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Reviewed, UniProtKB/Swiss-Prot Q8JZN5 (ACAD9_MOUSE)

Last modified June 16, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    Acyl-CoA dehydrogenase family member 9, mitochondrial
      Short name=ACAD-9
    EC=1.3.99.-
Gene names
Name: Acad9
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 length625 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 a dehydrogenase activity on palmitoyl-CoA (C16:0) and stearoyl-CoA (C18:0). It is three times more active on palmitoyl-CoA then on stearoyl-CoA. Has little activity on octanoyl-CoA (C8:0), butyryl-CoA (C4:0) or isovaleryl-CoA (5:0) By similarity.

Cofactor

FAD By similarity.

Subcellular location

Mitochondrion Potential.

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

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Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from direct assay. Source: MGI

   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 – ?Mitochondrion Potential
Chain? – 625Acyl-CoA dehydrogenase family member 9, mitochondrialPRO_0000000525

Sites

Active site4301Proton acceptor By similarity

Experimental info

Sequence conflict151A → G in BAC27565. Ref.1
Sequence conflict531K → E in BAC27565. Ref.1
Sequence conflict531K → E in BAC36096. Ref.1
Sequence conflict1631D → E in BAC27565. Ref.1
Sequence conflict1631D → E in BAC36096. Ref.1
Sequence conflict5401I → V in BAC27565. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q8JZN5-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 4F06FFFBFD82F022

FASTA62568,707
        10         20         30         40         50         60 
MSGCVLLSRG ATAAAAAARA SRVLREFTAR RRPLHTSLQS CSFAKELFLG NIKQKGVFPF 

        70         80         90        100        110        120 
PEVSQHELSE INQFVGPLEK FFTEEVDSRK IDQEGKIPVD TLEKLKSLGL FGIQVPEEYG 

       130        140        150        160        170        180 
GLGLSNTMYA RLGEIISLDA SITVTLAAHQ AIGLKGIILV GNDEQKAKYL PKLSSGEHIA 

       190        200        210        220        230        240 
AFCLTEPASG SDAASIQTRA TLSEDKKYFI LNGSKVWITN GGLANIFTVF AKTEVVDSDG 

       250        260        270        280        290        300 
SKTDKMTAFI VERDFGGITN GKPEDKLGIR GSNTCEVHFE NTRVPVENVL GEVGGGFKVA 

       310        320        330        340        350        360 
MNILNSGRFS MGSAVAGMLK KLIELTAEYA CTRKQFNRNL SEFGLIQEKF ALMAQKAYVM 

       370        380        390        400        410        420 
ESMAYLTSGM LDQPGFPDCS IEAAMVKVFS SEAAWQCVSE ALQILGGSGY MKDYPYERML 

       430        440        450        460        470        480 
RDARILLIFE GTNEILRLFI ALTGLQHAGR ILTSRIKELK SGNVTTVMET IGRKLRDSLG 

       490        500        510        520        530        540 
RTVDLGLTGD LGVVHPSLGD SANKLEENVH YFGRTVETLL LRFGKNIVEE QLVLKRVANI 

       550        560        570        580        590        600 
LINLYGMTAV LSRASRSIRI GLRNHDHEVL LANMFCVEAY FQNLFSLSQL DKNAPENLDE 

       610        620 
QIKKVSRQIL EKRAYICAHP LDRAS

« 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: Medulla oblongata.
[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: Kidney.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AK031820 mRNA. Translation: BAC27565.1.
AK075984 mRNA. Translation: BAC36096.1.
BC031137 mRNA. Translation: AAH31137.1.
BC032213 mRNA. Translation: AAH32213.1.
BC033277 mRNA. Translation: AAH33277.1.
IPIIPI00331710.
RefSeqNP_766266.3.
UniGeneMm.260997

3D structure databases

HSSPHSSP built from PDB template 1JQI based on UniProtKB P15651.
ModBaseSearch...

Proteomic databases

PRIDEQ8JZN5.

Genome annotation databases

EnsemblENSMUSG00000027710. Mus musculus. [Contig view]
GeneID229211.
KEGGmmu:229211.

Organism-specific databases

MGIMGI:1914272. Acad9.

Phylogenomic databases

HOGENOMQ8JZN5.
HOVERGENQ8JZN5.

Gene expression databases

ArrayExpressQ8JZN5.
BgeeQ8JZN5.
CleanExMM_ACAD9.
GermOnlineENSMUSG00000027710. 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. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio379350.
SOURCESearch...

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Entry information

Entry nameACAD9_MOUSE
AccessionPrimary (citable) accession number: Q8JZN5
Secondary accession number(s): Q8BK76, Q8C0B5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 3, 2003
Last sequence update: October 1, 2002
Last modified: June 16, 2009
This is version 63 of the entry and version 1 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

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