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Protein

Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

ACADM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acyl-CoA dehydrogenase specific for acyl chain lengths of 4 to 16 that catalyzes the initial step of fatty acid beta-oxidation. Utilizes the electron transfer flavoprotein (ETF) as an electron acceptor to transfer electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).1 Publication

Catalytic activityi

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

Cofactori

FAD1 Publication

Pathwayi: mitochondrial fatty acid beta-oxidation

This protein is involved in the pathway mitochondrial fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway mitochondrial fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei167Substrate; via carbonyl oxygen1
Binding sitei216Substrate1
Active sitei401Proton acceptor1
Binding sitei402Substrate; via amide nitrogen1
Binding sitei413Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi158 – 167FAD1 Publication10
Nucleotide bindingi191 – 193FAD1 Publication3
Nucleotide bindingi306 – 308FAD1 Publication3
Nucleotide bindingi316 – 317FAD1 Publication2
Nucleotide bindingi374 – 378FAD1 Publication5
Nucleotide bindingi403 – 405FAD1 Publication3

GO - Molecular functioni

GO - Biological processi

  • carnitine biosynthetic process Source: BHF-UCL
  • carnitine metabolic process, CoA-linked Source: BHF-UCL
  • fatty acid beta-oxidation Source: UniProtKB
  • fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: UniProtKB
  • lipid homeostasis Source: GO_Central
  • medium-chain fatty acid catabolic process Source: BHF-UCL
  • medium-chain fatty acid metabolic process Source: BHF-UCL
  • oxidation-reduction process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:HS04089-MONOMER.
ZFISH:HS04089-MONOMER.
ReactomeiR-HSA-1989781. PPARA activates gene expression.
R-HSA-77288. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
R-HSA-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-HSA-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
SABIO-RKP11310.
UniPathwayiUPA00660.

Chemistry databases

SwissLipidsiSLP:000001334.

Names & Taxonomyi

Protein namesi
Recommended name:
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.7)
Short name:
MCAD
Gene namesi
Name:ACADM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:89. ACADM.

Subcellular locationi

GO - Cellular componenti

  • axon Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: LIFEdb
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Acyl-CoA dehydrogenase medium-chain deficiency (ACADMD)14 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn inborn error of mitochondrial fatty acid beta-oxidation which causes fasting hypoglycemia, hepatic dysfunction and encephalopathy, often resulting in death in infancy.
See also OMIM:201450
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00031753R → C in ACADMD. Corresponds to variant rs398123072dbSNPEnsembl.1
Natural variantiVAR_01369867Y → H in ACADMD; mild. 1 PublicationCorresponds to variant rs121434280dbSNPEnsembl.1
Natural variantiVAR_01595478I → T in ACADMD. 1 PublicationCorresponds to variant rs398123074dbSNPEnsembl.1
Natural variantiVAR_000318115 – 116Missing in ACADMD. 1 Publication2
Natural variantiVAR_015955116C → Y in ACADMD. 1 Publication1
Natural variantiVAR_015956121T → I in ACADMD. 1 PublicationCorresponds to variant rs121434283dbSNPEnsembl.1
Natural variantiVAR_000319149M → I in ACADMD. 1 PublicationCorresponds to variant rs121434277dbSNPEnsembl.1
Natural variantiVAR_000320193T → A in ACADMD; the thermostability is markedly decreased. 2 PublicationsCorresponds to variant rs121434279dbSNPEnsembl.1
Natural variantiVAR_000321195G → R in ACADMD. 1 PublicationCorresponds to variant rs121434278dbSNPEnsembl.1
Natural variantiVAR_015957206R → L in ACADMD. 1 Publication1
Natural variantiVAR_000322244C → R in ACADMD. 1 PublicationCorresponds to variant rs121434276dbSNPEnsembl.1
Natural variantiVAR_013699245S → L in ACADMD. 1 PublicationCorresponds to variant rs121434281dbSNPEnsembl.1
Natural variantiVAR_000323267G → R in ACADMD. 1 PublicationCorresponds to variant rs121434274dbSNPEnsembl.1
Natural variantiVAR_013700281R → T in ACADMD; mild or benign clinical phenotype. 1 PublicationCorresponds to variant rs121434282dbSNPEnsembl.1
Natural variantiVAR_015958310G → R in ACADMD. 1 PublicationCorresponds to variant rs747268471dbSNPEnsembl.1
Natural variantiVAR_000324326M → T in ACADMD. 1 PublicationCorresponds to variant rs786204631dbSNPEnsembl.1
Natural variantiVAR_000325329K → E in ACADMD; most common variant. 6 PublicationsCorresponds to variant rs77931234dbSNPEnsembl.1
Natural variantiVAR_000326336S → R in ACADMD. 1 Publication1
Natural variantiVAR_015959352Y → C in ACADMD. 1 Publication1
Natural variantiVAR_000327375I → T in ACADMD. 1 PublicationCorresponds to variant rs121434275dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi86L → M: Strongly reduced rate of electron transfer to ETF. 1 Publication1
Mutagenesisi98L → W: Strongly reduced rate of electron transfer to ETF. 1 Publication1
Mutagenesisi100L → Y: Strongly reduced rate of electron transfer to ETF. 1 Publication1
Mutagenesisi108I → M: Strongly reduced rate of electron transfer to ETF. 1 Publication1
Mutagenesisi191W → A: Loss of electron transfer to ETF. 1 Publication1
Mutagenesisi191W → F: Reduces rate of electron transfer to ETF about six-fold. 1 Publication1
Mutagenesisi237E → A: Strongly reduced rate of electron transfer to ETF. 2 Publications1
Mutagenesisi384E → A: Reduces rate of electron transfer to ETF three-fold. 2 Publications1
Mutagenesisi384E → Q: Reduces rate of electron transfer to ETF two-fold. 2 Publications1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi34.
MalaCardsiACADM.
MIMi201450. phenotype.
OpenTargetsiENSG00000117054.
Orphaneti42. Medium chain acyl-CoA dehydrogenase deficiency.
PharmGKBiPA24425.

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

Polymorphism and mutation databases

BioMutaiACADM.
DMDMi113017.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 25MitochondrionAdd BLAST25
ChainiPRO_000000050226 – 421Medium-chain specific acyl-CoA dehydrogenase, mitochondrialAdd BLAST396

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei69N6-acetyllysine; alternateBy similarity1
Modified residuei69N6-succinyllysine; alternateBy similarity1
Modified residuei179N6-succinyllysineBy similarity1
Modified residuei212N6-acetyllysine; alternateBy similarity1
Modified residuei212N6-succinyllysine; alternateBy similarity1
Modified residuei217N6-acetyllysine; alternateBy similarity1
Modified residuei217N6-succinyllysine; alternateBy similarity1
Modified residuei259N6-acetyllysine; alternateBy similarity1
Modified residuei259N6-succinyllysine; alternateBy similarity1
Modified residuei271N6-acetyllysine; alternateBy similarity1
Modified residuei271N6-succinyllysine; alternateBy similarity1
Modified residuei279N6-acetyllysineCombined sources1
Modified residuei301N6-acetyllysineCombined sources1
Modified residuei351PhosphothreonineBy similarity1

Post-translational modificationi

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.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP11310.
MaxQBiP11310.
PaxDbiP11310.
PeptideAtlasiP11310.
PRIDEiP11310.

2D gel databases

REPRODUCTION-2DPAGEIPI00005040.
UCD-2DPAGEP11310.

PTM databases

iPTMnetiP11310.
PhosphoSitePlusiP11310.
SwissPalmiP11310.

Expressioni

Gene expression databases

BgeeiENSG00000117054.
CleanExiHS_ACADM.
ExpressionAtlasiP11310. baseline and differential.
GenevisibleiP11310. HS.

Organism-specific databases

HPAiHPA006198.
HPA026542.

Interactioni

Subunit structurei

Homotetramer. Interacts with the heterodimeric electron transfer flavoprotein ETF.3 Publications

GO - Molecular functioni

  • identical protein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi106552. 50 interactors.
DIPiDIP-34281N.
IntActiP11310. 9 interactors.
MINTiMINT-3007693.
STRINGi9606.ENSP00000409612.

