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P49748

- ACADV_HUMAN

UniProt

P49748 - ACADV_HUMAN

Protein

Very long-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

ACADVL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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 oxygenBy similarity
    Binding sitei366 – 3661FADBy similarity
    Active sitei462 – 4621Proton acceptor1 Publication
    Binding sitei463 – 4631Substrate; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi214 – 22310FAD
    Nucleotide bindingi249 – 2513FAD
    Nucleotide bindingi435 – 4395FADBy 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

    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

    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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 – 4040MitochondrionBy similarityAdd
    BLAST
    Chaini41 – 655615Very long-chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000515Add
    BLAST

    Amino acid modifications

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

    1
    655
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49748.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni41 – 482442CatalyticAdd
    BLAST
    Regioni338 – 3414Substrate bindingBy similarity
    Regioni462 – 4632Substrate binding
    Regioni483 – 51634Membrane-anchoringCuratedAdd
    BLAST

    Sequence similaritiesi

    Belongs to the acyl-CoA dehydrogenase family.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti193 – 1931G → C in BAA29057. (PubMed:8554625)Curated
    Sequence conflicti200 – 2001K → E in BAG57027. (PubMed:14702039)Curated
    Sequence conflicti541 – 5411E → K in BAG57027. (PubMed:14702039)Curated

    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. 1 PublicationVSP_046031Add
    BLAST
    Alternative sequencei47 – 6822Missing in isoform 2. 1 PublicationVSP_007734Add
    BLAST

    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

    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 THE SUBSTRATE ANALOG 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: October 1, 2014
    This is version 153 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