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P49748

- ACADV_HUMAN

UniProt

P49748 - ACADV_HUMAN

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Protein
Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
Gene
ACADVL, VLCAD
Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 Publication

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

FAD.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei223 – 2231Substrate; via carbonyl oxygen By similarity
Binding sitei366 – 3661FAD By similarity
Active sitei462 – 4621Proton acceptor1 Publication
Binding sitei463 – 4631Substrate; via amide nitrogen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi214 – 22310FAD
Nucleotide bindingi249 – 2513FAD
Nucleotide bindingi435 – 4395FAD By similarity
Nucleotide bindingi464 – 4663FAD

GO - Molecular functioni

  1. acyl-CoA dehydrogenase activity Source: Reactome
  2. flavin adenine dinucleotide binding Source: InterPro
  3. long-chain-acyl-CoA dehydrogenase activity Source: ProtInc

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. cellular lipid metabolic process Source: Reactome
  3. cellular protein metabolic process Source: Reactome
  4. endoplasmic reticulum unfolded protein response Source: Reactome
  5. energy derivation by oxidation of organic compounds Source: ProtInc
  6. epithelial cell differentiation Source: UniProt
  7. fatty acid beta-oxidation Source: Reactome
  8. fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: BHF-UCL
  9. negative regulation of fatty acid biosynthetic process Source: BHF-UCL
  10. negative regulation of fatty acid oxidation Source: BHF-UCL
  11. regulation of cholesterol metabolic process Source: BHF-UCL
  12. small molecule metabolic process Source: Reactome
  13. temperature homeostasis Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000072778-MONOMER.
ReactomeiREACT_18273. XBP1(S) activates chaperone genes.
REACT_2025. 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)
Short name:
VLCAD
Gene namesi
Name:ACADVL
Synonyms:VLCAD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:92. ACADVL.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. mitochondrial inner membrane Source: UniProtKB-SubCell
  3. mitochondrial matrix Source: Reactome
  4. mitochondrial nucleoid Source: BHF-UCL
  5. mitochondrion Source: BHF-UCL
  6. nucleolus Source: HPA
  7. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Involvement in diseasei

Acyl-CoA dehydrogenase very long-chain deficiency (ACADVLD) [MIM:201475]: An inborn error of mitochondrial fatty acid beta-oxidation which leads to impaired long-chain fatty acid beta-oxidation. It is clinically heterogeneous, with three major phenotypes: a severe childhood form characterized by early onset, high mortality and high incidence of cardiomyopathy; a milder childhood form with later onset, characterized by hypoketotic hypoglycemia, low mortality and rare cardiomyopathy; an adult form, with isolated skeletal muscle involvement, rhabdomyolysis and myoglobinuria, usually triggered by exercise or fasting.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti130 – 1301Missing in ACADVLD. 1 Publication
VAR_000331
Natural varianti158 – 1581T → N in ACADVLD.
VAR_000332
Natural varianti159 – 1591Q → R in ACADVLD.
VAR_000333
Natural varianti174 – 1741V → M in ACADVLD.
VAR_000334
Natural varianti185 – 1851G → S in ACADVLD.
VAR_000335
Natural varianti213 – 2131A → P in ACADVLD.
Corresponds to variant rs140629318 [ dbSNP | Ensembl ].
VAR_010101
Natural varianti218 – 2181E → K in ACADVLD.
VAR_000336
Natural varianti243 – 2431L → R in ACADVLD.
VAR_000337
Natural varianti247 – 2471K → E in ACADVLD.
VAR_010102
Natural varianti247 – 2471K → T in ACADVLD.
VAR_000338
Natural varianti260 – 2601T → M in ACADVLD.
Corresponds to variant rs113994168 [ dbSNP | Ensembl ].
VAR_000339
Natural varianti278 – 2781Missing in ACADVLD.
VAR_000340
Natural varianti281 – 2811A → D in ACADVLD.
VAR_000341
Natural varianti283 – 2831V → A in ACADVLD.
Corresponds to variant rs113994167 [ dbSNP | Ensembl ].
VAR_000342
Natural varianti290 – 2901G → D in ACADVLD.
VAR_000343
Natural varianti294 – 2941G → E in ACADVLD.
Corresponds to variant rs200573371 [ dbSNP | Ensembl ].
VAR_000344
Natural varianti299 – 2991K → N in ACADVLD.
VAR_000345
Natural varianti299 – 2991Missing in ACADVLD. 1 Publication
VAR_000346
Natural varianti317 – 3171V → A in ACADVLD.
VAR_000347
Natural varianti352 – 3521M → V in ACADVLD.
VAR_000348
Natural varianti366 – 3661R → C in ACADVLD.
VAR_000349
Natural varianti366 – 3661R → H in ACADVLD.
Corresponds to variant rs112406105 [ dbSNP | Ensembl ].
VAR_000350
Natural varianti381 – 3811Missing in ACADVLD.
VAR_000351
Natural varianti382 – 3821K → Q in ACADVLD. 1 Publication
Corresponds to variant rs118204015 [ dbSNP | Ensembl ].
VAR_000352
Natural varianti405 – 4051D → H in ACADVLD.
VAR_000353
Natural varianti441 – 4411G → D in ACADVLD.
Corresponds to variant rs2309689 [ dbSNP | Ensembl ].
VAR_000354
Natural varianti450 – 4501R → H in ACADVLD. 1 Publication
Corresponds to variant rs118204016 [ dbSNP | Ensembl ].
VAR_000355
Natural varianti453 – 4531R → Q in ACADVLD.
Corresponds to variant rs138058572 [ dbSNP | Ensembl ].
VAR_000356
Natural varianti454 – 4541D → N in ACADVLD.
VAR_000357
Natural varianti456 – 4561R → H in ACADVLD.
VAR_000358
Natural varianti458 – 4581F → L in ACADVLD.
Corresponds to variant rs118204017 [ dbSNP | Ensembl ].
VAR_010103
Natural varianti459 – 4591R → W in ACADVLD.
VAR_000359
Natural varianti463 – 4631G → E in ACADVLD.
Corresponds to variant rs200366828 [ dbSNP | Ensembl ].
VAR_000360
Natural varianti469 – 4691R → Q in ACADVLD.
VAR_000361
Natural varianti469 – 4691R → W in ACADVLD.
Corresponds to variant rs113994170 [ dbSNP | Ensembl ].
VAR_000362
Natural varianti490 – 4901A → P in ACADVLD.
VAR_010104
Natural varianti502 – 5021L → P in ACADVLD.
VAR_000363
Natural varianti534 – 5341E → K in ACADVLD.
Corresponds to variant rs2230180 [ dbSNP | Ensembl ].
VAR_010105
Natural varianti602 – 6021L → I in ACADVLD.
VAR_000364
Natural varianti613 – 6131R → W in ACADVLD. 1 Publication
Corresponds to variant rs118204014 [ dbSNP | Ensembl ].
VAR_000365
Natural varianti615 – 6151R → Q in ACADVLD.
Corresponds to variant rs148584617 [ dbSNP | Ensembl ].
VAR_010106

