P50544
PR
Gene name |
Acadvl |
Protein name |
Very long-chain specific acyl-CoA dehydrogenase, mitochondrial |
Names |
MVLCAD, VLCAD |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:11370 |
EC number |
1.3.8.9: With a flavin as acceptor |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
2 structures for P50544
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 8CA1 | EM | 430 A | A/B | 1-656 | PDB |
| AF-P50544-F1 | Predicted | AlphaFoldDB |
40 variants for P50544
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389172646 | 25 | T>A | No | EVA | |
| rs3389172645 | 38 | Q>* | No | EVA | |
| rs3389176631 | 50 | L>M | No | EVA | |
| rs3389178912 | 104 | K>VSDG* | No | EVA | |
| rs3389135330 | 107 | V>M | No | EVA | |
| rs3389143419 | 130 | E>G | No | EVA | |
| rs3389109289 | 141 | G>* | No | EVA | |
| rs3389184765 | 148 | P>S | No | EVA | |
| rs3389172846 | 197 | A>S | No | EVA | |
| rs3389176628 | 227 | A>S | No | EVA | |
| rs3389166393 | 264 | A>T | No | EVA | |
| rs3389168912 | 270 | D>Y | No | EVA | |
| rs3389168887 | 276 | V>M | No | EVA | |
| rs3389172817 | 288 | S>R | No | EVA | |
| rs3402377808 | 294 | H>Q | No | EVA | |
| rs3402673125 | 296 | L>P | No | EVA | |
| rs3389166352 | 309 | S>L | No | EVA | |
| rs3389109229 | 327 | V>M | No | EVA | |
| rs3389109238 | 329 | D>N | No | EVA | |
| rs3389178942 | 340 | N>S | No | EVA | |
| rs3389174063 | 351 | G>D | No | EVA | |
| rs3389160380 | 376 | N>K | No | EVA | |
| rs3389160341 | 378 | G>R | No | EVA | |
| rs3389171571 | 383 | K>R | No | EVA | |
| rs3389143367 | 398 | A>T | No | EVA | |
| rs3389160362 | 418 | I>M | No | EVA | |
| rs3389160325 | 429 | K>N | No | EVA | |
| rs3389160370 | 435 | I>V | No | EVA | |
| rs3389183390 | 456 | I>V | No | EVA | |
| rs3389168913 | 506 | A>S | No | EVA | |
| rs3389172629 | 515 | G>R | No | EVA | |
| rs3389135251 | 522 | L>M | No | EVA | |
| rs3389175194 | 534 | G>D | No | EVA | |
| rs3402383933 | 538 | V>A | No | EVA | |
| rs3389160319 | 551 | K>E | No | EVA | |
| rs3389175216 | 571 | D>E | No | EVA | |
| rs3389174070 | 572 | G>D | No | EVA | |
| rs3389135242 | 595 | P>L | No | EVA | |
| rs3389143421 | 620 | A>T | No | EVA | |
| rs3389143375 | 638 | I>N | No | EVA |
No associated diseases with P50544
5 regional properties for P50544
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Acyl-CoA dehydrogenase, conserved site | 216 - 228 | IPR006089-1 |
| conserved_site | Acyl-CoA dehydrogenase, conserved site | 436 - 455 | IPR006089-2 |
| domain | Acyl-CoA oxidase/dehydrogenase, middle domain | 214 - 316 | IPR006091 |
| domain | Acyl-CoA dehydrogenase/oxidase C-terminal | 328 - 474 | IPR009075 |
| domain | Acyl-CoA dehydrogenase/oxidase, N-terminal | 97 - 210 | IPR013786 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.3.8.9 | With a flavin as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| extrinsic component of mitochondrial inner membrane | The component of mitochondrial inner membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region. |
| mitochondrial inner membrane | The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. |
| mitochondrial membrane | Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope. |
| mitochondrial nucleoid | The region of a mitochondrion to which the DNA is confined. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
| nucleolus | A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| acyl-CoA dehydrogenase activity | Catalysis of the reaction: acyl-CoA + oxidized |
| fatty-acyl-CoA binding | Binding to a fatty-acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty acyl group. |
| flavin adenine dinucleotide binding | Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. |
| identical protein binding | Binding to an identical protein or proteins. |
| long-chain-acyl-CoA dehydrogenase activity | Catalysis of the reaction: a long-chain 2,3-saturated fatty acyl-CoA + H+ + oxidized = a long-chain (2E)-enoyl-CoA + reduced |
