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Protein

Very long-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

Acadvl

Organism
Rattus norvegicus (Rat)
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.

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 sitei223Substrate; via carbonyl oxygenBy similarity1
Binding sitei366FADBy similarity1
Active sitei462Proton acceptorBy similarity1
Binding sitei463Substrate; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi214 – 223FADBy similarity10
Nucleotide bindingi249 – 251FADBy similarity3
Nucleotide bindingi435 – 439FADBy similarity5
Nucleotide bindingi464 – 466FADBy similarity3

GO - Molecular functioni

  • acyl-CoA dehydrogenase activity Source: RGD
  • fatty-acyl-CoA binding Source: RGD
  • flavin adenine dinucleotide binding Source: RGD
  • long-chain-acyl-CoA dehydrogenase activity Source: RGD
  • very-long-chain-acyl-CoA dehydrogenase activity Source: RGD

GO - Biological processi

  • fatty acid beta-oxidation Source: RGD
  • fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: RGD
  • very long-chain fatty acid catabolic process Source: RGD

Keywordsi

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

Enzyme and pathway databases

UniPathwayiUPA00660

Chemistry databases

SwissLipidsiSLP:000001587

Names & Taxonomyi

Protein namesi
Recommended name:
Very long-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.9)
Short name:
VLCAD
Gene namesi
Name:Acadvl
Synonyms:Vlcad
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2014 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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2176830

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 40MitochondrionAdd BLAST40
ChainiPRO_000000051841 – 655Very long-chain specific acyl-CoA dehydrogenase, mitochondrialAdd BLAST615

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei51N6-acetyllysineBy similarity1
Modified residuei71N6-acetyllysine; alternateBy similarity1
Modified residuei71N6-succinyllysine; alternateBy similarity1
Modified residuei127N6-acetyllysine; alternateBy similarity1
Modified residuei127N6-succinyllysine; alternateBy similarity1
Modified residuei195N6-succinyllysineBy similarity1
Modified residuei237S-nitrosocysteineBy similarity1
Modified residuei239N6-acetyllysine; alternateBy similarity1
Modified residuei239N6-succinyllysine; alternateBy similarity1
Modified residuei268N6-succinyllysineBy similarity1
Modified residuei276N6-acetyllysine; alternateBy similarity1
Modified residuei276N6-succinyllysine; alternateBy similarity1
Modified residuei278N6-acetyllysine; alternateBy similarity1
Modified residuei278N6-succinyllysine; alternateBy similarity1
Modified residuei298N6-acetyllysineBy similarity1
Modified residuei316N6-acetyllysineBy similarity1
Modified residuei331N6-acetyllysine; alternateBy similarity1
Modified residuei331N6-succinyllysine; alternateBy similarity1
Modified residuei372N6-succinyllysineBy similarity1
Modified residuei482N6-acetyllysine; alternateBy similarity1
Modified residuei482N6-succinyllysine; alternateBy similarity1
Modified residuei517PhosphoserineBy similarity1
Modified residuei522PhosphoserineBy similarity1
Modified residuei550N6-acetyllysineBy similarity1
Modified residuei556N6-acetyllysine; alternateBy similarity1
Modified residuei556N6-succinyllysine; alternateBy similarity1
Modified residuei639N6-succinyllysineBy similarity1

Post-translational modificationi

S-nitrosylation at Cys-237 in liver improves catalytic efficiency.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

PaxDbiP45953
PRIDEiP45953

PTM databases

CarbonylDBiP45953
iPTMnetiP45953
PhosphoSitePlusiP45953

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000024973

Structurei

3D structure databases

ProteinModelPortaliP45953
SMRiP45953
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni41 – 482CatalyticAdd BLAST442
Regioni338 – 341Substrate bindingBy similarity4
Regioni462 – 463Substrate bindingBy similarity2
Regioni483 – 516Membrane-anchoringCuratedAdd BLAST34

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0137 Eukaryota
COG1960 LUCA
HOGENOMiHOG000131665
HOVERGENiHBG050448
InParanoidiP45953
KOiK09479
PhylomeDBiP45953

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.

P45953-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSARMTPSV GRQLLRLGAR SSRSAALQGQ PRPTSAQRLY ASEATQAVLE
60 70 80 90 100
KPETLSSDAS TREKPARAES KSFAVGMFKG QLTTDQVFPY PSVLNEGQTQ
110 120 130 140 150
FLKELVGPVA RFFEEVNDPA KNDSLEKVEE DTLQGLKELG AFGLQVPSEL
160 170 180 190 200
GGLGLSNTQY ARLAEIVGMH DLGVSVTLGA HQSIGFKGIL LYGTKAQKEK
210 220 230 240 250
YLPRVASGQA LAAFCLTEPS SGSDVASIRS SAVPSPCGKY YTLNGSKIWI
260 270 280 290 300
SNGGLADIFT VFAKTPIKDA ATGAVKEKIT AFVVERSFGG VTHGLPEKKM
310 320 330 340 350
GIKASNTSEV YFDGVKVPAE NVLGEVGDGF KVAVNILNNG RFGMAATLAG
360 370 380 390 400
TMKAIIAKAV DHATNRTQFG DKIHNFGVIQ EKLARMAILQ YVTESMAYML
410 420 430 440 450
SANMDQGFKD FQIEAAISKI FGSEAAWKVT DECIQIMGGM GFMKEPGVER
460 470 480 490 500
VLRDIRIFRI FEGTNDILRL FVALQGCMDK GKELTGLGNA LKNPLGNVGL
510 520 530 540 550
LIGEASKQLR RRTGIGSGLS LSGIVHPELS RSGELAVQAL EQFATVVEAK
560 570 580 590 600
LMKHKKGIVN EQFLLQRLAD GAIDLYAMVV VLSRASRSLS EGYPTAQHEK
610 620 630 640 650
MLCDSWCIEA ATRIRENMAS LQSNPQQQEL FRNFRSISKA MVENGGLVTS

NPLRV
Length:655
Mass (Da):70,749
Last modified:November 1, 1995 - v1
Checksum:iE808EDEB0E4595D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30647 mRNA Translation: BAA06331.1
PIRiA54872
RefSeqiNP_037023.1, NM_012891.2
UniGeneiRn.33319

Genome annotation databases

GeneIDi25363
KEGGirno:25363
UCSCiRGD:2014 rat

Similar proteinsi

Entry informationi

Entry nameiACADV_RAT
AccessioniPrimary (citable) accession number: P45953
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 23, 2018
This is version 139 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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