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UniProtKB/Swiss-Prot entry Q9JHI5


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IVD_MOUSE
Primary accession number Q9JHI5
Secondary accession numbers Q9CYI3 Q9DBD7
Integrated into Swiss-Prot on May 24, 2005
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 64)
Name and origin of the protein
Protein name Isovaleryl-CoA dehydrogenase, mitochondrial [Precursor]
Synonyms IVD
EC 1.3.99.10
Gene name
Name: Ivd
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=129/Ola;
DOI=10.1016/S0378-1119(01)00466-8; PubMed=11404023 [NCBI, ExPASy, EBI, Israel, Japan]
Willard J.M., Reinard T., Mohsen A.W., Vockley J.;
"Cloning of genomic and cDNA for mouse isovaleryl-CoA dehydrogenase (IVD) and evolutionary comparison to other known IVDs.";
Gene 270:253-257(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Liver;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Kidney, and Salivary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 57-76; 154-178; 212-221; 231-239; 273-285; 339-346; 400-411 AND 418-424, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[5]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-76, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan]
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.";
Mol. Cell 23:607-618(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF225989; AAF35888.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF226043; AAF67667.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF226039; AAF67667.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF226041; AAF67667.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF226040; AAF67667.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF226042; AAF67667.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK005024; BAB23751.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK017660; BAB30859.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018325; AAH18325.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027198; AAH27198.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_062800.1; -.
UniGene Mm.6635
3D structure databases
HSSP P26440; 1IVH. [HSSP ENTRY / PDB]
SMR Q9JHI5; 36-422.
ModBase Q9JHI5.
2D gel databases
REPRODUCTION-2DPAGE Q9JHI5; -.
Organism-specific databases
MGI MGI:1929242; Ivd.
Gene expression databases
ArrayExpress Q9JHI5; -.
CleanEx MM_IVD; -.
GermOnline ENSMUSG00000027332; Mus musculus.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR006091; Acyl-CoA_DHase/Oxase_M.
IPR006089; Acyl-CoA_DHase_CS.
IPR006092; Acyl-CoA_DHase_N.
IPR006090; Acyl-CoA_Oxase/DHase_1.
IPR013786; AcylCoA_DH/ox_N.
IPR013764; AcylCoA_oxidase/DH_1/2_C.
Graphical view of domain structure.
Gene3D G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1.
G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1.
G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 1.
Pfam PF00441; Acyl-CoA_dh_1; 1.
PF02770; Acyl-CoA_dh_M; 1.
PF02771; Acyl-CoA_dh_N; 1.
Pfam graphical view of domain structure.
PROSITE PS00072; ACYL_COA_DH_1; 1.
PS00073; ACYL_COA_DH_2; 1.
BLOCKS Q9JHI5.
Genome annotation databases
Ensembl ENSMUSG00000027332; Mus musculus. [Contig view]
GeneID 56357; -.
KEGG mmu:56357; -.
NMPDR fig|10090.3.peg.6671; -.
Phylogenomic databases
HOGENOM Q9JHI5; -.
HOVERGEN Q9JHI5; -.
Other
SOURCE Ivd; Mus musculus.
ProtoNet Q9JHI5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Direct protein sequencing; FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    30  30     Mitochondrion (By similarity). 
CHAIN   31   424  394     Isovaleryl-CoA dehydrogenase, mitochondrial. PRO_0000000532
ACT_SITE   284   284        Proton acceptor (By similarity). 
MOD_RES   76    76        N6-acetyllysine. 
CONFLICT   29    29        R -> G (in Ref. 2; BAB23751). 
CONFLICT   41    41        N -> K (in Ref. 2; BAB30859). 
Sequence information
Length: 424 AA [This is the length of the unprocessed precursor] Molecular weight: 46325 Da [This is the MW of the unprocessed precursor] CRC64: 7B8A556A9E73B0B6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATAIRLLGR RVSSWRLRPS PSPLAVPRRA HSILPVDDDI NGLNEEQKQL RHTISKFLQE 

        70         80         90        100        110        120 
NLAPKAQEID QTNDFKNLRE FWKQLGSLGV LGITAPVQYG GSGLGYLEHV LVMEEISRAS 

       130        140        150        160        170        180 
GAVGLSYGAH SNLCVNQIVR NGNEAQKEKY LPKLISGEFI GALAMSEPNA GSDVVSMKLK 

       190        200        210        220        230        240 
AEKKGDHYVL NGNKFWITNG PDADILVVYA KTDLTAVPAS RGITAFIVEK GMPGFSTSKK 

       250        260        270        280        290        300 
LDKLGMRGSN TCELVFEDCK VPAANVLSQE SKGVYVLMSG LDLERLVLAG GPLGIMQAVL 

       310        320        330        340        350        360 
DHTIPYLHVR EAFGQKIGQF QLMQGKMADM YTRLMASRQY VYNVAKACDE GHIIPKDCAG 

       370        380        390        400        410        420 
VILYAAECAT QVALDGIQCL GGNGYINDFP MGRFLRDAKL YEIGAGTSEV RRLVIGRAFN 


ADFR 

Q9JHI5 in FASTA format

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