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Q9H845 (ACAD9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length621 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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 than on stearoyl-CoA. Has little activity on octanoyl-CoA (C8:0), butyryl-CoA (C4:0) or isovaleryl-CoA (5:0).

Cofactor

FAD By similarity.

Subunit structure

Part of the mitochondrial complex I assembly (MCIA) complex. The complex comprises at least TMEM126B, NDUFAF1, ECSIT, and ACAD9 By similarity.

Subcellular location

Mitochondrion By similarity.

Tissue specificity

Ubiquitously expressed in most normal human tissues and cancer cell lines with high level of expression in heart, skeletal muscles, brain, kidney and liver. Ref.1

Involvement in disease

Acyl-CoA dehydrogenase family, member 9, deficiency (ACAD9 deficiency) [MIM:611126]: A metabolic disorder with variable manifestations that include dilated cardiomyopathy, liver failure, muscle weakness, neurologic dysfunction, hypoglycemia and Reye-like episodes (brain edema and vomiting that may rapidly progress to seizures, coma and death).
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentdendrite

Inferred from direct assay PubMed 21237683. Source: UniProtKB

mitochondrion

Inferred from direct assay. Source: LIFEdb

nucleus

Inferred from direct assay PubMed 21237683. Source: UniProtKB

   Molecular_functionacyl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 621Acyl-CoA dehydrogenase family member 9, mitochondrialPRO_0000000524

Sites

Active site4261Proton acceptor By similarity

Amino acid modifications

Modified residue411N6-acetyllysine Ref.6
Modified residue921N6-succinyllysine By similarity
Modified residue5211N6-acetyllysine; alternate By similarity
Modified residue5211N6-succinyllysine; alternate By similarity

Natural variations

Natural variant4771R → Q.
Corresponds to variant rs4494951 [ dbSNP | Ensembl ].
VAR_033459

Experimental info

Sequence conflict3971A → V in AAL56011. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9H845 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 064BCE0378877F54

FASTA62168,760
        10         20         30         40         50         60 
MSGCGLFLRT TAAARACRGL VVSTANRRLL RTSPPVRAFA KELFLGKIKK KEVFPFPEVS 

        70         80         90        100        110        120 
QDELNEINQF LGPVEKFFTE EVDSRKIDQE GKIPDETLEK LKSLGLFGLQ VPEEYGGLGF 

       130        140        150        160        170        180 
SNTMYSRLGE IISMDGSITV TLAAHQAIGL KGIILAGTEE QKAKYLPKLA SGEHIAAFCL 

       190        200        210        220        230        240 
TEPASGSDAA SIRSRATLSE DKKHYILNGS KVWITNGGLA NIFTVFAKTE VVDSDGSVKD 

       250        260        270        280        290        300 
KITAFIVERD FGGVTNGKPE DKLGIRGSNT CEVHFENTKI PVENILGEVG DGFKVAMNIL 

       310        320        330        340        350        360 
NSGRFSMGSV VAGLLKRLIE MTAEYACTRK QFNKRLSEFG LIQEKFALMA QKAYVMESMT 

       370        380        390        400        410        420 
YLTAGMLDQP GFPDCSIEAA MVKVFSSEAA WQCVSEALQI LGGLGYTRDY PYERILRDTR 

       430        440        450        460        470        480 
ILLIFEGTNE ILRMYIALTG LQHAGRILTT RIHELKQAKV STVMDTVGRR LRDSLGRTVD 

       490        500        510        520        530        540 
LGLTGNHGVV HPSLADSANK FEENTYCFGR TVETLLLRFG KTIMEEQLVL KRVANILINL 

       550        560        570        580        590        600 
YGMTAVLSRA SRSIRIGLRN HDHEVLLANT FCVEAYLQNL FSLSQLDKYA PENLDEQIKK 

       610        620 
VSQQILEKRA YICAHPLDRT C 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and functional characterization of ACAD-9, a novel member of human acyl-CoA dehydrogenase family."
Zhang J., Zhang W., Zou D., Chen G., Wan T., Zhang M., Cao X.
Biochem. Biophys. Res. Commun. 297:1033-1042(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY.
Tissue: Dendritic cell.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung and Uterus.
[5]"A new genetic disorder in mitochondrial fatty acid beta-oxidation: ACAD9 deficiency."
He M., Rutledge S.L., Kelly D.R., Palmer C.A., Murdoch G., Majumder N., Nicholls R.D., Pei Z., Watkins P.A., Vockley J.
Am. J. Hum. Genet. 81:87-103(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN ACAD9 DEFICIENCY.
[6]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-41, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF327351 mRNA. Translation: AAL56011.1.
AK024012 mRNA. Translation: BAB14775.1.
CH471052 Genomic DNA. Translation: EAW79295.1.
CH471052 Genomic DNA. Translation: EAW79296.1.
BC013354 mRNA. Translation: AAH13354.1.
BC007970 mRNA. Translation: AAH07970.1.
CCDSCCDS3053.1.
PIRJC7892.
RefSeqNP_054768.2. NM_014049.4.
UniGeneHs.567482.

3D structure databases

ProteinModelPortalQ9H845.
SMRQ9H845. Positions 38-617.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118799. 13 interactions.
DIPDIP-53699N.
IntActQ9H845. 16 interactions.
STRING9606.ENSP00000312618.

PTM databases

PhosphoSiteQ9H845.

Polymorphism databases

DMDM32469596.

Proteomic databases

MaxQBQ9H845.
PaxDbQ9H845.
PeptideAtlasQ9H845.
PRIDEQ9H845.

Protocols and materials databases

DNASU28976.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308982; ENSP00000312618; ENSG00000177646.
GeneID28976.
KEGGhsa:28976.
UCSCuc003ela.4. human.

Organism-specific databases

CTD28976.
GeneCardsGC03P128931.
H-InvDBHIX0003659.
HGNCHGNC:21497. ACAD9.
HPAHPA037716.
HPA046720.
MIM611103. gene.
611126. phenotype.
neXtProtNX_Q9H845.
Orphanet99901. Acyl-CoA dehydrogenase 9 deficiency.
2609. Isolated NADH-CoQ reductase deficiency.
PharmGKBPA134900655.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1960.
HOGENOMHOG000131665.
HOVERGENHBG050448.
InParanoidQ9H845.
KOK15980.
OMAHYLINGS.
OrthoDBEOG712TVX.
PhylomeDBQ9H845.
TreeFamTF105053.

Enzyme and pathway databases

SABIO-RKQ9H845.

Gene expression databases

ArrayExpressQ9H845.
BgeeQ9H845.
CleanExHS_ACAD9.
GenevestigatorQ9H845.

Family and domain databases

Gene3D1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMSSF47203. SSF47203. 2 hits.
SSF56645. SSF56645. 1 hit.
PROSITEPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiACAD9.
GenomeRNAi28976.
NextBio51851.
PROQ9H845.
SOURCESearch...

Entry information

Entry nameACAD9_HUMAN
AccessionPrimary (citable) accession number: Q9H845
Secondary accession number(s): D3DNB8, Q8WXX3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 3, 2003
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM