Reviewed, UniProtKB/Swiss-Prot P11310 (ACADM_HUMAN)

Names and origin

Protein names

Recommended name:
    Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
      Short name=MCAD
    EC=1.3.99.3

Gene names

Name:

ACADM

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	421 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	This enzyme is specific for acyl chain lengths of 4 to 16.
Catalytic activity	Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.
Cofactor	FAD.
Pathway	Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subunit structure	Homotetramer. Interacts with the heterodimeric electron transfer flavoprotein ETF. Ref.9 Ref.10 Ref.11
Subcellular location	Mitochondrion matrix.
Involvement in disease	Defects in ACADM are the cause of medium-chain acyl-CoA dehydrogenase deficiency (MCAD deficiency) [MIM:201450]. It is an autosomal recessive disease which causes fasting hypoglycemia, hepatic dysfunction, and encephalopathy, often resulting in death in infancy. The disease frequency is one in 13000.
Miscellaneous	A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues. Utilizes the electron transfer flavoprotein (ETF) as electron acceptor that transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).
Sequence similarities	Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Ref.6 Inferred from mutant phenotype. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro acyl-CoA dehydrogenase activity Ref.6 Inferred from mutant phenotype. Source: UniProtKB electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 25

25

Mitochondrion

Chain

26 – 421

396

Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

PRO_0000000502

Regions

Nucleotide binding

158 – 167

10

FAD

Nucleotide binding

191 – 193

3

FAD

Nucleotide binding

306 – 308

3

FAD

Nucleotide binding

316 – 317

2

FAD

Nucleotide binding

374 – 378

5

FAD

Nucleotide binding

403 – 405

3

FAD

Region

278 – 281

4

Substrate binding

Sites

Active site

401

1

Proton acceptor

Binding site

167

1

Substrate; via carbonyl oxygen

Binding site

402

1

Substrate; via amide nitrogen

Amino acid modifications

Modified residue

212

1

N6-acetyllysine Ref.8

Modified residue

279

1

N6-acetyllysine Ref.8

Modified residue

301

1

N6-acetyllysine Ref.8

Natural variations

Natural variant

53

1

R → C in MCAD deficiency.

VAR_000317

Natural variant

67

1

Y → H in MCAD deficiency; mild. Ref.24

VAR_013698

Natural variant

78

1

I → T in MCAD deficiency. Ref.24

VAR_015954

Natural variant

115 – 116

2

Missing in MCAD deficiency.

VAR_000318

Natural variant

116

1

C → Y in MCAD deficiency. Ref.21

VAR_015955

Natural variant

121

1

T → I in MCAD deficiency. Ref.24

VAR_015956

Natural variant

132

1

P → R in a breast cancer sample; somatic mutation. Ref.27

VAR_035716

Natural variant

149

1

M → I in MCAD deficiency. Ref.15

VAR_000319

Natural variant

193

1

T → A in MCAD deficiency; the thermostability is markedly decreased. Ref.21 Ref.22

VAR_000320

Natural variant

195

1

G → R in MCAD deficiency. Ref.20

VAR_000321

Natural variant

206

1

R → L in MCAD deficiency. Ref.23

VAR_015957

Natural variant

244

1

C → R in MCAD deficiency. Ref.15

VAR_000322

Natural variant

245

1

S → L in MCAD deficiency. Ref.25

VAR_013699

Natural variant

267

1

G → R in MCAD deficiency. Ref.15

VAR_000323

Natural variant

281

1

R → T in MCAD deficiency; mild or benign clinical phenotype. Ref.26

VAR_013700

Natural variant

310

1

G → R in MCAD deficiency. Ref.24

VAR_015958

Natural variant

326

1

M → T in MCAD deficiency. Ref.18

VAR_000324

Natural variant

329

1

K → E in MCAD deficiency; most common variant. Ref.23 Ref.26 Ref.6 Ref.13 Ref.14 Ref.16 Ref.17