Structurei

Secondary structure

1421
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 38Combined sources3
Helixi43 – 58Combined sources16
Helixi61 – 70Combined sources10
Helixi75 – 83Combined sources9
Helixi93 – 95Combined sources3
Helixi102 – 115Combined sources14
Helixi117 – 136Combined sources20
Helixi139 – 145Combined sources7
Helixi147 – 151Combined sources5
Beta strandi155 – 159Combined sources5
Beta strandi165 – 167Combined sources3
Helixi169 – 171Combined sources3
Beta strandi175 – 179Combined sources5
Beta strandi182 – 193Combined sources12
Turni194 – 197Combined sources4
Beta strandi198 – 206Combined sources9
Helixi215 – 218Combined sources4
Beta strandi219 – 225Combined sources7
Beta strandi231 – 236Combined sources6
Beta strandi239 – 241Combined sources3
Beta strandi247 – 258Combined sources12
Helixi259 – 261Combined sources3
Beta strandi262 – 265Combined sources4
Turni266 – 268Combined sources3
Helixi269 – 303Combined sources35
Beta strandi309 – 312Combined sources4
Helixi313 – 315Combined sources3
Helixi317 – 345Combined sources29
Helixi351 – 376Combined sources26
Helixi377 – 381Combined sources5
Helixi387 – 394Combined sources8
Helixi395 – 398Combined sources4
Beta strandi400 – 402Combined sources3
Helixi404 – 417Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4P13X-ray1.73A/B/C/D35-421[»]
ProteinModelPortaliP11310.
SMRiP11310.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11310.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni278 – 281Substrate binding4

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0140. Eukaryota.
COG1960. LUCA.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiP11310.
KOiK00249.
PhylomeDBiP11310.
TreeFamiTF105020.

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. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P11310-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAGFGRCCR VLRSISRFHW RSQHTKANRQ REPGLGFSFE FTEQQKEFQA
60 70 80 90 100
TARKFAREEI IPVAAEYDKT GEYPVPLIRR AWELGLMNTH IPENCGGLGL
110 120 130 140 150
GTFDACLISE ELAYGCTGVQ TAIEGNSLGQ MPIIIAGNDQ QKKKYLGRMT
160 170 180 190 200
EEPLMCAYCV TEPGAGSDVA GIKTKAEKKG DEYIINGQKM WITNGGKANW
210 220 230 240 250
YFLLARSDPD PKAPANKAFT GFIVEADTPG IQIGRKELNM GQRCSDTRGI
260 270 280 290 300
VFEDVKVPKE NVLIGDGAGF KVAMGAFDKT RPVVAAGAVG LAQRALDEAT
310 320 330 340 350
KYALERKTFG KLLVEHQAIS FMLAEMAMKV ELARMSYQRA AWEVDSGRRN
360 370 380 390 400
TYYASIAKAF AGDIANQLAT DAVQILGGNG FNTEYPVEKL MRDAKIYQIY
410 420
EGTSQIQRLI VAREHIDKYK N
Length:421
Mass (Da):46,588
Last modified:July 1, 1989 - v1
Checksum:i7CD0B5832410581B
GO
Isoform 2 (identifier: P11310-2) [UniParc]FASTAAdd to basket

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

Show »
Length:425
Mass (Da):47,020
Checksum:iC6A133404E1B6E70
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti356I → T in AAF63626 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00031753R → C in ACADMD. Corresponds to variant rs398123072dbSNPEnsembl.1
Natural variantiVAR_01369867Y → H in ACADMD; mild. 1 PublicationCorresponds to variant rs121434280dbSNPEnsembl.1
Natural variantiVAR_01595478I → T in ACADMD. 1 PublicationCorresponds to variant rs398123074dbSNPEnsembl.1
Natural variantiVAR_000318115 – 116Missing in ACADMD. 1 Publication2
Natural variantiVAR_015955116C → Y in ACADMD. 1 Publication1
Natural variantiVAR_015956121T → I in ACADMD. 1 PublicationCorresponds to variant rs121434283dbSNPEnsembl.1
Natural variantiVAR_035716132P → R in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_000319149M → I in ACADMD. 1 PublicationCorresponds to variant rs121434277dbSNPEnsembl.1
Natural variantiVAR_000320193T → A in ACADMD; the thermostability is markedly decreased. 2 PublicationsCorresponds to variant rs121434279dbSNPEnsembl.1
Natural variantiVAR_000321195G → R in ACADMD. 1 PublicationCorresponds to variant rs121434278dbSNPEnsembl.1
Natural variantiVAR_015957206R → L in ACADMD. 1 Publication1
Natural variantiVAR_000322244C → R in ACADMD. 1 PublicationCorresponds to variant rs121434276dbSNPEnsembl.1
Natural variantiVAR_013699245S → L in ACADMD. 1 PublicationCorresponds to variant rs121434281dbSNPEnsembl.1
Natural variantiVAR_000323267G → R in ACADMD. 1 PublicationCorresponds to variant rs121434274dbSNPEnsembl.1
Natural variantiVAR_013700281R → T in ACADMD; mild or benign clinical phenotype. 1 PublicationCorresponds to variant rs121434282dbSNPEnsembl.1
Natural variantiVAR_015958310G → R in ACADMD. 1 PublicationCorresponds to variant rs747268471dbSNPEnsembl.1
Natural variantiVAR_000324326M → T in ACADMD. 1 PublicationCorresponds to variant rs786204631dbSNPEnsembl.1
Natural variantiVAR_000325329K → E in ACADMD; most common variant. 6 PublicationsCorresponds to variant rs77931234dbSNPEnsembl.1
Natural variantiVAR_000326336S → R in ACADMD. 1 Publication1
Natural variantiVAR_015959352Y → C in ACADMD. 1 Publication1
Natural variantiVAR_000327375I → T in ACADMD. 1 PublicationCorresponds to variant rs121434275dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_03842010R → RCSLQ in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
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.
CCDSiCCDS44165.1. [P11310-2]
CCDS668.1. [P11310-1]
PIRiA29031. DEHUCM.
RefSeqiNP_000007.1. NM_000016.5. [P11310-1]
NP_001120800.1. NM_001127328.2. [P11310-2]
UniGeneiHs.445040.

Genome annotation databases

EnsembliENST00000370841; ENSP00000359878; ENSG00000117054. [P11310-1]
ENST00000420607; ENSP00000409612; ENSG00000117054. [P11310-2]
GeneIDi34.
KEGGihsa:34.
UCSCiuc001dgw.6. human. [P11310-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
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.
CCDSiCCDS44165.1. [P11310-2]
CCDS668.1. [P11310-1]
PIRiA29031. DEHUCM.
RefSeqiNP_000007.1. NM_000016.5. [P11310-1]
NP_001120800.1. NM_001127328.2. [P11310-2]
UniGeneiHs.445040.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4P13X-ray1.73A/B/C/D35-421[»]
ProteinModelPortaliP11310.
SMRiP11310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106552. 50 interactors.
DIPiDIP-34281N.
IntActiP11310. 9 interactors.
MINTiMINT-3007693.
STRINGi9606.ENSP00000409612.

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.
SwissLipidsiSLP:000001334.

PTM databases

iPTMnetiP11310.
PhosphoSitePlusiP11310.
SwissPalmiP11310.

Polymorphism and mutation databases

BioMutaiACADM.
DMDMi113017.

2D gel databases

REPRODUCTION-2DPAGEIPI00005040.
UCD-2DPAGEP11310.

Proteomic databases

EPDiP11310.
MaxQBiP11310.
PaxDbiP11310.
PeptideAtlasiP11310.
PRIDEiP11310.

Protocols and materials databases

DNASUi34.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370841; ENSP00000359878; ENSG00000117054. [P11310-1]
ENST00000420607; ENSP00000409612; ENSG00000117054. [P11310-2]
GeneIDi34.
KEGGihsa:34.
UCSCiuc001dgw.6. human. [P11310-1]

Organism-specific databases

CTDi34.
DisGeNETi34.
GeneCardsiACADM.
GeneReviewsiACADM.
HGNCiHGNC:89. ACADM.
HPAiHPA006198.
HPA026542.
MalaCardsiACADM.
MIMi201450. phenotype.
607008. gene.
neXtProtiNX_P11310.
OpenTargetsiENSG00000117054.
Orphaneti42. Medium chain acyl-CoA dehydrogenase deficiency.
PharmGKBiPA24425.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0140. Eukaryota.
COG1960. LUCA.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiP11310.
KOiK00249.
PhylomeDBiP11310.
TreeFamiTF105020.

Enzyme and pathway databases

UniPathwayiUPA00660.
BioCyciMetaCyc:HS04089-MONOMER.
ZFISH:HS04089-MONOMER.
ReactomeiR-HSA-1989781. PPARA activates gene expression.
R-HSA-77288. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
R-HSA-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-HSA-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
SABIO-RKP11310.

Miscellaneous databases

EvolutionaryTraceiP11310.
GenomeRNAii34.
PROiP11310.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000117054.
CleanExiHS_ACADM.
ExpressionAtlasiP11310. baseline and differential.
GenevisibleiP11310. HS.

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. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACADM_HUMAN
AccessioniPrimary (citable) accession number: P11310
Secondary accession number(s): Q5T4U4, Q9NYF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 2, 2016
This is version 196 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.