Reviewed, UniProtKB/Swiss-Prot Q9H845 (ACAD9_HUMAN)

Names and origin

Protein names

Recommended name:
    Acyl-CoA dehydrogenase family member 9, mitochondrial
      Short name=ACAD-9
    EC=1.3.99.-

Gene names

Name:

ACAD9

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	621 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 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).
Cofactor	FAD By similarity.
Subcellular location	MitochondrionPotential.
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.
Involvement in disease	Defects in ACAD9 are a cause of acyl-CoA dehydrogenase family member type 9 deficiency (ACAD9 deficiency) [MIM:611126]. ACAD9 deficiency patients present with episodic liver dysfunction during otherwise mild illnesses or cardiomyopathy, along with chronic neurologic dysfunction.
Sequence similarities	Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Gene Ontology (GO)
Cellular component	mitochondrion Inferred from direct assay. Source: LIFEdb
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 621		Acyl-CoA dehydrogenase family member 9, mitochondrial
Sites
	Active site	426	1	Proton acceptor By similarity
Natural variations
	Natural variant	477	1	R → Q: dbSNP rs4494951.
Experimental info
	Sequence conflict	397	1	A → V in AAL56011. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9H845-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 064BCE0378877F54	FASTA	621	68,760
	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

References

	« Hide 'large scale' referencesShow '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: 12359260] [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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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]. Tissue: Lung and Uterus.
[4]	"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: 17564966] [Abstract] Cited for: INVOLVEMENT IN ACAD9 DEFICIENCY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF327351 mRNA. Translation: AAL56011.1. AK024012 mRNA. Translation: BAB14775.1. BC013354 mRNA. Translation: AAH13354.1. BC007970 mRNA. Translation: AAH07970.1.
PIR	JC7892.
RefSeq	NP_054768.2.
UniGene	Hs.567482
3D structure databases
HSSP	HSSP built from PDB template 1JQI based on UniProtKB P15651.
ModBase	Search...
Proteomic databases
PeptideAtlas	Q9H845.
Genome annotation databases
Ensembl	ENSG00000177646. Homo sapiens. [Contig view]
GeneID	28976.
KEGG	hsa:28976.
Organism-specific databases
H-InvDB	HIX0003658. HIX0003659.
HGNC	HGNC:21497. ACAD9.
MIM	611103. gene. 611126. phenotype.
PharmGKB	PA134900655.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	Q9H845.
HOVERGEN	Q9H845.
Gene expression databases
ArrayExpress	Q9H845.
CleanEx	HS_ACAD9.
GermOnline	ENSG00000177646. Homo sapiens.
Family and domain databases
InterPro	IPR006091. Acyl-CoA_DHase/Oxase_M. IPR006089. Acyl-CoA_DHase_CS. IPR006092. Acyl-CoA_DHase_N. IPR006090. Acyl-CoA_Oxase/DHase_1. 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]
ProDom	Q9H845. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	Search...

Entry information

Entry name

ACAD9_HUMAN

Accession

Primary (citable) accession number: Q9H845
Secondary accession number(s): Q8WXX3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 3, 2003
Last sequence update:	March 1, 2001
Last modified:	September 23, 2008
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)