VAR_000325

Natural variant

336

1

S → R in MCAD deficiency. Ref.18

VAR_000326

Natural variant

352

1

Y → C in MCAD deficiency. Ref.21

VAR_015959

Natural variant

375

1

I → T in MCAD deficiency. Ref.15

VAR_000327

Experimental info

Mutagenesis

86

1

L → M: Strongly reduced rate of electron transfer to ETF. Ref.10

Mutagenesis

98

1

L → W: Strongly reduced rate of electron transfer to ETF. Ref.10

Mutagenesis

100

1

L → Y: Strongly reduced rate of electron transfer to ETF. Ref.10

Mutagenesis

108

1

I → M: Strongly reduced rate of electron transfer to ETF. Ref.10

Mutagenesis

191

1

W → A: Loss of electron transfer to ETF. Ref.11

Mutagenesis

191

1

W → F: Reduces rate of electron transfer to ETF about six-fold. Ref.11

Mutagenesis

237

1

E → A: Strongly reduced rate of electron transfer to ETF. Ref.10 Ref.11

Mutagenesis

384

1

E → A: Reduces rate of electron transfer to ETF three-fold. Ref.10 Ref.11

Mutagenesis

384

1

E → Q: Reduces rate of electron transfer to ETF two-fold. Ref.10 Ref.11

Sequence conflict

10

1

R → RCSLQ in AAF63626. Ref.3

Sequence conflict

356

1

I → T in AAF63626. Ref.3

Secondary structure

1

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421

Helix Strand Turn

Details...