| very-long-chain-acyl-CoA dehydrogenase activity | Catalysis of the reaction: a very-long-chain 2,3-saturated fatty acyl-CoA + H+ + oxidized = a very-long-chain (2E)-enoyl-CoA + reduced |
9 GO annotations of biological process
| Name | Definition |
|---|---|
| epithelial cell differentiation | The process in which a relatively unspecialized cell acquires specialized features of an epithelial cell, any of the cells making up an epithelium. |
| fatty acid beta-oxidation | A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). |
| fatty acid beta-oxidation using acyl-CoA dehydrogenase | A fatty acid beta-oxidation pathway in which the initial step of each oxidation cycle, which converts an acyl-CoA to a trans-2-enoyl-CoA, is catalyzed by acyl-CoA dehydrogenase; the electrons removed by oxidation pass through the respiratory chain to oxygen and leave H2O as the product. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). |
| fatty acid catabolic process | The chemical reactions and pathways resulting in the breakdown of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes. |
| negative regulation of fatty acid biosynthetic process | Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of fatty acids. |
| negative regulation of fatty acid oxidation | Any process that stops, prevents, or reduces the frequency, rate or extent of fatty acid oxidation. |
| regulation of cholesterol metabolic process | Any process that modulates the rate, frequency, or extent of cholesterol metabolism, the chemical reactions and pathways involving cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones. |
| response to cold | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism. |
| temperature homeostasis | A homeostatic process in which an organism modulates its internal body temperature. |
5 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P48818 | ACADVL | Very long-chain specific acyl-CoA dehydrogenase, mitochondrial | Bos taurus (Bovine) | PR |
| P49748 | ACADVL | Very long-chain specific acyl-CoA dehydrogenase, mitochondrial | Homo sapiens (Human) | PR |
| Q9DBL1 | Acadsb | Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial | Mus musculus (Mouse) | PR |
| Q07417 | Acads | Short-chain specific acyl-CoA dehydrogenase, mitochondrial | Mus musculus (Mouse) | PR |
| P45953 | Acadvl | Very long-chain specific acyl-CoA dehydrogenase, mitochondrial | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MQSARMTPSV | GRQLLRLGAR | SSRSTTVLQG | QPRPISAQRL | YAREATQAVL | DKPETLSSDA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| STREKPARAE | SKSFAVGMFK | GQLTIDQVFP | YPSVLSEEQA | QFLKELVGPV | ARFFEEVNDP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AKNDALEKVE | DDTLQGLKEL | GAFGLQVPSE | LGGLGLSNTQ | YARLAEIVGM | HDLGVSVTLG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AHQSIGFKGI | LLYGTKAQRE | KYLPRVASGQ | ALAAFCLTEP | SSGSDVASIR | SSAIPSPCGK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YYTLNGSKIW | ISNGGLADIF | TVFAKTPIKD | AATGAVKEKI | TAFVVERSFG | GVTHGLPEKK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| MGIKASNTSE | VYFDGVKVPS | ENVLGEVGDG | FKVAVNILNN | GRFGMAATLA | GTMKSLIAKA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VDHATNRTQF | GDKIHNFGVI | QEKLARMAIL | QYVTESMAYM | LSANMDQGFK | DFQIEAAISK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| IFCSEAAWKV | ADECIQIMGG | MGFMKEPGVE | RVLRDIRIFR | IFEGANDILR | LFVALQGCMD |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KGKELTGLGN | ALKNPFGNVG | LLMGEAGKQL | RRRTGIGSGL | SLSGIVHPEL | SRSGELAVQA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LDQFATVVEA | KLVKHKKGIV | NEQFLLQRLA | DGAIDLYAMV | VVLSRASRSL | SEGYPTAQHE |
| 610 | 620 | 630 | 640 | 650 | |
| KMLCDSWCIE | AATRIRENMA | SLQSSPQHQE | LFRNFRSISK | AMVENGGLVT | GNPLGI |