Keywords - Diseasei

Cardiomyopathy, Disease mutation

Organism-specific databases

MIMi201475. phenotype.
Orphaneti26793. Very long chain acyl-CoA dehydrogenase deficiency.
PharmGKBiPA24428.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4040Mitochondrion By similarity
Add
BLAST
Chaini41 – 655615Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000000515Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511N6-acetyllysine By similarity
Modified residuei71 – 711N6-acetyllysine; alternate By similarity
Modified residuei71 – 711N6-succinyllysine; alternate By similarity
Modified residuei195 – 1951N6-succinyllysine By similarity
Modified residuei237 – 2371S-nitrosocysteine By similarity
Modified residuei239 – 2391N6-acetyllysine; alternate1 Publication
Modified residuei239 – 2391N6-succinyllysine; alternate By similarity
Modified residuei276 – 2761N6-acetyllysine; alternate By similarity
Modified residuei276 – 2761N6-succinyllysine; alternate By similarity
Modified residuei278 – 2781N6-acetyllysine; alternate By similarity
Modified residuei278 – 2781N6-succinyllysine; alternate By similarity
Modified residuei298 – 2981N6-acetyllysine By similarity
Modified residuei331 – 3311N6-acetyllysine; alternate1 Publication
Modified residuei331 – 3311N6-succinyllysine; alternate By similarity
Cross-linki331 – 331Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Modified residuei372 – 3721N6-succinyllysine By similarity
Modified residuei482 – 4821N6-acetyllysine; alternate By similarity
Modified residuei482 – 4821N6-succinyllysine; alternate By similarity
Modified residuei550 – 5501N6-acetyllysine By similarity
Modified residuei556 – 5561N6-acetyllysine; alternate By similarity
Modified residuei556 – 5561N6-succinyllysine; alternate By similarity
Modified residuei639 – 6391N6-succinyllysine By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, S-nitrosylation, Ubl conjugation

Proteomic databases

MaxQBiP49748.
PaxDbiP49748.
PRIDEiP49748.

PTM databases

PhosphoSiteiP49748.

Expressioni

Gene expression databases

ArrayExpressiP49748.
BgeeiP49748.
CleanExiHS_ACADVL.
GenevestigatoriP49748.

Organism-specific databases

HPAiHPA019006.
HPA020595.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi106555. 11 interactions.
IntActiP49748. 12 interactions.
MINTiMINT-4824254.
STRINGi9606.ENSP00000325395.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi73 – 775
Turni78 – 803
Turni85 – 873
Helixi96 – 11520
Helixi119 – 1257
Helixi130 – 1389
Turni139 – 1424
Helixi148 – 1503
Helixi157 – 17014
Helixi172 – 18211
Turni183 – 1864
Helixi187 – 1926
Helixi195 – 20612
Beta strandi212 – 2154
Beta strandi221 – 2233
Helixi225 – 2273
Beta strandi231 – 2344
Beta strandi238 – 25114
Turni252 – 2554
Beta strandi257 – 26812
Turni270 – 2723
Beta strandi275 – 28511
Helixi286 – 2883
Beta strandi289 – 2935
Beta strandi307 – 31812
Helixi319 – 3213
Beta strandi322 – 3254
Helixi329 – 36537
Helixi373 – 3753
Helixi377 – 40529
Helixi412 – 43726
Helixi439 – 4424
Helixi448 – 4558
Helixi456 – 4594
Beta strandi461 – 4633
Helixi465 – 48521
Helixi486 – 4883
Turni522 – 5243
Helixi527 – 5293
Helixi530 – 55425
Helixi555 – 5606
Helixi562 – 59130
Helixi596 – 62227
Helixi627 – 64418

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2UXWX-ray1.45A72-655[»]
3B96X-ray1.91A69-655[»]
ProteinModelPortaliP49748.
SMRiP49748. Positions 69-655.