Beta strand

36 – 38

3

Helix

43 – 59

17

Helix

61 – 70

10

Helix

75 – 84

10

Helix

93 – 95

3

Helix

102 – 115

14

Helix

117 – 129

13

Helix

131 – 136

6

Helix

139 – 151

13

Beta strand

156 – 159

4

Beta strand

165 – 168

4

Helix

169 – 171

3

Beta strand

175 – 178

4

Beta strand

180 – 193

14

Turn

194 – 197

4

Beta strand

199 – 206

8

Helix

215 – 217

3

Beta strand

219 – 225

7

Beta strand

231 – 233

3

Beta strand

239 – 241

3

Beta strand

247 – 258

12

Helix

259 – 261

3

Beta strand

262 – 265

4

Helix

269 – 303

35

Helix

313 – 315

3

Helix

317 – 345

29

Helix

351 – 376

26

Helix

377 – 379

3

Helix

387 – 394

8

Helix

395 – 398

4

Turn

399 – 401

3

Helix

404 – 417

14

Sequences

	Sequence		Length	Mass (Da)
	P11310-1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 7CD0B5832410581B	FASTA	421	46,588
	10 20 30 40 50 60 MAAGFGRCCR VLRSISRFHW RSQHTKANRQ REPGLGFSFE FTEQQKEFQA TARKFAREEI 70 80 90 100 110 120 IPVAAEYDKT GEYPVPLIRR AWELGLMNTH IPENCGGLGL GTFDACLISE ELAYGCTGVQ 130 140 150 160 170 180 TAIEGNSLGQ MPIIIAGNDQ QKKKYLGRMT EEPLMCAYCV TEPGAGSDVA GIKTKAEKKG 190 200 210 220 230 240 DEYIINGQKM WITNGGKANW YFLLARSDPD PKAPANKAFT GFIVEADTPG IQIGRKELNM 250 260 270 280 290 300 GQRCSDTRGI VFEDVKVPKE NVLIGDGAGF KVAMGAFDKT RPVVAAGAVG LAQRALDEAT 310 320 330 340 350 360 KYALERKTFG KLLVEHQAIS FMLAEMAMKV ELARMSYQRA AWEVDSGRRN TYYASIAKAF 370 380 390 400 410 420 AGDIANQLAT DAVQILGGNG FNTEYPVEKL MRDAKIYQIY EGTSQIQRLI VAREHIDKYK N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of medium-chain acyl-CoA dehydrogenase mRNA and its expression in enzyme-deficient human tissue." Kelly D.P., Kim J.-J.P., Billadello J.J., Hainline B.E., Chu T.W., Strauss A.W. Proc. Natl. Acad. Sci. U.S.A. 84:4068-4072(1987) [PubMed: 3035565] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structural organization and regulatory regions of the human medium-chain acyl-CoA dehydrogenase gene." Zhang Z.F., Kelly D.P., Kim J.-J.P., Zhou Y.Q., Ogden M.L., Whelan A.J., Strauss A.W. Biochemistry 31:81-89(1992) [PubMed: 1731887] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Medium-chain acyl-CoA dehydrogenase." Sun F., Wang Y., Block G.D. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Colon.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[5]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 218-235, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[6]	"Identification of a common mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency." Matsubara Y., Narisawa K., Miyabayashi S., Tada K., Coates P.M., Bachmann C., Elsas L.J. II, Pollitt R.J., Rhead W.J., Roe C.R. Biochem. Biophys. Res. Commun. 171:498-505(1990) [PubMed: 2393404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 314-342, VARIANT MCAD DEFICIENCY GLU-329.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-212; LYS-279 AND LYS-301, MASS SPECTROMETRY.
[9]	"Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity." Lee H.J., Wang M., Paschke R., Nandy A., Ghisla S., Kim J.-J.P. Biochemistry 35:12412-12420(1996) [PubMed: 8823176] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FAD AND OCTANOYL-COENZYME A, SUBUNIT.
[10]	"Extensive domain motion and electron transfer in the human electron transferring flavoprotein-medium chain acyl-CoA dehydrogenase complex." Toogood H.S., van Thiel A., Basran J., Sutcliffe M.J., Scrutton N.S., Leys D. J. Biol. Chem. 279:32904-32912(2004) [PubMed: 15159392] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-421 IN COMPLEXES WITH FAD AND THE ETFA-ETFB HETERODIMER, MUTAGENESIS OF LEU-86; LEU-98; LEU-100; ILE-108; GLU-237 AND GLU-384, SUBUNIT.
[11]	"Stabilization of non-productive conformations underpins rapid electron transfer to electron-transferring flavoprotein." Toogood H.S., van Thiel A., Scrutton N.S., Leys D. J. Biol. Chem. 280:30361-30366(2005) [PubMed: 15975918] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEXES WITH FAD AND THE ETFA-ETFB HETERODIMER, MUTAGENESIS OF TRP-191; GLU-237 AND GLU-384, SUBUNIT.
[12]	"Mutations in the medium chain acyl-CoA dehydrogenase (MCAD) gene." Tanaka K., Yokota I., Coates P.M., Strauss A.W., Kelly D.P., Zhang Z.F., Gregersen N., Andresen B.S., Matsubara Y., Curtis D., Chen Y.-T. Hum. Mutat. 1:271-279(1992) [PubMed: 1363805] [Abstract] Cited for: REVIEW ON VARIANTS MCAD DEFICIENCY.
[13]	"Molecular basis of medium chain acyl-coenzyme A dehydrogenase deficiency. An A to G transition at position 985 that causes a lysine-304 to glutamate substitution in the mature protein is the single prevalent mutation." Yokota I., Indo Y., Coates P.M., Tanaka K. J. Clin. Invest. 86:1000-1003(1990) [PubMed: 2394825] [Abstract] Cited for: VARIANT MCAD DEFICIENCY GLU-329.
