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
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.

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
  • electron carrier activity Source: GO_Central
  • fatty-acyl-CoA binding Source: RGD
  • flavin adenine dinucleotide binding Source: RGD
  • long-chain-acyl-CoA dehydrogenase activity Source: RGD
  • oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor Source: GO_Central
  • 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
  • lipid homeostasis Source: GO_Central
  • very long-chain fatty acid catabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2014. Acadvl.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: RGD
  • mitochondrion Source: RGD
Complete GO annotation...

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

iPTMnetiP45953.
PhosphoSitePlusiP45953.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

MINTiMINT-4996754.
STRINGi10116.ENSRNOP00000024973.

Structurei

3D structure databases

ProteinModelPortaliP45953.
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.
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.

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP45953.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4996754.
STRINGi10116.ENSRNOP00000024973.

Chemistry databases

ChEMBLiCHEMBL2176830.
SwissLipidsiSLP:000001587.

PTM databases

iPTMnetiP45953.
PhosphoSitePlusiP45953.

Proteomic databases

PaxDbiP45953.
PRIDEiP45953.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25363.
KEGGirno:25363.
UCSCiRGD:2014. rat.

Organism-specific databases

CTDi37.
RGDi2014. Acadvl.

Phylogenomic databases

eggNOGiKOG0137. Eukaryota.
COG1960. LUCA.
HOGENOMiHOG000131665.
HOVERGENiHBG050448.
InParanoidiP45953.
KOiK09479.
PhylomeDBiP45953.

Enzyme and pathway databases

UniPathwayiUPA00660.

Miscellaneous databases

PROiP45953.

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 nameiACADV_RAT
AccessioniPrimary (citable) accession number: P45953
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 30, 2016
This is version 133 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, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.