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

Very long-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

Acadvl

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

Functioni

Active toward esters of long-chain and very long chain fatty acids such as palmitoyl-CoA, mysritoyl-CoA and stearoyl-CoA. Can accommodate substrate acyl chain lengths as long as 24 carbons, but shows little activity for substrates of less than 12 carbons (By similarity).By similarity

Miscellaneous

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

Catalytic activityi

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

Cofactori

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 sitei224Substrate; via carbonyl oxygenBy similarity1
Binding sitei367FADBy similarity1
Active sitei463Proton acceptorBy similarity1
Binding sitei464Substrate; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi215 – 224FADBy similarity10
Nucleotide bindingi250 – 252FADBy similarity3
Nucleotide bindingi436 – 440FADBy similarity5
Nucleotide bindingi465 – 467FADBy similarity3

GO - Molecular functioni

GO - Biological processi

  • epithelial cell differentiation Source: Ensembl
  • fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: BHF-UCL
  • fatty acid catabolic process Source: MGI
  • negative regulation of fatty acid biosynthetic process Source: BHF-UCL
  • negative regulation of fatty acid oxidation Source: BHF-UCL
  • regulation of cholesterol metabolic process Source: BHF-UCL
  • response to cold Source: MGI
  • temperature homeostasis Source: BHF-UCL

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-MMU-77305 Beta oxidation of palmitoyl-CoA to myristoyl-CoA
UniPathwayiUPA00660

Names & Taxonomyi

Protein namesi
Recommended name:
Very long-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.9)
Alternative name(s):
MVLCAD
Short name:
VLCAD
Gene namesi
Name:Acadvl
Synonyms:Vlcad
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:895149 Acadvl

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

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 41MitochondrionBy similarityAdd BLAST41
ChainiPRO_000000051742 – 656Very long-chain specific acyl-CoA dehydrogenase, mitochondrialAdd BLAST615

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei52N6-acetyllysineCombined sources1
Modified residuei72N6-acetyllysine; alternateCombined sources1
Modified residuei72N6-succinyllysine; alternateCombined sources1
Modified residuei128N6-acetyllysine; alternateCombined sources1
Modified residuei128N6-succinyllysine; alternateCombined sources1
Modified residuei196N6-succinyllysineCombined sources1
Modified residuei238S-nitrosocysteine1 Publication1
Modified residuei240N6-acetyllysine; alternateCombined sources1
Modified residuei240N6-succinyllysine; alternateCombined sources1
Modified residuei269N6-succinyllysineCombined sources1
Modified residuei277N6-acetyllysine; alternateCombined sources1
Modified residuei277N6-succinyllysine; alternateCombined sources1
Modified residuei279N6-acetyllysine; alternateCombined sources1
Modified residuei279N6-succinyllysine; alternateCombined sources1
Modified residuei299N6-acetyllysineCombined sources1
Modified residuei317N6-acetyllysineCombined sources1
Modified residuei332N6-acetyllysine; alternateCombined sources1
Modified residuei332N6-succinyllysine; alternateCombined sources1
Modified residuei373N6-succinyllysineCombined sources1
Modified residuei483N6-acetyllysine; alternateCombined sources1
Modified residuei483N6-succinyllysine; alternateCombined sources1
Modified residuei518PhosphoserineBy similarity1
Modified residuei523PhosphoserineBy similarity1
Modified residuei551N6-acetyllysineCombined sources1
Modified residuei557N6-acetyllysine; alternateCombined sources1
Modified residuei557N6-succinyllysine; alternateCombined sources1
Modified residuei640N6-succinyllysineCombined sources1

Post-translational modificationi

S-nitrosylation at Cys-238 in liver improves catalytic efficiency.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

EPDiP50544
MaxQBiP50544
PaxDbiP50544
PeptideAtlasiP50544
PRIDEiP50544

2D gel databases

SWISS-2DPAGEP50544

PTM databases

iPTMnetiP50544
PhosphoSitePlusiP50544
SwissPalmiP50544

Expressioni

Gene expression databases

BgeeiENSMUSG00000018574
CleanExiMM_ACADVL
ExpressionAtlasiP50544 baseline and differential
GenevisibleiP50544 MM

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi197914, 2 interactors
IntActiP50544, 2 interactors
MINTiP50544
STRINGi10090.ENSMUSP00000099634

Structurei

3D structure databases

ProteinModelPortaliP50544
SMRiP50544
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni42 – 483CatalyticAdd BLAST442
Regioni339 – 342Substrate bindingBy similarity4
Regioni463 – 464Substrate bindingBy similarity2
Regioni484 – 517Membrane-anchoringCuratedAdd BLAST34

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0137 Eukaryota
COG1960 LUCA
GeneTreeiENSGT00760000119007
HOGENOMiHOG000131665
HOVERGENiHBG050448
InParanoidiP50544
KOiK09479
OMAiNAFMGLR
OrthoDBiEOG091G04BS
PhylomeDBiP50544
TreeFamiTF105053

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.

