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P11310 (ACADM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 171. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

Short name=MCAD
EC=1.3.8.7
Gene names
Name:ACADM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme is specific for acyl chain lengths of 4 to 16.

Catalytic activity

A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.

Cofactor

FAD.

Pathway

Lipid metabolism; mitochondrial fatty acid beta-oxidation.

Subunit structure

Homotetramer. Interacts with the heterodimeric electron transfer flavoprotein ETF. Ref.13 Ref.14 Ref.15

Subcellular location

Mitochondrion matrix.

Post-translational modification

Acetylation at Lys-307 and Lys-311 in proximity of the cofactor-binding sites reduces catalytic activity By similarity. These sites are deacetylated by SIRT3. Ref.12

Involvement in disease

Acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:201450]: An inborn error of mitochondrial fatty acid beta-oxidation which causes fasting hypoglycemia, hepatic dysfunction and encephalopathy, often resulting in death in infancy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30

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 processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

carnitine biosynthetic process

Inferred from mutant phenotype PubMed 16972171. Source: BHF-UCL

carnitine metabolic process, CoA-linked

Inferred from mutant phenotype PubMed 16972171. Source: BHF-UCL

cellular lipid metabolic process

Traceable author statement. Source: Reactome

fatty acid beta-oxidation

Inferred from mutant phenotype Ref.9. Source: UniProtKB

fatty acid beta-oxidation using acyl-CoA dehydrogenase

Inferred from direct assay Ref.20PubMed 19224950. Source: BHF-UCL

glycogen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

medium-chain fatty acid catabolic process

Inferred from direct assay PubMed 1970566. Source: BHF-UCL

medium-chain fatty acid metabolic process

Inferred from direct assay PubMed 1970566. Source: BHF-UCL

oxidation-reduction process

Inferred from direct assay Ref.20. Source: BHF-UCL

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

regulation of gluconeogenesis

Inferred from electronic annotation. Source: Ensembl

response to cold

Inferred from electronic annotation. Source: Ensembl

response to starvation

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentaxon

Inferred from direct assay PubMed 21237683. Source: UniProtKB

mitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay. Source: LIFEdb

   Molecular_functionacyl-CoA dehydrogenase activity

Inferred from mutant phenotype Ref.9. Source: UniProtKB

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

identical protein binding

Inferred from direct assay PubMed 19224950. Source: BHF-UCL

medium-chain-acyl-CoA dehydrogenase activity

Inferred from direct assay Ref.20PubMed 19224950PubMed 1970566. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P11310-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P11310-2)

The sequence of this isoform differs from the canonical sequence as follows:
     10-10: R → RCSLQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2525Mitochondrion
Chain26 – 421396Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000000502

Regions

Nucleotide binding158 – 16710FAD
Nucleotide binding191 – 1933FAD
Nucleotide binding306 – 3083FAD
Nucleotide binding316 – 3172FAD
Nucleotide binding374 – 3785FAD
Nucleotide binding403 – 4053FAD
Region278 – 2814Substrate binding

Sites

Active site4011Proton acceptor
Binding site1671Substrate; via carbonyl oxygen
Binding site2161Substrate
Binding site4021Substrate; via amide nitrogen
Binding site4131Substrate

Amino acid modifications

Modified residue691N6-acetyllysine; alternate By similarity
Modified residue691N6-succinyllysine; alternate By similarity
Modified residue1791N6-succinyllysine By similarity
Modified residue2121N6-acetyllysine; alternate By similarity
Modified residue2121N6-succinyllysine; alternate By similarity
Modified residue2171N6-acetyllysine; alternate By similarity
Modified residue2171N6-succinyllysine; alternate By similarity
Modified residue2591N6-acetyllysine; alternate By similarity
Modified residue2591N6-succinyllysine; alternate By similarity
Modified residue2711N6-acetyllysine; alternate By similarity
Modified residue2711N6-succinyllysine; alternate By similarity
Modified residue2791N6-acetyllysine Ref.10
Modified residue3011N6-acetyllysine Ref.10