Miscellaneous databases

EvolutionaryTraceiP49748.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni41 – 482442Catalytic
Add
BLAST
Regioni338 – 3414Substrate binding By similarity
Regioni462 – 4632Substrate binding
Regioni483 – 51634Membrane-anchoring Inferred
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1960.
HOVERGENiHBG050448.
InParanoidiP49748.
KOiK09479.
OMAiATNRTQF.
OrthoDBiEOG712TVX.
PhylomeDBiP49748.
TreeFamiTF105053.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
2.40.110.10. 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]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P49748-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MQAARMAASL GRQLLRLGGG SSRLTALLGQ PRPGPARRPY AGGAAQLALD    50
KSDSHPSDAL TRKKPAKAES KSFAVGMFKG QLTTDQVFPY PSVLNEEQTQ 100
FLKELVEPVS RFFEEVNDPA KNDALEMVEE TTWQGLKELG AFGLQVPSEL 150
GGVGLCNTQY ARLVEIVGMH DLGVGITLGA HQSIGFKGIL LFGTKAQKEK 200
YLPKLASGET VAAFCLTEPS SGSDAASIRT SAVPSPCGKY YTLNGSKLWI 250
SNGGLADIFT VFAKTPVTDP ATGAVKEKIT AFVVERGFGG ITHGPPEKKM 300
GIKASNTAEV FFDGVRVPSE NVLGEVGSGF KVAMHILNNG RFGMAAALAG 350
TMRGIIAKAV DHATNRTQFG EKIHNFGLIQ EKLARMVMLQ YVTESMAYMV 400
SANMDQGATD FQIEAAISKI FGSEAAWKVT DECIQIMGGM GFMKEPGVER 450
VLRDLRIFRI FEGTNDILRL FVALQGCMDK GKELSGLGSA LKNPFGNAGL 500
LLGEAGKQLR RRAGLGSGLS LSGLVHPELS RSGELAVRAL EQFATVVEAK 550
LIKHKKGIVN EQFLLQRLAD GAIDLYAMVV VLSRASRSLS EGHPTAQHEK 600
MLCDTWCIEA AARIREGMAA LQSDPWQQEL YRNFKSISKA LVERGGVVTS 650
NPLGF 655
Length:655
Mass (Da):70,390
Last modified:October 1, 1996 - v1
Checksum:iA5594D1EA7911D19
GO
Isoform 2 (identifier: P49748-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     47-68: Missing.

Note: No experimental confirmation available.

Show »
Length:633
Mass (Da):68,058
Checksum:iD84E8F01DF1E8958
GO
Isoform 3 (identifier: P49748-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MQAARMAASLGRQLLRLGGG → MLGGLAAAAGTRIMGKEIEAEAQRPLRQTWRPGQPPAMTAKTM

Note: No experimental confirmation available.

