Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P49748

- ACADV_HUMAN

UniProt

P49748 - ACADV_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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

FAD1 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
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-KW
  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.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

BgeeiP49748.
CleanExiHS_ACADVL.
ExpressionAtlasiP49748. baseline and differential.
GenevestigatoriP49748.

Organism-specific databases

HPAiHPA019006.
HPA020595.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi106555. 20 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 – 775Combined sources
Turni78 – 803Combined sources
Turni85 – 873Combined sources
Helixi96 – 11520Combined sources
Helixi119 – 1257Combined sources
Helixi130 – 1389Combined sources
Turni139 – 1424Combined sources
Helixi148 – 1503Combined sources
Helixi157 – 17014Combined sources
Helixi172 – 18211Combined sources
Turni183 – 1864Combined sources
Helixi187 – 1926Combined sources
Helixi195 – 20612Combined sources
Beta strandi212 – 2154Combined sources
Beta strandi221 – 2233Combined sources
Helixi225 – 2273Combined sources
Beta strandi231 – 2344Combined sources
Beta strandi238 – 25114Combined sources
Turni252 – 2554Combined sources
Beta strandi257 – 26812Combined sources
Turni270 – 2723Combined sources
Beta strandi275 – 28511Combined sources
Helixi286 – 2883Combined sources
Beta strandi289 – 2935Combined sources
Beta strandi307 – 31812Combined sources
Helixi319 – 3213Combined sources
Beta strandi322 – 3254Combined sources
Helixi329 – 36537Combined sources
Helixi373 – 3753Combined sources
Helixi377 – 40529Combined sources
Helixi412 – 43726Combined sources
Helixi439 – 4424Combined sources
Helixi448 – 4558Combined sources
Helixi456 – 4594Combined sources
Beta strandi461 – 4633Combined sources
Helixi465 – 48521Combined sources
Helixi486 – 4883Combined sources
Turni522 – 5243Combined sources
Helixi527 – 5293Combined sources
Helixi530 – 55425Combined sources
Helixi555 – 5606Combined sources
Helixi562 – 59130Combined sources
Helixi596 – 62227Combined sources
Helixi627 – 64418Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119007.
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

        10         20         30         40         50
MQAARMAASL GRQLLRLGGG SSRLTALLGQ PRPGPARRPY AGGAAQLALD
60 70 80 90 100
KSDSHPSDAL TRKKPAKAES KSFAVGMFKG QLTTDQVFPY PSVLNEEQTQ
110 120 130 140 150
FLKELVEPVS RFFEEVNDPA KNDALEMVEE TTWQGLKELG AFGLQVPSEL
160 170 180 190 200
GGVGLCNTQY ARLVEIVGMH DLGVGITLGA HQSIGFKGIL LFGTKAQKEK
210 220 230 240 250
YLPKLASGET VAAFCLTEPS SGSDAASIRT SAVPSPCGKY YTLNGSKLWI
260 270 280 290 300
SNGGLADIFT VFAKTPVTDP ATGAVKEKIT AFVVERGFGG ITHGPPEKKM
310 320 330 340 350
GIKASNTAEV FFDGVRVPSE NVLGEVGSGF KVAMHILNNG RFGMAAALAG
360 370 380 390 400
TMRGIIAKAV DHATNRTQFG EKIHNFGLIQ EKLARMVMLQ YVTESMAYMV
410 420 430 440 450
SANMDQGATD FQIEAAISKI FGSEAAWKVT DECIQIMGGM GFMKEPGVER
460 470 480 490 500
VLRDLRIFRI FEGTNDILRL FVALQGCMDK GKELSGLGSA LKNPFGNAGL
510 520 530 540 550
LLGEAGKQLR RRAGLGSGLS LSGLVHPELS RSGELAVRAL EQFATVVEAK
560 570 580 590 600
LIKHKKGIVN EQFLLQRLAD GAIDLYAMVV VLSRASRSLS EGHPTAQHEK
610 620 630 640 650
MLCDTWCIEA AARIREGMAA LQSDPWQQEL YRNFKSISKA LVERGGVVTS

NPLGF
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 20 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.
GeneTreei ENSGT00760000119007.
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

Bgeei P49748.
CleanExi HS_ACADVL.
ExpressionAtlasi P49748. baseline and differential.
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 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: November 26, 2014
This is version 155 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