Very long-chain specific acyl-CoA dehydrogenase, mitochondrial precursor - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P49748 (ACADV_HUMAN)

Last modified November 25, 2008. Version 90. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
    Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
      Short name=VLCAD
    EC=1.3.99.-

Gene names

Name:	ACADVL
Synonyms:	VLCAD

Organism

Homo sapiens (Human)

Taxonomic identifier

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	655 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Active toward esters of long-chain and very long chain fatty acids such as palmitoyl-CoA, mysritoyl-CoA and stearoyl-CoA. Can accomodate substrate acyl chain lengths as long as 24 carbons, but shows little activity for substrates of less than 12 carbons.
Catalytic activity	Acyl-CoA + ETF = 2,3-dehydroacyl-CoA + reduced ETF.
Cofactor	FAD.
Pathway	Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subunit structure	Homodimer.
Subcellular location	Mitochondrion inner membrane.
Involvement in disease	Defects in ACADVL are the cause of very long chain acyl-CoA dehydrogenase deficiency (VLCAD deficiency) [MIM:201475]. VLCAD deficiency is an autosomal recessive disease which leads to impaired long-chain fatty acid beta-oxidation. It is clinically heterogeneous, with three major phenotypes: a severe childhood form, with early onset, high mortality, and high incidence of cardiomyopathy; a milder childhood form, with later onset, usually with hypoketotic hypoglycemia as the main presenting feature, low mortality, and rare cardiomyopathy; and an adult form, with isolated skeletal muscle involvement, rhabdomyolysis, and myoglobinuria, usually triggered by exercise or fasting.
Miscellaneous	A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.
Sequence similarities	Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Cardiomyopathy Disease mutation
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	energy derivation by oxidation of organic compounds Traceable author statement. Source: ProtInc fatty acid beta-oxidation Ref.1 Traceable author statement. Source: ProtInc oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro long-chain-acyl-CoA dehydrogenase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P49748-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P49748-2) The sequence of this isoform differs from the canonical sequence as follows: 47-68: Missing.
Notes: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

40

Mitochondrion By similarity

Chain

615

Very long-chain specific acyl-CoA dehydrogenase, mitochondrial

PRO_0000000515

Regions

Region

442

Catalytic

Region

34

Membrane-anchoring Probable

Sites

Active site

1

Proton acceptor

Amino acid modifications

Modified residue

1

N6-acetyllysine By similarity

Modified residue

1

N6-acetyllysine By similarity

Cross-link

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence

22

Missing in isoform 2.

VSP_007734

Natural variant

1

L → F: dbSNP rs2230179.

VAR_029286

Natural variant

1

G → D in VLCAD deficiency; could be a polymorphism. dbSNP rs2230178.

VAR_000330

Natural variant

1

Missing in VLCAD deficiency.

VAR_000331

Natural variant

1

T → N in VLCAD deficiency.

VAR_000332

Natural variant

1

Q → R in VLCAD deficiency.

VAR_000333

Natural variant

1

V → M in VLCAD deficiency.

VAR_000334

Natural variant

1

G → S in VLCAD deficiency.

VAR_000335

Natural variant

1

A → P in VLCAD deficiency.

VAR_010101

Natural variant

1

E → K in VLCAD deficiency.

VAR_000336

Natural variant

1

L → R in VLCAD deficiency.

VAR_000337

Natural variant

1

K → E in VLCAD deficiency.

VAR_010102

Natural variant

1

K → T in VLCAD deficiency.

VAR_000338

Natural variant

1

T → M in VLCAD deficiency.

VAR_000339

Natural variant

1

Missing in VLCAD deficiency.

VAR_000340

Natural variant

1

A → D in VLCAD deficiency.

VAR_000341

Natural variant

1

V → A in VLCAD deficiency.

VAR_000342

Natural variant

1

G → D in VLCAD deficiency.

VAR_000343

Natural variant

1

G → E in VLCAD deficiency.

VAR_000344

Natural variant

1

K → N in VLCAD deficiency.

VAR_000345

Natural variant

1

Missing in VLCAD deficiency.

VAR_000346

Natural variant

1

V → A in VLCAD deficiency.

VAR_000347

Natural variant

1

M → V in VLCAD deficiency.

VAR_000348

Natural variant

1

A → S: dbSNP rs1051701.

VAR_011990

Natural variant

1

R → C in VLCAD deficiency.

VAR_000349

Natural variant

1

R → H in VLCAD deficiency.

VAR_000350

Natural variant

1

Missing in VLCAD deficiency.

VAR_000351

Natural variant

1

K → Q in VLCAD deficiency.

VAR_000352

Natural variant

1

D → H in VLCAD deficiency.

VAR_000353

Natural variant

1

G → D in VLCAD deficiency. dbSNP rs2309689.

VAR_000354

Natural variant

1

R → H in VLCAD deficiency.

VAR_000355

Natural variant

1

R → Q in VLCAD deficiency.

VAR_000356

Natural variant

1

D → N in VLCAD deficiency.

VAR_000357

Natural variant

1

R → H in VLCAD deficiency.

VAR_000358

Natural variant

1

F → L in VLCAD deficiency.

VAR_010103

Natural variant

1

R → W in VLCAD deficiency.

VAR_000359

Natural variant

1

G → E in VLCAD deficiency.

VAR_000360

Natural variant

1

R → Q in VLCAD deficiency.

VAR_000361

Natural variant

1

R → W in VLCAD deficiency.

VAR_000362

Natural variant

1

A → P in VLCAD deficiency.

VAR_010104

Natural variant

1

L → P in VLCAD deficiency.

VAR_000363

Natural variant

1

E → K in VLCAD deficiency. dbSNP rs2230180.

VAR_010105

Natural variant

1

L → I in VLCAD deficiency.

VAR_000364

Natural variant

1

R → W in VLCAD deficiency.

VAR_000365

Natural variant

1

R → Q in VLCAD deficiency.

VAR_010106

Natural variant

1

S → F: dbSNP rs13383.

VAR_011991

Experimental info

Sequence conflict

1

G → C in BAA29057. Ref.3

Secondary structure

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655

Helix Strand Turn