Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Short-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

Acads

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Introduces a double bond at position 2 in saturated acyl-CoA's of short chain length, i.e. less than 6 carbon atoms.By similarity

Miscellaneous

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

Catalytic activityi

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

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

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 sitei161Substrate; via carbonyl oxygenBy similarity1
Binding sitei297FADBy similarity1
Binding sitei297FAD; shared with dimeric partnerBy similarity1
Binding sitei308FADBy similarity1
Active sitei392Proton acceptorBy similarity1
Binding sitei393Substrate; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi152 – 161FADBy similarity10
Nucleotide bindingi185 – 187FADBy similarity3
Nucleotide bindingi365 – 369FADBy similarity5
Nucleotide bindingi394 – 396FADBy similarity3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processFatty acid metabolism, Lipid metabolism
LigandFAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-MMU-77350 Beta oxidation of hexanoyl-CoA to butanoyl-CoA
R-MMU-77352 Beta oxidation of butanoyl-CoA to acetyl-CoA
UniPathwayiUPA00660

Names & Taxonomyi

Protein namesi
Recommended name:
Short-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.1)
Short name:
SCAD
Alternative name(s):
Butyryl-CoA dehydrogenase
Gene namesi
Name:Acads
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:87868 Acads

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 24MitochondrionBy similarityAdd BLAST24
ChainiPRO_000000049925 – 412Short-chain specific acyl-CoA dehydrogenase, mitochondrialAdd BLAST388

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei27PhosphothreonineCombined sources1
Modified residuei51N6-acetyllysine; alternateCombined sources1
Modified residuei51N6-succinyllysine; alternateCombined sources1
Modified residuei72N6-acetyllysineCombined sources1
Modified residuei129N6-acetyllysine; alternateCombined sources1
Modified residuei129N6-succinyllysine; alternateCombined sources1
Modified residuei208N6-acetyllysineCombined sources1
Modified residuei262N6-acetyllysine; alternateCombined sources1
Modified residuei262N6-succinyllysine; alternateCombined sources1
Modified residuei292N6-acetyllysineCombined sources1
Modified residuei306N6-acetyllysine; alternateCombined sources1
Modified residuei306N6-succinyllysine; alternateCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ07417
MaxQBiQ07417
PaxDbiQ07417
PeptideAtlasiQ07417
PRIDEiQ07417

2D gel databases

REPRODUCTION-2DPAGEQ07417

PTM databases

iPTMnetiQ07417
PhosphoSitePlusiQ07417
SwissPalmiQ07417

Expressioni

Gene expression databases

BgeeiENSMUSG00000029545
CleanExiMM_ACADS
GenevisibleiQ07417 MM

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi197915, 1 interactor
IntActiQ07417, 5 interactors
MINTiQ07417
STRINGi10090.ENSMUSP00000031524

Structurei

3D structure databases

ProteinModelPortaliQ07417
SMRiQ07417
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni269 – 272Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0139 Eukaryota
COG1960 LUCA
GeneTreeiENSGT00760000119007
HOGENOMiHOG000131659
HOVERGENiHBG000224
InParanoidiQ07417
KOiK00248
OMAiTNSWEAS
OrthoDBiEOG091G04BS
TreeFamiTF105019

Family and domain databases

Gene3Di1.10.540.10, 1 hit
InterProiView protein in InterPro
IPR006089 Acyl-CoA_DH_CS
IPR006091 Acyl-CoA_Oxase/DH_cen-dom
IPR036250 AcylCo_DH-like_C
IPR009075 AcylCo_DH/oxidase_C
IPR013786 AcylCoA_DH/ox_N
IPR037069 AcylCoA_DH/ox_N_sf
IPR009100 AcylCoA_DH/oxidase_NM_dom
PfamiView protein in Pfam
PF00441 Acyl-CoA_dh_1, 1 hit
PF02770 Acyl-CoA_dh_M, 1 hit
PF02771 Acyl-CoA_dh_N, 1 hit
SUPFAMiSSF47203 SSF47203, 1 hit
SSF56645 SSF56645, 1 hit
PROSITEiView protein in PROSITE
PS00072 ACYL_COA_DH_1, 1 hit
PS00073 ACYL_COA_DH_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q07417-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAALLARAR GPLRRALGVR DWRRLHTVYQ SVELPETHQM LRQTCRDFAE
60 70 80 90 100
KELVPIAAQL DREHLFPTAQ VKKMGELGLL AMDVPEELSG AGLDYLAYSI
110 120 130 140 150
ALEEISRACA STGVIMSVNN SLYLGPILKF GSAQQKQQWI TPFTNGDKIG
160 170 180 190 200
CFALSEPGNG SDAGAASTTA REEGDSWVLN GTKAWITNSW EASATVVFAS
210 220 230 240 250
TDRSRQNKGI SAFLVPMPTP GLTLGKKEDK LGIRASSTAN LIFEDCRIPK
260 270 280 290 300
ENLLGEPGMG FKIAMQTLDM GRIGIASQAL GIAQASLDCA VKYAENRNAF
310 320 330 340 350
GAPLTKLQNI QFKLADMALA LESARLLTWR AAMLKDNKKP FTKESAMAKL
360 370 380 390 400
AASEAATAIS HQAIQILGGM GYVTEMPAER YYRDARITEI YEGTSEIQRL
410
VIAGHLLRSY RS
Length:412
Mass (Da):44,890
Last modified:July 27, 2011 - v2
Checksum:i53DDE98661DF6333
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti94D → G in AAA16714 (PubMed:8276399).Curated1
Sequence conflicti348A → R in AAA16714 (PubMed:8276399).Curated1
Sequence conflicti369G → S in AAA16714 (PubMed:8276399).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11163 mRNA Translation: AAA16714.1
AK155361 mRNA Translation: BAE33217.1
AK169428 mRNA Translation: BAE41170.1
CH466529 Genomic DNA Translation: EDL19883.1
BC016259 mRNA Translation: AAH16259.1
CCDSiCCDS19579.1
PIRiI49605
RefSeqiNP_031409.2, NM_007383.3
UniGeneiMm.18759

Genome annotation databases

EnsembliENSMUST00000031524; ENSMUSP00000031524; ENSMUSG00000029545
GeneIDi11409
KEGGimmu:11409
UCSCiuc008zdb.2 mouse

Similar proteinsi

Entry informationi

Entry nameiACADS_MOUSE
AccessioniPrimary (citable) accession number: Q07417
Secondary accession number(s): Q91W85
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 27, 2011
Last modified: May 23, 2018
This is version 155 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health