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UniProtKB/Swiss-Prot entry P12007


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

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Entry information
Entry name IVD_RAT
Primary accession number P12007
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1989
Sequence was last modified on April 1, 1990 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 82)
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
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2777793 [NCBI, ExPASy, EBI, Israel, Japan]
Matsubara Y., Indo Y., Naito E., Ozasa H., Glassberg R., Vockley J., Ikeda Y., Kraus J., Tanaka K.;
"Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family.";
J. Biol. Chem. 264:16321-16331(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-48.
DOI=10.1016/0888-7543(87)90053-X; PubMed=3446585 [NCBI, ExPASy, EBI, Israel, Japan]
Kraus J.P., Matsubara Y., Barton D., Yang-Feng T.L., Glassberg R., Ito M., Ikeda Y., Mole J., Francke U., Tanaka K.;
"Isolation of cDNA clones coding for rat isovaleryl-CoA dehydrogenase and assignment of the gene to human chromosome 15.";
Genomics 1:264-269(1987).
[4]
PROTEIN SEQUENCE OF 119-140; 273-285 AND 400-411, AND MASS SPECTROMETRY.
STRAIN=Sprague-Dawley;
TISSUE=Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
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
J05031; AAA41454.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC088401; AAH88401.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M19867; AAA41459.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C34252; C34252.
RefSeq NP_036724.1; -.
UniGene Rn.147
3D structure databases
HSSP P26440; 1IVH. [HSSP ENTRY / PDB]
SMR P12007; 36-422.
ModBase P12007.
Organism-specific databases
RGD 2936; Ivd.
Gene expression databases
ArrayExpress P12007; -.
GermOnline ENSRNOG00000009421; Rattus norvegicus.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
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 P12007.
Genome annotation databases
Ensembl ENSRNOG00000009421; Rattus norvegicus. [Contig view]
GeneID 24513; -.
KEGG rno:24513; -.
NMPDR fig|10116.3.peg.19461; -.
Phylogenomic databases
HOVERGEN P12007; -.
Other
ProtoNet P12007.
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. 
CHAIN   31   424  394     Isovaleryl-CoA dehydrogenase, mitochondrial. PRO_0000000534
ACT_SITE   284   284        Proton acceptor (By similarity). 
MOD_RES   76    76        N6-acetyllysine (By similarity). 
Sequence information
Length: 424 AA [This is the length of the unprocessed precursor] Molecular weight: 46435 Da [This is the MW of the unprocessed precursor] CRC64: D09FFD0A88EA5791 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATAVRLLGR RVSSWRLRPL PSPLAVPQRA HSMLPVDDDI NGLNEEQKQL RHTISKFVQE 

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

       130        140        150        160        170        180 
AAVGLSYGAH SNLCINQIVR NGNEAQKEKY LPKLISGEFI GALAMSEPNA GSDVVSMRLK 

       190        200        210        220        230        240 
AEKKGDHYVL NGNKFWITNG PDADVLVVYA KTDLTAVPAS RGITAFIVEK DMPGFSTSKK 

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

       310        320        330        340        350        360 
DHTIPYLHVR EAFGQKIGQF QLMQGKMADM YTRLMACRQY VYNVARACDE GHITAKDCAG 

       370        380        390        400        410        420 
VILYTAECAT QVALDGIQCL GGNGYINDFP MGRFLRDAKL YEIGGGTSEV RRLVIGRAFN 


ADFR 

P12007 in FASTA format

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