Natural variations

Alternative sequence101R → RCSLQ in isoform 2.
VSP_038420
Natural variant531R → C in ACADMD.
VAR_000317
Natural variant671Y → H in ACADMD; mild. Ref.28
VAR_013698
Natural variant781I → T in ACADMD. Ref.28
VAR_015954
Natural variant115 – 1162Missing in ACADMD.
VAR_000318
Natural variant1161C → Y in ACADMD. Ref.25
VAR_015955
Natural variant1211T → I in ACADMD. Ref.28
VAR_015956
Natural variant1321P → R in a breast cancer sample; somatic mutation. Ref.31
VAR_035716
Natural variant1491M → I in ACADMD. Ref.19
VAR_000319
Natural variant1931T → A in ACADMD; the thermostability is markedly decreased. Ref.25 Ref.26
VAR_000320
Natural variant1951G → R in ACADMD. Ref.24
VAR_000321
Natural variant2061R → L in ACADMD. Ref.27
VAR_015957
Natural variant2441C → R in ACADMD. Ref.19
VAR_000322
Natural variant2451S → L in ACADMD. Ref.29
VAR_013699
Natural variant2671G → R in ACADMD. Ref.19
VAR_000323
Natural variant2811R → T in ACADMD; mild or benign clinical phenotype. Ref.30
VAR_013700
Natural variant3101G → R in ACADMD. Ref.28
VAR_015958
Natural variant3261M → T in ACADMD. Ref.22
VAR_000324
Natural variant3291K → E in ACADMD; most common variant. Ref.9 Ref.17 Ref.18 Ref.20 Ref.21 Ref.27 Ref.30
Corresponds to variant rs77931234 [ dbSNP | Ensembl ].
VAR_000325
Natural variant3361S → R in ACADMD. Ref.22
VAR_000326
Natural variant3521Y → C in ACADMD. Ref.25
VAR_015959
Natural variant3751I → T in ACADMD. Ref.19
VAR_000327

Experimental info

Mutagenesis861L → M: Strongly reduced rate of electron transfer to ETF. Ref.14
Mutagenesis981L → W: Strongly reduced rate of electron transfer to ETF. Ref.14
Mutagenesis1001L → Y: Strongly reduced rate of electron transfer to ETF. Ref.14
Mutagenesis1081I → M: Strongly reduced rate of electron transfer to ETF. Ref.14
Mutagenesis1911W → A: Loss of electron transfer to ETF. Ref.15
Mutagenesis1911W → F: Reduces rate of electron transfer to ETF about six-fold. Ref.15
Mutagenesis2371E → A: Strongly reduced rate of electron transfer to ETF. Ref.14 Ref.15
Mutagenesis3841E → A: Reduces rate of electron transfer to ETF three-fold. Ref.14 Ref.15
Mutagenesis3841E → Q: Reduces rate of electron transfer to ETF two-fold. Ref.14 Ref.15
Sequence conflict3561I → T in AAF63626. Ref.3

Secondary structure

........................................................... 421
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 7CD0B5832410581B

FASTA42146,588
        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 

« Hide

Isoform 2 [UniParc].

Checksum: C6A133404E1B6E70
Show »

FASTA42547,020

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[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] (ISOFORM 2).
Tissue: Colon.
[4]"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] (ISOFORM 1).
Tissue: Heart.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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].
[7]"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] (ISOFORM 1).
Tissue: Liver.
[8]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 218-235, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[9]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 314-342, VARIANT ACADMD GLU-329.
[10]"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-279 AND LYS-301, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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].
[12]"SIRT3 regulates long-chain acyl-coA dehydrogenase by deacetylating conserved lysines near the active site."
Bharathi S.S., Zhang Y., Mohsen A.W., Uppala R., Balasubramani M., Schreiber E., Uechi G., Beck M.E., Rardin M.J., Vockley J., Verdin E., Gibson B.W., Hirschey M.D., Goetzman E.S.
J. Biol. Chem. 288:33837-33847(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: DEACETYLATION BY SIRT3.
[13]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FAD AND OCTANOYL-COENZYME A, SUBUNIT.
[14]"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] [Europe PMC] [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.
[15]"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] [Europe PMC] [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.
[16]"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] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS ACADMD.
[17]"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] [Europe PMC] [Abstract]
Cited for: VARIANT ACADMD GLU-329.
[18]"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] [Europe PMC] [Abstract]
Cited for: VARIANT ACADMD GLU-329.
[19]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS ACADMD ILE-149; ARG-244; ARG-267 AND THR-375.
[20]"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] [Europe PMC] [Abstract]
Cited for: VARIANT ACADMD GLU-329.
[21]"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] [Europe PMC] [Abstract]
Cited for: VARIANT ACADMD GLU-329 FREQUENCY.
[22]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS ACADMD THR-326 AND ARG-336.
[23]"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] [Europe PMC] [Abstract]
Cited for: VARIANT ACADMD 115-GLY-CYS-116 DEL.
[24]"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] [Europe PMC] [Abstract]
Cited for: VARIANT ACADMD ARG-195.
[25]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS ACADMD TYR-116; ALA-193 AND CYS-352.
[26]"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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT ACADMD ALA-193.
[27]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS ACADMD LEU-206 AND GLU-329.
[28]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS ACADMD HIS-67; THR-78; ILE-121 AND ARG-310.
[29]"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] [Europe PMC] [Abstract]
Cited for: VARIANT ACADMD LEU-245.
[30]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS ACADMD THR-281 AND GLU-329.
[31]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-132.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16827 mRNA. Translation: AAA51566.1.
M91432 expand/collapse EMBL AC list , M91421, M91422, M91423, M91425, M91426, M91427, M91428, M91429, M91430, M91431 Genomic DNA. Translation: AAA59567.1.
AF251043 mRNA. Translation: AAF63626.1.
AK312629 mRNA. Translation: BAG35514.1.
AL357314 Genomic DNA. Translation: CAI22390.1.
CH471059 Genomic DNA. Translation: EAX06401.1.
BC005377 mRNA. Translation: AAH05377.1.
M60505 Genomic DNA. Translation: AAB59625.1.
PIRDEHUCM. A29031.
RefSeqNP_000007.1. NM_000016.5.
NP_001120800.1. NM_001127328.2.
UniGeneHs.445040.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EGCX-ray2.60A/B/C/D26-421[»]
1EGDX-ray2.40A/B/C/D26-421[»]
1EGEX-ray2.75A/B/C/D26-421[»]
1T9GX-ray2.90A/B/C/D26-421[»]
2A1TX-ray2.80A/B/C/D1-421[»]
ProteinModelPortalP11310.
SMRP11310. Positions 35-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106552. 10 interactions.
DIPDIP-34281N.
IntActP11310. 6 interactions.
MINTMINT-3007693.
STRING9606.ENSP00000409612.

PTM databases

PhosphoSiteP11310.

Polymorphism databases

DMDM113017.

2D gel databases

REPRODUCTION-2DPAGEIPI00005040.
UCD-2DPAGEP11310.

Proteomic databases

PaxDbP11310.
PRIDEP11310.

Protocols and materials databases

DNASU34.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370841; ENSP00000359878; ENSG00000117054. [P11310-1]
ENST00000420607; ENSP00000409612; ENSG00000117054. [P11310-2]
GeneID34.
KEGGhsa:34.
UCSCuc001dgw.4. human. [P11310-1]
uc009wbp.3. human. [P11310-2]

Organism-specific databases

CTD34.
GeneCardsGC01P076190.
HGNCHGNC:89. ACADM.
HPAHPA006198.
HPA026542.
MIM201450. phenotype.
607008. gene.
neXtProtNX_P11310.
Orphanet42. Medium chain acyl-CoA dehydrogenase deficiency.
PharmGKBPA24425.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1960.
HOGENOMHOG000131659.
HOVERGENHBG000224.
KOK00249.
OrthoDBEOG74FF0S.
PhylomeDBP11310.
TreeFamTF105020.

Enzyme and pathway databases

BioCycMetaCyc:HS04089-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP11310.
UniPathwayUPA00660.

Gene expression databases

ArrayExpressP11310.
BgeeP11310.
CleanExHS_ACADM.
GenevestigatorP11310.

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. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11310.
GenomeRNAi34.
NextBio131.
PROP11310.
SOURCESearch...

Entry information

Entry nameACADM_HUMAN
AccessionPrimary (citable) accession number: P11310
Secondary accession number(s): Q5T4U4, Q9NYF1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 171 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

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 1

Human chromosome 1: entries, gene names and cross-references to MIM