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Reviewed, UniProtKB/Swiss-Prot Q9D7B6 (ACAD8_MOUSE)

Last modified June 16, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Isobutyryl-CoA dehydrogenase, mitochondrial
    EC=1.3.99.-
Alternative name(s):
    Acyl-CoA dehydrogenase family member 8
      Short name=ACAD-8
Gene names
Name: Acad8
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Has very high activity toward isobutyryl-CoA. Is an isobutyryl-CoA dehydrogenase that functions in valine catabolism By similarity.

Catalytic activity

Isobutyryl-CoA + ETF = methylacrylyl-CoA + reduced ETF.

Cofactor

FAD By similarity.

Pathway

Amino-acid degradation; L-valine degradation.

Subunit structure

Homotetramer, formed by a dimer of dimers. Subunit of the large multiprotein complex ARC/DRIP By similarity.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

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Ontologies

Keywords
   Biological processBranched-chain amino acid catabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processbranched chain family amino acid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD 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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2020Mitochondrion Potential
Chain21 – 413393Isobutyryl-CoA dehydrogenase, mitochondrial
PRO_0000000523

Regions

Nucleotide binding155 – 16511FAD By similarity
Nucleotide binding369 – 3757FAD By similarity
Nucleotide binding398 – 4003FAD By similarity
Region272 – 2754Substrate binding By similarity

Sites

Active site3961Proton acceptor By similarity
Binding site3001FAD By similarity
Binding site4081Substrate By similarity

Experimental info

Sequence conflict2071G → E in BAB26255. Ref.1
Sequence conflict2071G → E in BAB31764. Ref.1
Sequence conflict2071G → E in BAC26664. Ref.1
Sequence conflict2071G → E in BAC34521. Ref.1
Sequence conflict2071G → E in BAC36757. Ref.1
Sequence conflict2541A → P in BAC34521. Ref.1
Sequence conflict4131D → RLAPKLESLAWSLCAAGISL DAPMGCSVQVNHEVDQRAEL F in BAB31764. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q9D7B6-1 [UniParc].

Last modified May 16, 2003. Version 2.
Checksum: 13DED42D4BD51231

FASTA41345,020
        10         20         30         40         50         60 
MAMLRSGYRR FGCLRAALKS LAQTHHRSIT FCIDPSLGLN EEQKGFQKVA FDFAAREMAP 

        70         80         90        100        110        120 
NMAEWDQKEL FPVDVMRKAA QLGFGGVYVR TDVGGSGLSR LDTSVIFEAL ATGCTSTTAY 

       130        140        150        160        170        180 
ISIHNMCAWM IDSFGNEEQR HKFCPPLCTM EKFASYCLTE PGSGSDAASL LTSAKQQGDH 

       190        200        210        220        230        240 
YILNGSKAFI SGGGESDIYV VMCRTGGSGA KGISCIVVEK GTPGLSFGKK EKKVGWNSQP 

       250        260        270        280        290        300 
TRAVIFEDCA VPVANRIGTE GQGFLIAMKG LNGGRINVAS CSLGAAHASV ILTQEHLKVR 

       310        320        330        340        350        360 
KQFGAPLARS QYLQFQLADM ATKLVASRLM IRTAAVALQE EREDAVALCS MAKLFATEEC 

       370        380        390        400        410 
FAICNQALQM HGGYGYLKDY AVQQYMRDSR VHQILEGSNE VMRMLISRNL LQD

« Hide

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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. expand/collapse author list , 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: Embryo, Pituitary, Skin, Testis and Tongue.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.

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Cross-references

Sequence databases

AK009379 mRNA. Translation: BAB26255.2.
AK019502 mRNA. Translation: BAB31764.1.
AK029897 mRNA. Translation: BAC26664.1. Different initiation.
AK051091 mRNA. Translation: BAC34521.1.
AK077335 mRNA. Translation: BAC36757.1.
BC037644 mRNA. Translation: AAH37644.1.
IPIIPI00274222.
RefSeqNP_080138.2.
UniGeneMm.289244

3D structure databases

HSSPHSSP built from PDB template 1BUC based on UniProtKB Q06319.
SMRQ9D7B6. Positions 30-413.
ModBaseSearch...

Genome annotation databases

EnsemblENSMUSG00000031969. Mus musculus. [Contig view]
GeneID66948.
KEGGmmu:66948.

Organism-specific databases

MGIMGI:1914198. Acad8.

Phylogenomic databases

HOVERGENQ9D7B6.

Gene expression databases

ArrayExpressQ9D7B6.
BgeeQ9D7B6.
CleanExMM_ACAD8.
GermOnlineENSMUSG00000031969. Mus musculus.

Family and domain databases

InterProIPR006089. 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]
Gene3DG3DSA: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.
PfamPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
PROSITEPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio323096.
SOURCESearch...

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Entry information

Entry nameACAD8_MOUSE
AccessionPrimary (citable) accession number: Q9D7B6
Secondary accession number(s): Q8BK36 expand/collapse secondary AC list , Q8BKQ8, Q8CFY9, Q9D2L8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: May 16, 2003
Last modified: June 16, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents