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P49748 (ACADV_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Very long-chain specific acyl-CoA dehydrogenase, mitochondrial

Short name=VLCAD
EC=1.3.8.9
Gene names
Name:ACADVL
Synonyms:VLCAD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length655 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Active toward esters of long-chain and very long chain fatty acids such as palmitoyl-CoA, mysritoyl-CoA and stearoyl-CoA. Can accommodate substrate acyl chain lengths as long as 24 carbons, but shows little activity for substrates of less than 12 carbons. Ref.11

Catalytic activity

A very-long-chain acyl-CoA + electron-transfer flavoprotein = a very-long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.

Cofactor

FAD. Ref.11

Pathway

Lipid metabolism; mitochondrial fatty acid beta-oxidation.

Subunit structure

Homodimer. Ref.11

Subcellular location

Mitochondrion inner membrane.

Post-translational modification

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

Involvement in disease

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. Ref.12 Ref.13 Ref.14

Miscellaneous

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

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCardiomyopathy
Disease mutation
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
Isopeptide bond
S-nitrosylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

cellular lipid metabolic process

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

energy derivation by oxidation of organic compounds

Traceable author statement PubMed 7479827. Source: ProtInc

epithelial cell differentiation

Inferred from expression pattern PubMed 21492153. Source: UniProt

fatty acid beta-oxidation

Traceable author statement. Source: Reactome

fatty acid beta-oxidation using acyl-CoA dehydrogenase

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of fatty acid biosynthetic process

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of fatty acid oxidation

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of cholesterol metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

temperature homeostasis

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

mitochondrial inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrial nucleoid

Inferred from direct assay PubMed 18063578. Source: BHF-UCL

mitochondrion

Inferred from sequence or structural similarity. Source: BHF-UCL

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionacyl-CoA dehydrogenase activity

Traceable author statement. Source: Reactome

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

long-chain-acyl-CoA dehydrogenase activity

Traceable author statement PubMed 8466512. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P49748-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P49748-2)

The sequence of this isoform differs from the canonical sequence as follows:
     47-68: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P49748-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MQAARMAASLGRQLLRLGGG → MLGGLAAAAGTRIMGKEIEAEAQRPLRQTWRPGQPPAMTAKTM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4040Mitochondrion By similarity
Chain41 – 655615Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000000515

Regions

Nucleotide binding214 – 22310FAD
Nucleotide binding249 – 2513FAD
Nucleotide binding435 – 4395FAD By similarity
Nucleotide binding464 – 4663FAD
Region41 – 482442Catalytic
Region338 – 3414Substrate binding By similarity
Region462 – 4632Substrate binding
Region483 – 51634Membrane-anchoring Probable

Sites

Active site4621Proton acceptor Ref.11
Binding site2231Substrate; via carbonyl oxygen By similarity
Binding site3661FAD By similarity
Binding site4631Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue511N6-acetyllysine By similarity
Modified residue711N6-acetyllysine; alternate By similarity
Modified residue711N6-succinyllysine; alternate By similarity
Modified residue1951N6-succinyllysine By similarity
Modified residue2371S-nitrosocysteine By similarity
Modified residue2391N6-acetyllysine; alternate Ref.9
Modified residue2391N6-succinyllysine; alternate By similarity
Modified residue2761N6-acetyllysine; alternate By similarity
Modified residue2761N6-succinyllysine; alternate By similarity
Modified residue2781N6-acetyllysine; alternate By similarity
Modified residue2781N6-succinyllysine; alternate By similarity
Modified residue2981N6-acetyllysine By similarity
Modified residue3311N6-acetyllysine; alternate Ref.9
Modified residue3311N6-succinyllysine; alternate By similarity
Modified residue3721N6-succinyllysine By similarity
Modified residue4821N6-acetyllysine; alternate By similarity
Modified residue4821N6-succinyllysine; alternate By similarity
Modified residue5501N6-acetyllysine By similarity
Modified residue5561N6-acetyllysine; alternate By similarity
Modified residue5561N6-succinyllysine; alternate By similarity
Modified residue6391N6-succinyllysine By similarity
Cross-link331Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Natural variations

Alternative sequence1 – 2020MQAAR…RLGGG → MLGGLAAAAGTRIMGKEIEA EAQRPLRQTWRPGQPPAMTA KTM in isoform 3.
VSP_046031
Alternative sequence47 – 6822Missing in isoform 2.
VSP_007734
Natural variant171L → F.
Corresponds to variant rs2230179 [ dbSNP | Ensembl ].
VAR_029286
Natural variant431G → D.
Corresponds to variant rs2230178 [ dbSNP | Ensembl ].
VAR_000330
Natural variant651P → L.
Corresponds to variant rs28934585 [ dbSNP | Ensembl ].
VAR_048176
Natural variant1301Missing in ACADVLD. Ref.12
VAR_000331
Natural variant1581T → N in ACADVLD.
VAR_000332
Natural variant1591Q → R in ACADVLD.
VAR_000333
Natural variant1741V → M in ACADVLD.
VAR_000334
Natural variant1851G → S in ACADVLD.
VAR_000335
Natural variant2131A → P in ACADVLD.
Corresponds to variant rs140629318 [ dbSNP | Ensembl ].
VAR_010101
Natural variant2181E → K in ACADVLD.
VAR_000336
Natural variant2431L → R in ACADVLD.
VAR_000337
Natural variant2471K → E in ACADVLD.
VAR_010102
Natural variant2471K → T in ACADVLD.
VAR_000338
Natural variant2601T → M in ACADVLD.
Corresponds to variant rs113994168 [ dbSNP | Ensembl ].
VAR_000339
Natural variant2781Missing in ACADVLD.
VAR_000340
Natural variant2811A → D in ACADVLD.
VAR_000341
Natural variant2831V → A in ACADVLD.
Corresponds to variant rs113994167 [ dbSNP | Ensembl ].
VAR_000342
Natural variant2901G → D in ACADVLD.
VAR_000343
Natural variant2941G → E in ACADVLD.
Corresponds to variant rs200573371 [ dbSNP | Ensembl ].
VAR_000344
Natural variant2991K → N in ACADVLD.
VAR_000345
Natural variant2991Missing in ACADVLD. Ref.12
VAR_000346
Natural variant3171V → A in ACADVLD.
VAR_000347
Natural variant3521M → V in ACADVLD.
VAR_000348
Natural variant3591A → S.
Corresponds to variant rs1051701 [ dbSNP | Ensembl ].
VAR_011990
Natural variant3661R → C in ACADVLD.
VAR_000349
Natural variant3661R → H in ACADVLD.
Corresponds to variant rs112406105 [ dbSNP | Ensembl ].
VAR_000350
Natural variant3811Missing in ACADVLD.
VAR_000351
Natural variant3821K → Q in ACADVLD. Ref.12
Corresponds to variant rs118204015 [ dbSNP | Ensembl ].
VAR_000352
Natural variant4051D → H in ACADVLD.
VAR_000353
Natural variant4411G → D in ACADVLD.
Corresponds to variant rs2309689 [ dbSNP | Ensembl ].
VAR_000354
Natural variant4501R → H in ACADVLD. Ref.13
Corresponds to variant rs118204016 [ dbSNP | Ensembl ].
VAR_000355
Natural variant4531R → Q in ACADVLD.
Corresponds to variant rs138058572 [ dbSNP | Ensembl ].
VAR_000356
Natural variant4541D → N in ACADVLD.
VAR_000357
Natural variant4561R → H in ACADVLD.
VAR_000358
Natural variant4581F → L in ACADVLD.
Corresponds to variant rs118204017 [ dbSNP | Ensembl ].
VAR_010103
Natural variant4591R → W in ACADVLD.
VAR_000359
Natural variant4631G → E in ACADVLD.
Corresponds to variant rs200366828 [ dbSNP | Ensembl ].
VAR_000360
Natural variant4691R → Q in ACADVLD.
VAR_000361
Natural variant4691R → W in ACADVLD.
Corresponds to variant rs113994170 [ dbSNP | Ensembl ].
VAR_000362
Natural variant4901A → P in ACADVLD.
VAR_010104
Natural variant5021L → P in ACADVLD.
VAR_000363
Natural variant5341E → K in ACADVLD.
Corresponds to variant rs2230180 [ dbSNP | Ensembl ].
VAR_010105
Natural variant6021L → I in ACADVLD.
VAR_000364
Natural variant6131R → W in ACADVLD. Ref.12
Corresponds to variant rs118204014 [ dbSNP | Ensembl ].
VAR_000365
Natural variant6151R → Q in ACADVLD.
Corresponds to variant rs148584617 [ dbSNP | Ensembl ].
VAR_010106
Natural variant6231S → F.
Corresponds to variant rs13383 [ dbSNP | Ensembl ].
VAR_011991

Experimental info

Sequence conflict1931G → C in BAA29057. Ref.3
Sequence conflict2001K → E in BAG57027. Ref.4
Sequence conflict5411E → K in BAG57027. Ref.4

Secondary structure

............................................................................ 655
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: A5594D1EA7911D19

FASTA65570,390
        10         20         30         40         50         60 
MQAARMAASL GRQLLRLGGG SSRLTALLGQ PRPGPARRPY AGGAAQLALD KSDSHPSDAL 

        70         80         90        100        110        120 
TRKKPAKAES KSFAVGMFKG QLTTDQVFPY PSVLNEEQTQ FLKELVEPVS RFFEEVNDPA 

       130        140        150        160        170        180 
KNDALEMVEE TTWQGLKELG AFGLQVPSEL GGVGLCNTQY ARLVEIVGMH DLGVGITLGA 

       190        200        210        220        230        240 
HQSIGFKGIL LFGTKAQKEK YLPKLASGET VAAFCLTEPS SGSDAASIRT SAVPSPCGKY 

