Reviewed, UniProtKB/Swiss-Prot Q9DBL1 (ACDSB_MOUSE)

Names and origin

Protein names

Recommended name:
    Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
      Short name=SBCAD
    EC=1.3.99.-
Alternative name(s):
    2-methyl branched chain acyl-CoA dehydrogenase
      Short name=2-MEBCAD
    2-methylbutyryl-coenzyme A dehydrogenase
      Short name=2-methylbutyryl-CoA dehydrogenase

Gene names

Name:

Acadsb

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has greatest activity toward short branched chain acyl-CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl-CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent By similarity.
Catalytic activity	Acyl-CoA + ETF = 2,3-dehydroacyl-CoA + reduced ETF.
Cofactor	FAD By similarity.
Pathway	Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subunit structure	Homotetramer By similarity.
Subcellular location	Mitochondrion matrix Probable.
Sequence similarities	Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro acyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 33	33	Mitochondrion By similarity
	Chain	34 – 432	399	Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial		PRO_0000000520
Sites
	Active site	414	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	284	1	N6-acetyllysine Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9DBL1-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 0272723CE36BCC46	FASTA	432	47,874
	10 20 30 40 50 60 MAVSALQLWR MGGLLRRRFP TCLSPWKIPP RVLKSSQPEA LVSLTNNAVA FAPLQTLTDE 70 80 90 100 110 120 EIMMKQTVKK FAQEHVAPLV SSMDENSKME KSVIQGLFQQ GLMGIEVEAQ YGGTEASFFC 130 140 150 160 170 180 SVLVIEELAK VDASVALLCD IQNTIINNLF RKHASEEQKA TYLPKLVTEK LGSFCLSEAG 190 200 210 220 230 240 AGSDSFAMKT RADKSGNYYV LNGSKMWISH AEHAELFLVF ANVDPSSGYR GITCFLVDRD 250 260 270 280 290 300 TEGFQIGKRE NKMGIRASST CQLTFENVKV PETNILGKIG HGYKYAIGSL NEGRIGIAAQ 310 320 330 340 350 360 MLGLAQGCFD YTIPYIKERM QFGKRIFDFQ GLQHQVAQVA TQLEATRLLT YNAARLVEAG 370 380 390 400 410 420 RPFIKEASMA KYYASEVAGL TTSKCIEWMG GVGYTKDYPV EKFFRDAKIG TIYEGASNIQ 430 LNTIAKHIDA EY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Liver.
[2]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 348-355, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[3]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." 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. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-284, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK004889 mRNA. Translation: BAB23646.1.
IPI	IPI00119842.
RefSeq	NP_080102.1.
UniGene	Mm.334274
3D structure databases
HSSP	HSSP built from PDB template 1BUC based on UniProtKB Q06319.
SMR	Q9DBL1. Positions 52-432.
ModBase	Search...
PTM databases
PhosphoSite	Q9DBL1.
Proteomic databases
PRIDE	Q9DBL1.
Genome annotation databases
Ensembl	ENSMUSG00000030861. Mus musculus. [Contig view]
GeneID	66885.
KEGG	mmu:66885.
NMPDR	fig|10090.3.peg.17790.
Organism-specific databases
MGI	MGI:1914135. Acadsb.
Phylogenomic databases
HOGENOM	Q9DBL1.
HOVERGEN	Q9DBL1.
OMA	Q9DBL1. IEWMGGV.
Gene expression databases
ArrayExpress	Q9DBL1.
Bgee	Q9DBL1.
GermOnline	ENSMUSG00000030861. Mus musculus.
Family and domain databases
InterPro	IPR006089. Acyl-CoA_DH_CS. IPR006092. Acyl-CoA_DH_N. IPR006090. Acyl-CoA_Oxase/DH_1. IPR006091. Acyl-CoA_Oxase/DH_M. IPR013786. AcylCoA_DH/ox_N. IPR013764. AcylCoA_oxidase/DH_1/2_C. [Graphical view]
Gene3D	G3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit. G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit. G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 1 hit.
Pfam	PF00441. Acyl-CoA_dh_1. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. PF02771. Acyl-CoA_dh_N. 1 hit. [Graphical view]
PROSITE	PS00072. ACYL_COA_DH_1. 1 hit. PS00073. ACYL_COA_DH_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	322929.
SOURCE	Search...

Entry information

Entry name

ACDSB_MOUSE

Accession

Primary (citable) accession number: Q9DBL1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2002
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)