Reviewed,
UniProtKB/Swiss-Prot P18163 (ACSL1_RAT)
Last modified
January 19, 2010.
Version 90.
History...
Clusters with 100%,
90%,
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Long-chain-fatty-acid--CoA ligase 1 EC=6.2.1.3 Alternative name(s): Long-chain acyl-CoA synthetase 1 Short name=LACS 1 Long-chain-fatty-acid--CoA ligase, liver isozyme | ||||
| Gene names |
| ||||
| Organism | Rattus norvegicus (Rat) | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 699 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses oleate, arachidonate, eicosapentaenoate and docosahexaenoate as substrates. |
| Catalytic activity | ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA. |
| Cofactor | Magnesium. |
| Subcellular location | Mitochondrion outer membrane; Single-pass type III membrane protein By similarity. Peroxisome membrane; Single-pass type III membrane protein By similarity. Microsome membrane; Single-pass type III membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass type III membrane protein By similarity. |
| Tissue specificity | Liver, heart, epididymal adipose and to a lesser extent brain, small intestine and lung. |
| Developmental stage | Levels remain constant during development. |
| Induction | By high fat and high carbohydrate diets. |
| Sequence similarities | Belongs to the ATP-dependent AMP-binding enzyme family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 699 | 699 | Long-chain-fatty-acid--CoA ligase 1 | PRO_0000193106 | |||||
Regions | |||||||||
| Transmembrane | 25 – 45 | 21 | Signal-anchor for type III membrane protein Potential | ||||||
| Topological domain | 46 – 699 | 654 | Cytoplasmic Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine Ref.2 | ||||||
| Modified residue | 9 | 1 | Nitrated tyrosine Ref.2 | ||||||
| Modified residue | 85 | 1 | Phosphotyrosine Ref.2 | ||||||
| Modified residue | 86 | 1 | Nitrated tyrosine Ref.2 | ||||||
| Modified residue | 544 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 633 | 1 | N6-acetyllysine Ref.2 | ||||||
Sequences
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References
| [1] | "Structure and regulation of rat long-chain acyl-CoA synthetase." Suzuki H., Kawarabayasi Y., Kondo J., Abe T., Nishikawa K., Kimura S., Hashimoto T., Yamamoto T. J. Biol. Chem. 265:8681-8685(1990) [PubMed: 2341402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: Wistar. Tissue: Liver. |
| [2] | "Post-translational modifications of rat liver mitochondrial outer membrane proteins identified by mass spectrometry." Distler A.M., Kerner J., Hoppel C.L. Biochim. Biophys. Acta 1774:628-636(2007) [PubMed: 17478130] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-19; 82-91 AND 628-641, ACETYLATION AT MET-1 AND LYS-633, NITRATION AT TYR-9 AND TYR-86, PHOSPHORYLATION AT TYR-85, MASS SPECTROMETRY. Tissue: Liver. |
| [3] | "Biochemical studies of two rat acyl-CoA synthetases, ACS1 and ACS2." Iijima H., Fujino T., Minekura H., Suzuki H., Kang M.-J., Yamamoto T.T. Eur. J. Biochem. 242:186-190(1996) [PubMed: 8973631] [Abstract] Cited for: CHARACTERIZATION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D90109 mRNA. Translation: BAA14136.1. |
| IPI | IPI00188989. |
| PIR | A36275. |
| RefSeq | NP_036952.1. |
| UniGene | Rn.6215 |
3D structure databases | |
| SMR | P18163. Positions 90-690. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P18163. |
PTM databases | |
| PhosphoSite | P18163. |
Proteomic databases | |
| PRIDE | P18163. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000014235; ENSRNOP00000014235; ENSRNOG00000010633; Rattus norvegicus. [Genome view] |
| GeneID | 25288. |
| KEGG | rno:25288. |
| NMPDR | fig|10116.3.peg.12441. |
| UCSC | NM_012820. rat. |
Organism-specific databases | |
| CTD | 25288. |
| RGD | 2015. Acsl1. |
Phylogenomic databases | |
| eggNOG | roNOG13164. |
| HOVERGEN | P18163. |
| InParanoid | P18163. |
| OMA | SECIGSA. |
| OrthoDB | EOG973S9M. |
| PhylomeDB | P18163. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-14442. |
| BRENDA | 6.2.1.3. 248. |
Gene expression databases | |
| ArrayExpress | P18163. |
| Genevestigator | P18163. |
| GermOnline | ENSRNOG00000010633. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view] |
| Pfam | PF00501. AMP-binding. 1 hit. [Graphical view] |
| PROSITE | PS00455. AMP_BINDING. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 606025. |
Entry information
| Entry name | ACSL1_RAT | ||||||||
| Accession | Primary (citable) accession number: P18163 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