       250        260        270        280        290        300 
YTLNGSKLWI SNGGLADIFT VFAKTPVTDP ATGAVKEKIT AFVVERGFGG ITHGPPEKKM 

       310        320        330        340        350        360 
GIKASNTAEV FFDGVRVPSE NVLGEVGSGF KVAMHILNNG RFGMAAALAG TMRGIIAKAV 

       370        380        390        400        410        420 
DHATNRTQFG EKIHNFGLIQ EKLARMVMLQ YVTESMAYMV SANMDQGATD FQIEAAISKI 

       430        440        450        460        470        480 
FGSEAAWKVT DECIQIMGGM GFMKEPGVER VLRDLRIFRI FEGTNDILRL FVALQGCMDK 

       490        500        510        520        530        540 
GKELSGLGSA LKNPFGNAGL LLGEAGKQLR RRAGLGSGLS LSGLVHPELS RSGELAVRAL 

       550        560        570        580        590        600 
EQFATVVEAK LIKHKKGIVN EQFLLQRLAD GAIDLYAMVV VLSRASRSLS EGHPTAQHEK 

       610        620        630        640        650 
MLCDTWCIEA AARIREGMAA LQSDPWQQEL YRNFKSISKA LVERGGVVTS NPLGF 

« Hide

Isoform 2 [UniParc].

Checksum: D84E8F01DF1E8958
Show »

FASTA63368,058
Isoform 3 [UniParc].

Checksum: 65A9CFB675A59E94
Show »

FASTA67872,927

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Clear correlation of genotype with disease phenotype in very-long-chain acyl-CoA dehydrogenase deficiency."
Andresen B.S., Olpin S., Poorthuis B.J.H.M., Scholte H.R., Vianey-Saban C., Wanders R., Ijlst L., Morris A., Pourfarzam M., Bartlett K., Baumgartner E.R., de Klerk J.B.C., Schroeder L.D., Corydon T.J., Lund H., Winter V., Bross P., Bolund L., Gregersen N.
Am. J. Hum. Genet. 64:479-494(1999) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Very long chain acyl-coenzyme A dehydrogenase deficiency with adult onset."
Smelt A.H., Poorthuis B.J.H.M., Onkenhout W., Scholte H.R., Andresen B.S., van Duinen S.G., Gregersen N., Wintzen A.R.
Ann. Neurol. 43:540-544(1998) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11090.1. [P49748-1]
CCDS42249.1. [P49748-2]
CCDS58509.1. [P49748-3]
PIRS54183.
RefSeqNP_000009.1. NM_000018.3. [P49748-1]
NP_001029031.1. NM_001033859.2. [P49748-2]
NP_001257376.1. NM_001270447.1. [P49748-3]
UniGeneHs.437178.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2UXWX-ray1.45A72-655[»]
3B96X-ray1.91A69-655[»]
ProteinModelPortalP49748.
SMRP49748. Positions 69-655.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106555. 11 interactions.
IntActP49748. 12 interactions.
MINTMINT-4824254.
STRING9606.ENSP00000325395.

PTM databases

PhosphoSiteP49748.

Polymorphism databases

DMDM1703068.

Proteomic databases

MaxQBP49748.
PaxDbP49748.
PRIDEP49748.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000350303; ENSP00000344152; ENSG00000072778. [P49748-2]
ENST00000356839; ENSP00000349297; ENSG00000072778. [P49748-1]
ENST00000543245; ENSP00000438689; ENSG00000072778. [P49748-3]
GeneID37.
KEGGhsa:37.
UCSCuc002gev.4. human. [P49748-1]
uc002gew.4. human. [P49748-2]

Organism-specific databases

CTD37.
GeneCardsGC17P007120.
GeneReviewsACADVL.
HGNCHGNC:92. ACADVL.
HPAHPA019006.
HPA020595.
MIM201475. phenotype.
609575. gene.
neXtProtNX_P49748.
Orphanet26793. Very long chain acyl-CoA dehydrogenase deficiency.
PharmGKBPA24428.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1960.
HOVERGENHBG050448.
InParanoidP49748.
KOK09479.
OMAATNRTQF.
OrthoDBEOG712TVX.
PhylomeDBP49748.
TreeFamTF105053.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000072778-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.
UniPathwayUPA00660.

Gene expression databases

ArrayExpressP49748.
BgeeP49748.
CleanExHS_ACADVL.
GenevestigatorP49748.

Family and domain databases

Gene3D1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProIPR006089. 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]
PfamPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACADVL. human.
EvolutionaryTraceP49748.
GenomeRNAi37.
NextBio143.
PROP49748.
SOURCESearch...

Entry information

Entry nameACADV_HUMAN
AccessionPrimary (citable) accession number: P49748
Secondary accession number(s): B4DEB6 expand/collapse secondary AC list , F5H2A9, O76056, Q8WUL0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM