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Protein

Acyl-CoA dehydrogenase family member 9, mitochondrial

Gene

Acad9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Required for mitochondrial complex I assembly (By similarity). 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. However, it does not play a primary role in long-chain fatty acid oxidation (By similarity). Has little activity on octanoyl-CoA (C8:0), butyryl-CoA (C4:0) or isovaleryl-CoA (5:0) (By similarity).By similarity

Cofactori

FADBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei430 – 4301Proton acceptorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-MMU-6799198. Complex I biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA dehydrogenase family member 9, mitochondrial (EC:1.3.99.-)
Short name:
ACAD-9
Gene namesi
Name:Acad9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1914272. Acad9.

Subcellular locationi

  • Mitochondrion By similarity

GO - Cellular componenti

  • dendrite Source: MGI
  • mitochondrion Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 625Acyl-CoA dehydrogenase family member 9, mitochondrialPRO_0000000525
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei45 – 451N6-acetyllysineBy similarity
Modified residuei96 – 961N6-succinyllysineCombined sources
Modified residuei242 – 2421N6-succinyllysineCombined sources
Modified residuei482 – 4821PhosphothreonineCombined sources
Modified residuei525 – 5251N6-acetyllysine; alternateCombined sources
Modified residuei525 – 5251N6-succinyllysine; alternateCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8JZN5.
MaxQBiQ8JZN5.
PaxDbiQ8JZN5.
PeptideAtlasiQ8JZN5.
PRIDEiQ8JZN5.

PTM databases

iPTMnetiQ8JZN5.
PhosphoSiteiQ8JZN5.
SwissPalmiQ8JZN5.

Expressioni

Gene expression databases

BgeeiQ8JZN5.
CleanExiMM_ACAD9.
ExpressionAtlasiQ8JZN5. baseline and differential.
GenevisibleiQ8JZN5. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-59192N.
IntActiQ8JZN5. 2 interactions.
MINTiMINT-4086603.
STRINGi10090.ENSMUSP00000011492.

Structurei

3D structure databases

ProteinModelPortaliQ8JZN5.
SMRiQ8JZN5. Positions 39-621.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0137. Eukaryota.
COG1960. LUCA.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131665.
HOVERGENiHBG050448.
InParanoidiQ8JZN5.
KOiK15980.
OMAiPQNTLAS.
OrthoDBiEOG712TVX.
TreeFamiTF105053.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
InterProiIPR006089. 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]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 2 hits.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8JZN5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGCVLLSRG ATAAAAAARA SRVLREFTAR RRPLHTSLQS CSFAKELFLG
60 70 80 90 100
NIEQKGVFPF PEVSQHELSE INQFVGPLEK FFTEEVDSRK IDQEGKIPVD
110 120 130 140 150
TLEKLKSLGL FGIQVPEEYG GLGLSNTMYA RLGEIISLDA SITVTLAAHQ
160 170 180 190 200
AIGLKGIILV GNEEQKAKYL PKLSSGEHIA AFCLTEPASG SDAASIQTRA
210 220 230 240 250
TLSEDKKYFI LNGSKVWITN GGLANIFTVF AKTEVVDSDG SKTDKMTAFI
260 270 280 290 300
VERDFGGITN GKPEDKLGIR GSNTCEVHFE NTRVPVENVL GEVGGGFKVA
310 320 330 340 350
MNILNSGRFS MGSAVAGMLK KLIELTAEYA CTRKQFNRNL SEFGLIQEKF
360 370 380 390 400
ALMAQKAYVM ESMAYLTSGM LDQPGFPDCS IEAAMVKVFS SEAAWQCVSE
410 420 430 440 450
ALQILGGSGY MKDYPYERML RDARILLIFE GTNEILRLFI ALTGLQHAGR
460 470 480 490 500
ILTSRIKELK SGNVTTVMET IGRKLRDSLG RTVDLGLTGD LGVVHPSLGD
510 520 530 540 550
SANKLEENVH YFGRTVETLL LRFGKNIVEE QLVLKRVANI LINLYGMTAV
560 570 580 590 600
LSRASRSIRI GLRNHDHEVL LANMFCVEAY FQNLFSLSQL DKNAPENLDE
610 620
QIKKVSRQIL EKRAYICAHP LDRAS
Length:625
Mass (Da):68,722
Last modified:July 27, 2011 - v2
Checksum:i29567F60B52E6FEA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151A → G in BAC27565 (PubMed:16141072).Curated
Sequence conflicti53 – 531E → K in AAH31137 (PubMed:15489334).Curated
Sequence conflicti53 – 531E → K in AAH32213 (PubMed:15489334).Curated
Sequence conflicti53 – 531E → K in AAH33277 (PubMed:15489334).Curated
Sequence conflicti163 – 1631E → D in AAH31137 (PubMed:15489334).Curated
Sequence conflicti163 – 1631E → D in AAH32213 (PubMed:15489334).Curated
Sequence conflicti163 – 1631E → D in AAH33277 (PubMed:15489334).Curated
Sequence conflicti540 – 5401I → V in BAC27565 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031820 mRNA. Translation: BAC27565.1.
AK075984 mRNA. Translation: BAC36096.1.
AK145423 mRNA. Translation: BAE26429.1.
BC031137 mRNA. Translation: AAH31137.1.
BC032213 mRNA. Translation: AAH32213.1.
BC033277 mRNA. Translation: AAH33277.1.
CCDSiCCDS17310.1.
RefSeqiNP_766266.3. NM_172678.3.
UniGeneiMm.260997.

