ID MUL1_MOUSE Reviewed; 352 AA. AC Q8VCM5; A2AM82; A2AM84; B5M498; Q3TDK4; Q8BHF2; Q9DCV9; DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 2. DT 22-SEP-2009, entry version 61. DE RecName: Full=Mitochondrial ubiquitin ligase activator of NFKB 1; DE EC=6.3.2.-; DE AltName: Full=E3 ubiquitin-protein ligase MUL1; DE AltName: Full=Growth inhibition and death E3 ligase; GN Name=Mul1; Synonyms=Gide; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=18591963; DOI=10.1038/cr.2008.75; RA Zhang B., Huang J., Li H.-L., Liu T., Wang Y.-Y., Waterman P., RA Mao A.-P., Xu L.-G., Zhai Z., Liu D., Marrack P., Shu H.-B.; RT "GIDE is a mitochondrial E3 ubiquitin ligase that induces apoptosis RT and slows growth."; RL Cell Res. 18:900-910(2008). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Brain cortex, Head, Kidney, Liver, 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., 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 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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Liver; 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). CC -!- FUNCTION: E3 ubiquitin-protein ligase that plays a role in the CC control of mitochondrial morphology. Promotes mitochondrial CC fragmentation and influences mitochondrial localization. Inhibits CC cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 CC and induces caspase-dependent apoptosis. E3 ubiquitin ligases CC accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the CC form of a thioester and then directly transfer the ubiquitin to CC targeted substrates (By similarity). CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Homooligomer. Interacts with MAP3K7/TAK1 (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass CC membrane protein (By similarity). Peroxisome (By similarity). CC Note=Transported in mitochondrion-derived vesicles from the CC mitochondrion to the peroxisome (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8VCM5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8VCM5-2; Sequence=VSP_034454, VSP_034455; CC Note=Gene prediction based on EST data; CC Name=3; CC IsoId=Q8VCM5-3; Sequence=VSP_034453; CC Note=Gene prediction based on EST data; CC -!- DOMAIN: The zinc finger domain is required for E3 ligase activity CC (By similarity). CC -!- SIMILARITY: Contains 1 RING-type zinc finger. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EU935009; ACH72646.1; -; mRNA. DR EMBL; AK002416; BAB22084.1; -; mRNA. DR EMBL; AK044088; BAC31768.1; -; mRNA. DR EMBL; AK076419; BAC36332.1; -; mRNA. DR EMBL; AK083295; BAC38848.1; -; mRNA. DR EMBL; AK153956; BAE32279.1; -; mRNA. DR EMBL; AK170149; BAE41597.1; -; mRNA. DR EMBL; AL807249; CAM18879.1; -; Genomic_DNA. DR EMBL; AL807249; CAM18880.1; -; Genomic_DNA. DR EMBL; AL807249; CAM18881.1; -; Genomic_DNA. DR EMBL; BC019516; AAH19516.1; -; mRNA. DR IPI; IPI00308263; -. DR IPI; IPI00649455; -. DR IPI; IPI00649724; -. DR RefSeq; NP_080965.2; -. DR RefSeq; XP_001479685.1; -. DR UniGene; Mm.103413; -. DR HSSP; P38398; 1JM7. DR STRING; Q8VCM5; -. DR PRIDE; Q8VCM5; -. DR Ensembl; ENSMUST00000044058; ENSMUSP00000039604; ENSMUSG00000041241; Mus musculus. DR Ensembl; ENSMUST00000105814; ENSMUSP00000101440; ENSMUSG00000041241; Mus musculus. DR GeneID; 68350; -. DR KEGG; mmu:100048020; -. DR KEGG; mmu:68350; -. DR UCSC; uc008vky.1; mouse. DR CTD; 68350; -. DR MGI; MGI:1915600; Mul1. DR HOVERGEN; Q8VCM5; -. DR OMA; Q8VCM5; VIGHYIS. DR NextBio; 461442; -. DR ArrayExpress; Q8VCM5; -. DR Bgee; Q8VCM5; -. DR GO; GO:0031307; C:integral to mitochondrial outer membrane; ISS:UniProtKB. DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB. DR GO; GO:0004871; F:signal transducer activity; ISS:UniProtKB. DR GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006919; P:activation of caspase activity; ISS:UniProtKB. DR GO; GO:0007257; P:activation of JUN kinase activity; ISS:UniProtKB. DR GO; GO:0006917; P:induction of apoptosis; ISS:UniProtKB. DR GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB. DR GO; GO:0051646; P:mitochondrion localization; ISS:UniProtKB. DR GO; GO:0019941; P:modification-dependent protein catabolic pr...; IEA:UniProtKB-KW. DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB. DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-k...; ISS:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR017907; Znf_RING_CS. DR SMART; SM00184; RING; 1. DR PROSITE; PS00518; ZF_RING_1; FALSE_NEG. DR PROSITE; PS50089; ZF_RING_2; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Apoptosis; Ligase; Membrane; Metal-binding; KW Mitochondrion; Mitochondrion outer membrane; Peroxisome; KW Transmembrane; Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1 352 Mitochondrial ubiquitin ligase activator FT of NFKB 1. FT /FTId=PRO_0000277662. FT TOPO_DOM 1 8 Cytoplasmic (Potential). FT TRANSMEM 9 29 Potential. FT TOPO_DOM 30 238 Mitochondrial intermembrane (Potential). FT TRANSMEM 239 259 Potential. FT TOPO_DOM 260 352 Cytoplasmic (Potential). FT ZN_FING 302 340 RING-type. FT VAR_SEQ 1 40 MESGSRPSLGQVILLGTSSMVTAVLYSIYRQKAQVAQELK FT -> MVVVLCWLEFHSPSAKDLFWQLYGRWTLEPKSYHQ FT (in isoform 3). FT /FTId=VSP_034453. FT VAR_SEQ 111 123 NDYSKIIHQRTNT -> CVSSGFYTSEVVV (in FT isoform 2). FT /FTId=VSP_034454. FT VAR_SEQ 124 352 Missing (in isoform 2). FT /FTId=VSP_034455. FT CONFLICT 38 38 E -> V (in Ref. 2; BAE41597). FT CONFLICT 208 208 V -> F (in Ref. 2; BAB22084). FT CONFLICT 242 242 I -> V (in Ref. 1; ACH72646 and 4; FT AAH19516). SQ SEQUENCE 352 AA; 39835 MW; 252530F1BD917871 CRC64; MESGSRPSLG QVILLGTSSM VTAVLYSIYR QKAQVAQELK GAKKIHLGED LKGILSEAPG KCVPYAVIEG AVRSVKETLN SQFVENCKGV IQRLSLQEHK MVWNRTTHLW NDYSKIIHQR TNTVPFDLVP HEDGVAVSVR VLKPLDSVDL GLETVYEKFH PSVQSFTDAI GHYISGERPK GIQETEEMLK VGATLTGIGE LVLDNNAVRL QPPKQGMQYY LSSQDFDSLL HRQESSVRLW KILVLVFGFA TCATLFFILR KQYLHRQERL RQQQLQEEFL EHEAQLLSQA SPEDRESLKS ACVVCLSNFK SCVFLECGHV CSCRQCYLAL PEPKRCPICR REITRVIPLY NS //