; -.
DR STRING; 10090.ENSMUSP00000040229; -.
DR iPTMnet; Q6PDK8; -.
DR PhosphoSitePlus; Q6PDK8; -.
DR MaxQB; Q6PDK8; -.
DR PaxDb; Q6PDK8; -.
DR PRIDE; Q6PDK8; -.
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 eggNOG; ENOG410IEMS; Eukaryota.
DR eggNOG; ENOG4111EY2; LUCA.
DR GeneTree; ENSGT00440000035370; -.
DR HOGENOM; HOG000007352; -.
DR HOVERGEN; HBG007213; -.
DR InParanoid; Q6PDK8; -.
DR KO; K06058; -.
DR OMA; PRICYLP; -.
DR OrthoDB; EOG091G04KU; -.
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 PRO; PR:Q6PDK8; -.
DR Proteomes; UP000000589; Chromosome 19.
DR Bgee; ENSMUSG00000039982; -.
DR CleanEx; MM_DTX4; -.
DR Genevisible; Q6PDK8; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.720.50; -; 2.
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 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 Complete proteome; Cytoplasm; Direct protein sequencing;
KW Metal-binding; Notch signaling pathway; Reference proteome; Repeat;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1 616 E3 ubiquitin-protein ligase DTX4.
FT /FTId=PRO_0000280556.
FT DOMAIN 1 78 WWE 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00248}.
FT DOMAIN 79 155 WWE 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00248}.
FT ZN_FING 406 465 RING-type; atypical.
FT {ECO:0000255|PROSITE-ProRule:PRU00175}.
FT CONFLICT 272 272 A -> T (in Ref. 1; AAH58647).
FT {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
//