Genome annotation databases

EnsembliENSMUST00000011492; ENSMUSP00000011492; ENSMUSG00000027710.
GeneIDi229211.
KEGGimmu:229211.
UCSCiuc008oze.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031820 mRNA. Translation: BAC27565.1.
AK075984 mRNA. Translation: BAC36096.1.
AK145423 mRNA. Translation: BAE26429.1.
BC031137 mRNA. Translation: AAH31137.1.
BC032213 mRNA. Translation: AAH32213.1.
BC033277 mRNA. Translation: AAH33277.1.
CCDSiCCDS17310.1.
RefSeqiNP_766266.3. NM_172678.3.
UniGeneiMm.260997.

3D structure databases

ProteinModelPortaliQ8JZN5.
SMRiQ8JZN5. Positions 39-621.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59192N.
IntActiQ8JZN5. 2 interactions.
MINTiMINT-4086603.
STRINGi10090.ENSMUSP00000011492.

PTM databases

iPTMnetiQ8JZN5.
PhosphoSiteiQ8JZN5.
SwissPalmiQ8JZN5.

Proteomic databases

EPDiQ8JZN5.
MaxQBiQ8JZN5.
PaxDbiQ8JZN5.
PeptideAtlasiQ8JZN5.
PRIDEiQ8JZN5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000011492; ENSMUSP00000011492; ENSMUSG00000027710.
GeneIDi229211.
KEGGimmu:229211.
UCSCiuc008oze.1. mouse.

Organism-specific databases

CTDi28976.
MGIiMGI:1914272. Acad9.

Phylogenomic databases

eggNOGiKOG0137. Eukaryota.
COG1960. LUCA.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131665.
HOVERGENiHBG050448.
InParanoidiQ8JZN5.
KOiK15980.
OMAiPQNTLAS.
OrthoDBiEOG712TVX.
TreeFamiTF105053.

Enzyme and pathway databases

ReactomeiR-MMU-6799198. Complex I biogenesis.

Miscellaneous databases

PROiQ8JZN5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8JZN5.
CleanExiMM_ACAD9.
ExpressionAtlasiQ8JZN5. baseline and differential.
GenevisibleiQ8JZN5. MM.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
InterProiIPR006089. 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]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 2 hits.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-482, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-96; LYS-242 AND LYS-525, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-525, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiACAD9_MOUSE
AccessioniPrimary (citable) accession number: Q8JZN5
Secondary accession number(s): Q3ULL9, Q8BK76, Q8C0B5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 3, 2003
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.