Show »
Length:678
Mass (Da):72,927
Checksum:i65A9CFB675A59E94
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171L → F.
Corresponds to variant rs2230179 [ dbSNP | Ensembl ].
VAR_029286
Natural varianti43 – 431G → D.
Corresponds to variant rs2230178 [ dbSNP | Ensembl ].
VAR_000330
Natural varianti65 – 651P → L.
Corresponds to variant rs28934585 [ dbSNP | Ensembl ].
VAR_048176
Natural varianti130 – 1301Missing in ACADVLD. 1 Publication
VAR_000331
Natural varianti158 – 1581T → N in ACADVLD.
VAR_000332
Natural varianti159 – 1591Q → R in ACADVLD.
VAR_000333
Natural varianti174 – 1741V → M in ACADVLD.
VAR_000334
Natural varianti185 – 1851G → S in ACADVLD.
VAR_000335
Natural varianti213 – 2131A → P in ACADVLD.
Corresponds to variant rs140629318 [ dbSNP | Ensembl ].
VAR_010101
Natural varianti218 – 2181E → K in ACADVLD.
VAR_000336
Natural varianti243 – 2431L → R in ACADVLD.
VAR_000337
Natural varianti247 – 2471K → E in ACADVLD.
VAR_010102
Natural varianti247 – 2471K → T in ACADVLD.
VAR_000338
Natural varianti260 – 2601T → M in ACADVLD.
Corresponds to variant rs113994168 [ dbSNP | Ensembl ].
VAR_000339
Natural varianti278 – 2781Missing in ACADVLD.
VAR_000340
Natural varianti281 – 2811A → D in ACADVLD.
VAR_000341
Natural varianti283 – 2831V → A in ACADVLD.
Corresponds to variant rs113994167 [ dbSNP | Ensembl ].
VAR_000342
Natural varianti290 – 2901G → D in ACADVLD.
VAR_000343
Natural varianti294 – 2941G → E in ACADVLD.
Corresponds to variant rs200573371 [ dbSNP | Ensembl ].
VAR_000344
Natural varianti299 – 2991K → N in ACADVLD.
VAR_000345
Natural varianti299 – 2991Missing in ACADVLD. 1 Publication
VAR_000346
Natural varianti317 – 3171V → A in ACADVLD.
VAR_000347
Natural varianti352 – 3521M → V in ACADVLD.
VAR_000348
Natural varianti359 – 3591A → S.
Corresponds to variant rs1051701 [ dbSNP | Ensembl ].
VAR_011990
Natural varianti366 – 3661R → C in ACADVLD.
VAR_000349
Natural varianti366 – 3661R → H in ACADVLD.
Corresponds to variant rs112406105 [ dbSNP | Ensembl ].
VAR_000350
Natural varianti381 – 3811Missing in ACADVLD.
VAR_000351
Natural varianti382 – 3821K → Q in ACADVLD. 1 Publication
Corresponds to variant rs118204015 [ dbSNP | Ensembl ].
VAR_000352
Natural varianti405 – 4051D → H in ACADVLD.
VAR_000353
Natural varianti441 – 4411G → D in ACADVLD.
Corresponds to variant rs2309689 [ dbSNP | Ensembl ].
VAR_000354
Natural varianti450 – 4501R → H in ACADVLD. 1 Publication
Corresponds to variant rs118204016 [ dbSNP | Ensembl ].
VAR_000355
Natural varianti453 – 4531R → Q in ACADVLD.
Corresponds to variant rs138058572 [ dbSNP | Ensembl ].
VAR_000356
Natural varianti454 – 4541D → N in ACADVLD.
VAR_000357
Natural varianti456 – 4561R → H in ACADVLD.
VAR_000358
Natural varianti458 – 4581F → L in ACADVLD.
Corresponds to variant rs118204017 [ dbSNP | Ensembl ].
VAR_010103
Natural varianti459 – 4591R → W in ACADVLD.
VAR_000359
Natural varianti463 – 4631G → E in ACADVLD.
Corresponds to variant rs200366828 [ dbSNP | Ensembl ].
VAR_000360
Natural varianti469 – 4691R → Q in ACADVLD.
VAR_000361
Natural varianti469 – 4691R → W in ACADVLD.
Corresponds to variant rs113994170 [ dbSNP | Ensembl ].
VAR_000362
Natural varianti490 – 4901A → P in ACADVLD.
VAR_010104
Natural varianti502 – 5021L → P in ACADVLD.
VAR_000363
Natural varianti534 – 5341E → K in ACADVLD.
Corresponds to variant rs2230180 [ dbSNP | Ensembl ].
VAR_010105
Natural varianti602 – 6021L → I in ACADVLD.
VAR_000364
Natural varianti613 – 6131R → W in ACADVLD. 1 Publication
Corresponds to variant rs118204014 [ dbSNP | Ensembl ].
VAR_000365
Natural varianti615 – 6151R → Q in ACADVLD.
Corresponds to variant rs148584617 [ dbSNP | Ensembl ].
VAR_010106
Natural varianti623 – 6231S → F.
Corresponds to variant rs13383 [ dbSNP | Ensembl ].
VAR_011991

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2020MQAAR…RLGGG → MLGGLAAAAGTRIMGKEIEA EAQRPLRQTWRPGQPPAMTA KTM in isoform 3.
VSP_046031Add
BLAST
Alternative sequencei47 – 6822Missing in isoform 2.
VSP_007734Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti193 – 1931G → C in BAA29057. 1 Publication
Sequence conflicti200 – 2001K → E in BAG57027. 1 Publication
Sequence conflicti541 – 5411E → K in BAG57027. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D43682 mRNA. Translation: BAA07781.1.
L46590 Genomic DNA. Translation: AAA79002.1.
X86556 mRNA. Translation: CAA60253.1.
D78298 Genomic DNA. Translation: BAA29057.1.
AK293549 mRNA. Translation: BAG57027.1.
AC120057 Genomic DNA. No translation available.
BC000399 mRNA. Translation: AAH00399.1.
BC012912 mRNA. Translation: AAH12912.1.
BC020218 mRNA. Translation: AAH20218.1.
CCDSiCCDS11090.1. [P49748-1]
CCDS42249.1. [P49748-2]
CCDS58509.1. [P49748-3]
PIRiS54183.
RefSeqiNP_000009.1. NM_000018.3. [P49748-1]
NP_001029031.1. NM_001033859.2. [P49748-2]
NP_001257376.1. NM_001270447.1. [P49748-3]
UniGeneiHs.437178.

Genome annotation databases

EnsembliENST00000350303; ENSP00000344152; ENSG00000072778. [P49748-2]
ENST00000356839; ENSP00000349297; ENSG00000072778. [P49748-1]
ENST00000543245; ENSP00000438689; ENSG00000072778. [P49748-3]
GeneIDi37.
KEGGihsa:37.
UCSCiuc002gev.4. human. [P49748-1]
uc002gew.4. human. [P49748-2]

Polymorphism databases

DMDMi1703068.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D43682 mRNA. Translation: BAA07781.1 .
L46590 Genomic DNA. Translation: AAA79002.1 .
X86556 mRNA. Translation: CAA60253.1 .
D78298 Genomic DNA. Translation: BAA29057.1 .
AK293549 mRNA. Translation: BAG57027.1 .
AC120057 Genomic DNA. No translation available.
BC000399 mRNA. Translation: AAH00399.1 .
BC012912 mRNA. Translation: AAH12912.1 .
BC020218 mRNA. Translation: AAH20218.1 .
CCDSi CCDS11090.1. [P49748-1 ]
CCDS42249.1. [P49748-2 ]
CCDS58509.1. [P49748-3 ]
PIRi S54183.
RefSeqi NP_000009.1. NM_000018.3. [P49748-1 ]
NP_001029031.1. NM_001033859.2. [P49748-2 ]
NP_001257376.1. NM_001270447.1. [P49748-3 ]
UniGenei Hs.437178.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2UXW X-ray 1.45 A 72-655 [» ]
3B96 X-ray 1.91 A 69-655 [» ]
ProteinModelPortali P49748.
SMRi P49748. Positions 69-655.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106555. 11 interactions.
IntActi P49748. 12 interactions.
MINTi MINT-4824254.
STRINGi 9606.ENSP00000325395.

PTM databases

PhosphoSitei P49748.

Polymorphism databases

DMDMi 1703068.

Proteomic databases

MaxQBi P49748.
PaxDbi P49748.
PRIDEi P49748.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000350303 ; ENSP00000344152 ; ENSG00000072778 . [P49748-2 ]
ENST00000356839 ; ENSP00000349297 ; ENSG00000072778 . [P49748-1 ]
ENST00000543245 ; ENSP00000438689 ; ENSG00000072778 . [P49748-3 ]
GeneIDi 37.
KEGGi hsa:37.
UCSCi uc002gev.4. human. [P49748-1 ]
uc002gew.4. human. [P49748-2 ]

Organism-specific databases

CTDi 37.
GeneCardsi GC17P007120.
GeneReviewsi ACADVL.
HGNCi HGNC:92. ACADVL.
HPAi HPA019006.
HPA020595.
MIMi 201475. phenotype.
609575. gene.
neXtProti NX_P49748.
Orphaneti 26793. Very long chain acyl-CoA dehydrogenase deficiency.
PharmGKBi PA24428.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1960.
HOVERGENi HBG050448.
InParanoidi P49748.
KOi K09479.
OMAi ATNRTQF.
OrthoDBi EOG712TVX.
PhylomeDBi P49748.
TreeFami TF105053.

Enzyme and pathway databases

UniPathwayi UPA00660 .
BioCyci MetaCyc:ENSG00000072778-MONOMER.
Reactomei REACT_18273. XBP1(S) activates chaperone genes.
REACT_2025. Beta oxidation of palmitoyl-CoA to myristoyl-CoA.

Miscellaneous databases

ChiTaRSi ACADVL. human.
EvolutionaryTracei P49748.
GenomeRNAii 37.
NextBioi 143.
PROi P49748.
SOURCEi Search...

Gene expression databases

ArrayExpressi P49748.
Bgeei P49748.
CleanExi HS_ACADVL.
Genevestigatori P49748.

Family and domain databases

Gene3Di 1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProi IPR006089. 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 ]
Pfami PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEi PS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of human very-long-chain acyl-coenzyme A dehydrogenase and molecular characterization of its deficiency in two patients."
    Aoyama T., Souri M., Ueno I., Kamijo T., Yamaguchi S., Rhead W.J., Tanaka K., Hashimoto T.
    Am. J. Hum. Genet. 57:273-283(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Cloning and characterization of human very-long-chain acyl-CoA dehydrogenase cDNA, chromosomal assignment of the gene and identification in four patients of nine different mutations within the VLCAD gene."
    Andresen B.S., Bross P., Vianey-Saban C., Divry P., Zabot M.-T., Roe C.R., Nada M.A., Byskov A., Kruse T.A., Neve S., Kristiansen K., Knudsen I., Corydon M.J., Gregersen N.
    Hum. Mol. Genet. 5:461-472(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS.
    Tissue: Placenta.
  3. "Genomic DNA organization of human mitochondrial very-long-chain acyl-CoA dehydrogenase and mutation analysis."
    Orii K.O., Aoyama T., Souri M., Orii K.E., Kondo N., Orii T., Hashimoto T.
    Biochem. Biophys. Res. Commun. 217:987-992(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    Tissue: Peripheral blood.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Cerebellum.
  5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Liver, Lung and Pancreas.
  7. "Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients."
    Aoyama T., Souri M., Ushikubo S., Kamijo T., Yamaguchi S., Kelley R.I., Rhead W.J., Uetake K., Tanaka K., Hashimoto T.
    J. Clin. Invest. 95:2465-2473(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. Cited for: REVIEW ON VARIANTS.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239 AND LYS-331, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase."
    McAndrew R.P., Wang Y., Mohsen A.W., He M., Vockley J., Kim J.J.
    J. Biol. Chem. 283:9435-9443(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 69-655 IN COMPLEX WITH MYRISTOYL-COA, FUNCTION, SUBUNIT, COFACTOR, ACTIVE SITE.
  12. "Mutation analysis of very-long-chain acyl-coenzyme A dehydrogenase (VLCAD) deficiency: identification and characterization of mutant VLCAD cDNAs from four patients."
    Souri M., Aoyama T., Orii K., Yamaguchi S., Hashimoto T.
    Am. J. Hum. Genet. 58:97-106(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ACADVLD GLU-130 DEL; LYS-299 DEL; GLN-382 AND TRP-613.
  13. Cited for: VARIANT ACADVLD HIS-450.
  14. "Molecular heterogeneity in very-long-chain acyl-CoA dehydrogenase deficiency causing pediatric cardiomyopathy and sudden death."
    Mathur A., Sims H.F., Gopalakrishnan D., Gibson B., Rinaldo P., Vockley J., Hug G., Strauss A.W.
    Circulation 99:1337-1343(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ACADVLD.

Entry informationi

Entry nameiACADV_HUMAN
AccessioniPrimary (citable) accession number: P49748
Secondary accession number(s): B4DEB6
, F5H2A9, O76056, Q8WUL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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