[14]	"Molecular characterization of inherited medium-chain acyl-CoA dehydrogenase deficiency." Kelly D.P., Whelan A.J., Ogden M.L., Alpers R., Zhang Z.F., Bellus G., Gregersen N., Dorland L., Strauss A.W. Proc. Natl. Acad. Sci. U.S.A. 87:9236-9240(1990) [PubMed: 2251268] [Abstract] Cited for: VARIANT MCAD DEFICIENCY GLU-329.
[15]	"Molecular survey of a prevalent mutation, 985A-to-G transition, and identification of five infrequent mutations in the medium-chain Acyl-CoA dehydrogenase (MCAD) gene in 55 patients with MCAD deficiency." Yokota I., Coates P.M., Hale D.E., Rinaldo P., Tanaka K. Am. J. Hum. Genet. 49:1280-1291(1991) [PubMed: 1684086] [Abstract] Cited for: VARIANTS MCAD DEFICIENCY ILE-149; ARG-244; ARG-267 AND THR-375.
[16]	"Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coli." Gregersen N., Andresen B.S., Bross P., Winter V., Ruediger N., Engst S., Christensen E., Kelly D., Strauss A.W., Koelvraa S., Bolund L., Ghisla S. Hum. Genet. 86:545-551(1991) [PubMed: 1902818] [Abstract] Cited for: VARIANT MCAD DEFICIENCY GLU-329.
[17]	"Frequency of the G985 MCAD mutation in the general population." Blakemore A.I., Singleton H., Pollitt R.J., Engel P.C., Kolvraa S., Gregersen N., Curtis D. Lancet 337:298-299(1991) [PubMed: 1671131] [Abstract] Cited for: VARIANT MCAD DEFICIENCY GLU-329 FREQUENCY.
[18]	"Disease-causing mutations in exon 11 of the medium-chain acyl-CoA dehydrogenase gene." Andresen B.S., Jensen T.G., Bross P., Knudsen I., Winter V., Koelvraa S., Bolund L., Ding J.-H., Chen Y.-T., van Hove J.L.K., Curtis D., Yokota I., Tanaka K., Kim J.-J.P., Gregersen N. Am. J. Hum. Genet. 54:975-988(1994) [PubMed: 8198141] [Abstract] Cited for: VARIANTS MCAD DEFICIENCY THR-326 AND ARG-336.
[19]	"Medium chain acyl-CoA dehydrogenase deficiency in Pennsylvania: neonatal screening shows high incidence and unexpected mutation frequencies." Ziadeh R., Hoffman E.P., Finegold D.N., Hoop R.C., Brackett J.C., Strauss A.W., Naylor E.W. Pediatr. Res. 37:675-678(1995) [PubMed: 7603790] [Abstract] Cited for: VARIANT MCAD DEFICIENCY 115-GLY-CYS-116 DEL.
[20]	"A novel mutation in medium chain acyl-CoA dehydrogenase causes sudden neonatal death." Brackett J.C., Sims H.F., Steiner R.D., Nunge M., Zimmerman E.M., Demartinville B., Rinaldo P., Slaugh R., Strauss A.W. J. Clin. Invest. 94:1477-1483(1994) [PubMed: 7929823] [Abstract] Cited for: VARIANT MCAD DEFICIENCY ARG-195.
[21]	"The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in compound heterozygous patients: is there correlation between genotype and phenotype?" Andresen B.S., Bross P., Udvari S., Kirk J., Gray G., Kmoch S., Chamoles N., Knudsen I., Winter V., Wilcken B., Yokota I., Hart K., Packman S., Harpey J.P., Saudubray J.-M., Hale D.E., Bolund L., Koelvraa S., Gregersen N. Hum. Mol. Genet. 6:695-707(1997) [PubMed: 9158144] [Abstract] Cited for: VARIANTS MCAD DEFICIENCY TYR-116; ALA-193 AND CYS-352.
[22]	"Biochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site." Kuchler B., Abdel-Ghany A.G., Bross P., Nandy A., Rasched I., Ghisla S. Biochem. J. 337:225-230(1999) [PubMed: 9882619] [Abstract] Cited for: CHARACTERIZATION OF VARIANT MCAD DEFICIENCY ALA-193.
[23]	"Identification of a novel mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency." Yang B.-Z., Ding J.-H., Zhou C., Dimachkie M.M., Sweetman L., Dasouki M.J., Wilkinson J., Roe C.R. Mol. Genet. Metab. 69:259-262(2000) [PubMed: 10767181] [Abstract] Cited for: VARIANTS MCAD DEFICIENCY LEU-206 AND GLU-329.
[24]	"Medium-chain acyl-CoA dehydrogenase (MCAD) mutations identified by MS/MS-based prospective screening of newborns differ from those observed in patients with clinical symptoms: identification and characterization of a new, prevalent mutation that results in mild MCAD deficiency." Andresen B.S., Dobrowolski S.F., O'Reilly L., Muenzer J., McCandless S.E., Frazier D.M., Udvari S., Bross P., Knudsen I., Banas R., Chace D.H., Engel P.C., Naylor E.W., Gregersen N. Am. J. Hum. Genet. 68:1408-1418(2001) [PubMed: 11349232] [Abstract] Cited for: VARIANTS MCAD DEFICIENCY HIS-67; THR-78; ILE-121 AND ARG-310.
[25]	"Molecular and functional characterization of mild MCAD deficiency." Zschocke J., Schulze A., Lindner M., Fiesel S., Olgemoller K., Hoffmann G.F., Penzien J., Ruiter J.P.N., Wanders R.J.A., Mayatepek E. Hum. Genet. 108:404-408(2001) [PubMed: 11409868] [Abstract] Cited for: VARIANT MCAD DEFICIENCY LEU-245.
[26]	"Compound heterozygosity in four asymptomatic siblings with medium-chain acyl-CoA dehydrogenase deficiency." Albers S., Levy H.L., Irons M., Strauss A.W., Marsden D. J. Inherit. Metab. Dis. 24:417-418(2001) [PubMed: 11486912] [Abstract] Cited for: VARIANTS MCAD DEFICIENCY THR-281 AND GLU-329.
[27]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-132.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBLGenBankDDBJ

M16827 mRNA. Translation: AAA51566.1.
M91432 , M91421, M91422, M91423, M91425, M91426, M91427, M91428, M91429, M91430, M91431 Genomic DNA. Translation: AAA59567.1.
AF251043 mRNA. Translation: AAF63626.1.
BC005377 mRNA. Translation: AAH05377.1.
M60505 Genomic DNA. Translation: AAB59625.1.

IPI

IPI00005040.

PIR

DEHUCM. A29031.

RefSeq

NP_000007.1.
NP_001120800.1.

UniGene

Hs.445040

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EGC	X-ray	2.60	A/B/C/D	26-421	[»]
1EGD	X-ray	2.40	A/B/C/D	26-421	[»]
1EGE	X-ray	2.75	A/B/C/D	26-421	[»]
1T9G	X-ray	2.90	A/B/C/D	26-421	[»]
2A1T	X-ray	2.80	A/B/C/D	1-421	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P11310.

2-D gel databases

REPRODUCTION-2DPAGE

IPI00005040.

Proteomic databases

PRIDE

P11310.

Genome annotation databases

Ensembl

ENST00000370834; ENSP00000359871; ENSG00000117054; Homo sapiens. [Genome view]
ENST00000370841; ENSP00000359878; ENSG00000117054; Homo sapiens. [Genome view]
ENST00000420607; ENSP00000409612; ENSG00000117054; Homo sapiens. [Genome view]

GeneID

34.

KEGG

hsa:34.

UCSC

uc001dgw.2. human.

Organism-specific databases

CTD

34.

GeneCards

GC01P075902.

H-InvDB

HIX0000706.

HGNC

HGNC:89. ACADM.

HPA

HPA006198.
HPA026542.

MIM

201450. phenotype.
607008. gene.

Orphanet

42. Acyl-CoA dehydrogenase, medium chain, deficiency of.

PharmGKB

PA24425.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P11310.

Enzyme and pathway databases

BRENDA

1.3.99.3. 247.

Pathway_Interaction_DB

hnf3bpathway. FOXA2 and FOXA3 transcription factor networks.

Reactome

REACT_602. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

P11310.

Bgee

P11310.

CleanEx

HS_ACADM.

Genevestigator

P11310.

GermOnline

ENSG00000117054. Homo sapiens.

Family and domain databases

InterPro

IPR006089. 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]

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]

ProtoNet

Search...

Other Resources

NextBio

131.

SOURCE

Search...

Entry information

Entry name

ACADM_HUMAN

Accession

Primary (citable) accession number: P11310
Secondary accession number(s): Q9NYF1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	October 13, 2009
This is version 122 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.