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P45952

- ACADM_MOUSE

UniProt

P45952 - ACADM_MOUSE

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Protein
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Gene
Acadm
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

FAD By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei167 – 1671Substrate; via carbonyl oxygen By similarity
Active sitei401 – 4011Proton acceptor By similarity
Binding sitei402 – 4021Substrate; via amide nitrogen By similarity
Binding sitei413 – 4131Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi158 – 16710FAD By similarity
Nucleotide bindingi191 – 1933FAD By similarity
Nucleotide bindingi306 – 3083FAD By similarity
Nucleotide bindingi316 – 3172FAD By similarity
Nucleotide bindingi374 – 3785FAD By similarity
Nucleotide bindingi403 – 4053FAD By similarity

GO - Molecular functioni

  1. acyl-CoA dehydrogenase activity Source: UniProtKB
  2. flavin adenine dinucleotide binding Source: InterPro
  3. medium-chain-acyl-CoA dehydrogenase activity Source: BHF-UCL

GO - Biological processi

  1. cardiac muscle cell differentiation Source: MGI
  2. carnitine biosynthetic process Source: Ensembl
  3. carnitine metabolic process Source: MGI
  4. carnitine metabolic process, CoA-linked Source: BHF-UCL
  5. fatty acid beta-oxidation Source: UniProtKB
  6. fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: BHF-UCL
  7. glycogen biosynthetic process Source: BHF-UCL
  8. heart development Source: MGI
  9. liver development Source: MGI
  10. medium-chain fatty acid catabolic process Source: Ensembl
  11. medium-chain fatty acid metabolic process Source: BHF-UCL
  12. organic acid metabolic process Source: MGI
  13. post-embryonic development Source: MGI
  14. regulation of gluconeogenesis Source: BHF-UCL
  15. response to cold Source: MGI
  16. response to starvation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiREACT_198602. PPARA activates gene expression.
UniPathwayiUPA00660.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:87867. Acadm.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. axon Source: Ensembl
  2. mitochondrial matrix Source: UniProtKB-SubCell
  3. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2525Mitochondrion By similarity
Add
BLAST
Chaini26 – 421396Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000000504Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301N6-acetyllysine; alternate1 Publication
Modified residuei30 – 301N6-succinyllysine; alternate1 Publication
Modified residuei69 – 691N6-acetyllysine; alternate1 Publication
Modified residuei69 – 691N6-succinyllysine; alternate1 Publication
Modified residuei79 – 791N6-acetyllysine1 Publication
Modified residuei179 – 1791N6-succinyllysine1 Publication
Modified residuei212 – 2121N6-acetyllysine; alternate1 Publication
Modified residuei212 – 2121N6-succinyllysine; alternate1 Publication
Modified residuei217 – 2171N6-acetyllysine; alternate1 Publication
Modified residuei217 – 2171N6-succinyllysine; alternate1 Publication
Modified residuei235 – 2351N6-acetyllysine; alternate1 Publication
Modified residuei235 – 2351N6-succinyllysine; alternate1 Publication
Modified residuei259 – 2591N6-acetyllysine; alternate1 Publication
Modified residuei259 – 2591N6-succinyllysine; alternate1 Publication
Modified residuei271 – 2711N6-acetyllysine; alternate1 Publication
Modified residuei271 – 2711N6-succinyllysine; alternate1 Publication
Modified residuei301 – 3011N6-acetyllysine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP45952.
PaxDbiP45952.
PRIDEiP45952.

2D gel databases

SWISS-2DPAGEP45952.

PTM databases

PhosphoSiteiP45952.

Expressioni

Gene expression databases

ArrayExpressiP45952.
BgeeiP45952.
CleanExiMM_ACADM.
GenevestigatoriP45952.

Interactioni

Subunit structurei

Homotetramer By similarity.

Protein-protein interaction databases

IntActiP45952. 2 interactions.
MINTiMINT-1860219.

Structurei

3D structure databases

ProteinModelPortaliP45952.
SMRiP45952. Positions 35-421.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni278 – 2814Substrate binding By similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1960.
GeneTreeiENSGT00750000117417.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiP45952.
KOiK00249.
OMAiSAWEVDQ.
OrthoDBiEOG74FF0S.
PhylomeDBiP45952.
TreeFamiTF105020.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
2.40.110.10. 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]

Sequencei

Sequence statusi: Complete.

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

P45952-1 [UniParc]FASTAAdd to Basket

« Hide

MAAAFRRGCR VLRSVSHFEC RTQHSKAAHK QEPGLGFSFE LTEQQKEFQA    50
TARKFAREEI IPVAPEYDKS GEYPFPLIKR AWELGLINAH IPESCGGLGL 100
GTFDACLITE ELAYGCTGVQ TAIEANSLGQ MPVILAGNDQ QKKKYLGRMT 150
EQPMMCAYCV TEPSAGSDVA AIKTKAEKKG DEYVINGQKM WITNGGKANW 200
YFLLARSNPD PKVPASKAFT GFIVEADTPG IHIGKKELNM GQRCSDTRGI 250
AFEDVRVPKE NVLIGEGAGF KIAMGAFDRT RPTVAAGAVG LAQRALDEAT 300
KYALDRKTFG KLLVEHQGVS FLLAEMAMKV ELARLSYQRA AWEVDSGRRN 350
TYYASIAKAF AGDIANQLAT DAVQIFGGYG FNTEYPVEKL MRDAKIYQIY 400
EGTAQIQRLI IAREHIEKYK N 421
Length:421
Mass (Da):46,481
Last modified:November 1, 1995 - v1
Checksum:i36976704E3E48CBB
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351L → I in S48759. 1 Publication
Sequence conflicti184 – 1841V → A in S48761. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U07159 mRNA. Translation: AAA76733.1.
S48761 Genomic DNA. No translation available.
S48759 Genomic DNA. No translation available.
CCDSiCCDS17924.1.
PIRiA55724.
RefSeqiNP_031408.1. NM_007382.5.
UniGeneiMm.10530.

Genome annotation databases

EnsembliENSMUST00000072697; ENSMUSP00000072483; ENSMUSG00000062908.
GeneIDi11364.
KEGGimmu:11364.
UCSCiuc008ruj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U07159 mRNA. Translation: AAA76733.1 .
S48761 Genomic DNA. No translation available.
S48759 Genomic DNA. No translation available.
CCDSi CCDS17924.1.
PIRi A55724.
RefSeqi NP_031408.1. NM_007382.5.
UniGenei Mm.10530.

3D structure databases

ProteinModelPortali P45952.
SMRi P45952. Positions 35-421.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P45952. 2 interactions.
MINTi MINT-1860219.

PTM databases

PhosphoSitei P45952.

2D gel databases

SWISS-2DPAGE P45952.

Proteomic databases

MaxQBi P45952.
PaxDbi P45952.
PRIDEi P45952.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000072697 ; ENSMUSP00000072483 ; ENSMUSG00000062908 .
GeneIDi 11364.
KEGGi mmu:11364.
UCSCi uc008ruj.1. mouse.

Organism-specific databases

CTDi 34.
MGIi MGI:87867. Acadm.

Phylogenomic databases

eggNOGi COG1960.
GeneTreei ENSGT00750000117417.
HOGENOMi HOG000131659.
HOVERGENi HBG000224.
InParanoidi P45952.
KOi K00249.
OMAi SAWEVDQ.
OrthoDBi EOG74FF0S.
PhylomeDBi P45952.
TreeFami TF105020.

Enzyme and pathway databases

UniPathwayi UPA00660 .
Reactomei REACT_198602. PPARA activates gene expression.

Miscellaneous databases

NextBioi 278640.
PROi P45952.
SOURCEi Search...

Gene expression databases

ArrayExpressi P45952.
Bgeei P45952.
CleanExi MM_ACADM.
Genevestigatori P45952.

Family and domain databases

Gene3Di 1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProi IPR006089. 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 ]
Pfami PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEi PS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of the mouse medium-chain acyl-CoA dehydrogenase cDNA."
    Tolwani R.J., Farmer S.C., Wood P.A.
    Genomics 23:247-249(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Liver.
  2. "Molecular studies of mouse medium and long-chain acyl-CoA dehydrogenase genes for site-directed mutagenesis of embryonic stem cells."
    Wood P.A., Farmer S.C., Tolwani R.J., Warren J.R., Steinkampf M.P., Johnson L.W., Mountz J.D., Kelly D.P.
    Prog. Clin. Biol. Res. 375:151-160(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-193.
  3. "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-30; LYS-69; LYS-179; LYS-212; LYS-217; LYS-235; LYS-259 AND LYS-271, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "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-30; LYS-69; LYS-79; LYS-212; LYS-217; LYS-235; LYS-259; LYS-271 AND LYS-301, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiACADM_MOUSE
AccessioniPrimary (citable) accession number: P45952
Secondary accession number(s): Q64235
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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