Q8JZR0 · ACSL5_MOUSE
- ProteinLong-chain-fatty-acid--CoA ligase 5
- GeneAcsl5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids683 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation (By similarity).
ACSL5 may activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage (By similarity).
It was suggested that it may also stimulate fatty acid oxidation (By similarity).
At the villus tip of the crypt-villus axis of the small intestine may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL (By similarity).
May have a role in the survival of glioma cells (By similarity).
Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids (By similarity).
ACSL5 may activate fatty acids from exogenous sources for the synthesis of triacylglycerol destined for intracellular storage (By similarity).
It was suggested that it may also stimulate fatty acid oxidation (By similarity).
At the villus tip of the crypt-villus axis of the small intestine may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL (By similarity).
May have a role in the survival of glioma cells (By similarity).
Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids (By similarity).
Catalytic activity
- a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphateThis reaction proceeds in the forward direction.
- ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-CoAThis reaction proceeds in the forward direction.
- (E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA + AMP + diphosphateThis reaction proceeds in the forward direction.
- 15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + ATP + CoA = 15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-CoA + AMP + diphosphateThis reaction proceeds in the forward direction.
- 12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + ATP + CoA = 12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-CoA + AMP + diphosphateThis reaction proceeds in the forward direction.
- 5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = 5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphateThis reaction proceeds in the forward direction.
- 14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + ATP + CoA = 14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoyl-CoA + AMP + diphosphateThis reaction proceeds in the forward direction.
- 11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate + ATP + CoA = 11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoyl-CoA + AMP + diphosphateThis reaction proceeds in the forward direction.
- (9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP + diphosphateThis reaction proceeds in the forward direction.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | membrane | |
Cellular Component | mitochondrial inner membrane | |
Cellular Component | mitochondrial outer membrane | |
Cellular Component | mitochondrion | |
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | arachidonate-CoA ligase activity | |
Molecular Function | ATP binding | |
Molecular Function | long-chain fatty acid-CoA ligase activity | |
Molecular Function | oleoyl-CoA ligase activity | |
Biological Process | fatty acid transport | |
Biological Process | long-chain fatty acid metabolic process | |
Biological Process | long-chain fatty-acyl-CoA biosynthetic process | |
Biological Process | phospholipid biosynthetic process | |
Biological Process | positive regulation of fatty acid beta-oxidation | |
Biological Process | positive regulation of long-chain fatty acid import across plasma membrane | |
Biological Process | positive regulation of triglyceride biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLong-chain-fatty-acid--CoA ligase 5
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8JZR0
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion outer membrane ; Single-pass type III membrane protein
Endoplasmic reticulum membrane ; Single-pass type III membrane protein
Features
Showing features for transmembrane, topological domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 12-32 | Helical; Signal-anchor for type III membrane protein | ||||
Sequence: LPTPALICLLTFGTAIFLWLI | ||||||
Topological domain | 33-683 | Cytoplasmic | ||||
Sequence: NRPQPVLPLIDLDNQSVGIEGGARRGAFQKNNDLILYYFSDAKTLYENFQRGLAVSDNGPCLGYRKPNQPYKWISYKQVSDRAEYLGSCLLHKGYKSSQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVICDTPQKATMLVENVEKGLTPGLKTIILMDPFDDDLMKRGEKCGVEMLSLHDAENIGKENFKKPVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEPIFQPTSDDVTISYLPLAHMFERLVQGILFSCGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAKTPLKKFLLNLAIISKFNEVKNGIIRRDSLWDKLVFSKIQGSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAQGEYIAPEKIENVYSRSRPVLQVFVHGESLRSFLIGVVVPDPDSLPSFAAKIGVKGSFEELCKNQCVKEAILEDLQKIGKEGGLKSFEQVKSIFVHPEPFTIENGLLTPTLKAKRVELAKFFQTQIKSLYESIEE |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000193113 | 1-683 | Long-chain-fatty-acid--CoA ligase 5 | |||
Sequence: MLFIFNFLFSPLPTPALICLLTFGTAIFLWLINRPQPVLPLIDLDNQSVGIEGGARRGAFQKNNDLILYYFSDAKTLYENFQRGLAVSDNGPCLGYRKPNQPYKWISYKQVSDRAEYLGSCLLHKGYKSSQDQFVGIFAQNRPEWVISELACYTYSMVAVPLYDTLGTEAIIFVINRADIPVVICDTPQKATMLVENVEKGLTPGLKTIILMDPFDDDLMKRGEKCGVEMLSLHDAENIGKENFKKPVPPKPEDLSVICFTSGTTGDPKGAMLTHENVVSNMAAFLKFLEPIFQPTSDDVTISYLPLAHMFERLVQGILFSCGGKIGFFQGDIRLLPDDMKALKPTVFPTVPRLLNRVYDKVQNEAKTPLKKFLLNLAIISKFNEVKNGIIRRDSLWDKLVFSKIQGSLGGKVRLMITGAAPISTPVLTFFRAAMGCWVFEAYGQTECTGGCSITSPGDWTAGHVGTPVACNFVKLEDVADMNYFSVNNEGEICIKGNNVFKGYLKDPEKTQEVLDKDGWLHTGDIGRWLPNGTLKIVDRKKNIFKLAQGEYIAPEKIENVYSRSRPVLQVFVHGESLRSFLIGVVVPDPDSLPSFAAKIGVKGSFEELCKNQCVKEAILEDLQKIGKEGGLKSFEQVKSIFVHPEPFTIENGLLTPTLKAKRVELAKFFQTQIKSLYESIEE | ||||||
Modified residue | 361 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length683
- Mass (Da)76,206
- Last updated2002-10-01 v1
- Checksum734A1A5878741D70
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A286YD68 | A0A286YD68_MOUSE | Acsl5 | 117 | ||
A0A286YCF3 | A0A286YCF3_MOUSE | Acsl5 | 62 | ||
A0A286YCG4 | A0A286YCG4_MOUSE | Acsl5 | 96 | ||
A0A286YE29 | A0A286YE29_MOUSE | Acsl5 | 95 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC031544 EMBL· GenBank· DDBJ | AAH31544.1 EMBL· GenBank· DDBJ | mRNA |