P50544-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSARMTPSV GRQLLRLGAR SSRSTTVLQG QPRPISAQRL YAREATQAVL
60 70 80 90 100
DKPETLSSDA STREKPARAE SKSFAVGMFK GQLTIDQVFP YPSVLSEEQA
110 120 130 140 150
QFLKELVGPV ARFFEEVNDP AKNDALEKVE DDTLQGLKEL GAFGLQVPSE
160 170 180 190 200
LGGLGLSNTQ YARLAEIVGM HDLGVSVTLG AHQSIGFKGI LLYGTKAQRE
210 220 230 240 250
KYLPRVASGQ ALAAFCLTEP SSGSDVASIR SSAIPSPCGK YYTLNGSKIW
260 270 280 290 300
ISNGGLADIF TVFAKTPIKD AATGAVKEKI TAFVVERSFG GVTHGLPEKK
310 320 330 340 350
MGIKASNTSE VYFDGVKVPS ENVLGEVGDG FKVAVNILNN GRFGMAATLA
360 370 380 390 400
GTMKSLIAKA VDHATNRTQF GDKIHNFGVI QEKLARMAIL QYVTESMAYM
410 420 430 440 450
LSANMDQGFK DFQIEAAISK IFCSEAAWKV ADECIQIMGG MGFMKEPGVE
460 470 480 490 500
RVLRDIRIFR IFEGANDILR LFVALQGCMD KGKELTGLGN ALKNPFGNVG
510 520 530 540 550
LLMGEAGKQL RRRTGIGSGL SLSGIVHPEL SRSGELAVQA LDQFATVVEA
560 570 580 590 600
KLVKHKKGIV NEQFLLQRLA DGAIDLYAMV VVLSRASRSL SEGYPTAQHE
610 620 630 640 650
KMLCDSWCIE AATRIRENMA SLQSSPQHQE LFRNFRSISK AMVENGGLVT

GNPLGI
Length:656
Mass (Da):70,875
Last modified:May 30, 2000 - v3
Checksum:iA0110CA5C6CF4F89
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti339 – 341NNG → GTR in AAA85185 (Ref. 5) Curated3
Sequence conflicti423C → W in AAA85185 (Ref. 5) Curated1
Sequence conflicti427A → G in AAA85185 (Ref. 5) Curated1
Sequence conflicti441M → I in AAA85185 (Ref. 5) Curated1
Sequence conflicti507G → A in AAA85185 (Ref. 5) Curated1
Sequence conflicti532R → P in AAA85185 (Ref. 5) Curated1
Sequence conflicti567Q → K in AAA85185 (Ref. 5) Curated1
Sequence conflicti570 – 571AD → GG in AAA85185 (Ref. 5) Curated2
Sequence conflicti573A → P in AAA85185 (Ref. 5) Curated1
Sequence conflicti593G → A in AAA85185 (Ref. 5) Curated1
Sequence conflicti596T → A in AAA85185 (Ref. 5) Curated1
Sequence conflicti612A → P in AAA85185 (Ref. 5) Curated1
Sequence conflicti628H → Q in AAC31642 (PubMed:9680378).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11770 Genomic DNA Translation: CAA72435.1
Z71189 mRNA Translation: CAA94919.2
BC026559 mRNA Translation: AAH26559.1
AF017176 mRNA Translation: AAC31642.1
U41497 mRNA Translation: AAA85185.1
CCDSiCCDS24931.1
RefSeqiNP_059062.1, NM_017366.3
UniGeneiMm.18630

Genome annotation databases

EnsembliENSMUST00000102574; ENSMUSP00000099634; ENSMUSG00000018574
GeneIDi11370
KEGGimmu:11370
UCSCiuc007jto.2 mouse

Similar proteinsi

Entry informationi

Entry nameiACADV_MOUSE
AccessioniPrimary (citable) accession number: P50544
Secondary accession number(s): O35289, O55133
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 30, 2000
Last modified: May 23, 2018
This is version 158 of the entry and version 3 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