CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014497
UniProt Accession
Genbank Protein ID
 D30666 
Genbank Nucleotide ID
Protein Name
 Long-chain-fatty-acid--CoA ligase 3 
Protein Synonyms/Alias
 Brain acyl-CoA synthetase II; Long-chain acyl-CoA synthetase 3; LACS 3 
Gene Name
 Acsl3 
Gene Synonyms/Alias
 Acs3; Facl3 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
220SKELLQTKLKDIVSLacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL3 is required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins) (By similarity). Has mainly an anabolic role in energy metabolism. Mediates hepatic lipogenesis. Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates. Both isoforms exhibit the same level of activity. 
Sequence Annotation
 MOD_RES 683 683 Phosphoserine (By similarity).  
Keyword
 Alternative initiation; ATP-binding; Complete proteome; Endoplasmic reticulum; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Membrane; Microsome; Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding; Peroxisome; Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 720 AA 
Protein Sequence
MNNHVSSTPS TMKLKQTIHP ILLYFIHFII SLYTILTYIP FYFLCESKQE KPNHIKAKPV 60
SSKPDSAYRS VNSMDGLASV LYPGCDTLDK VFMYAKNKFK DKRLLGTREI LNEEDEIQPN 120
GKVFKKVILG HYNWLSYEDV FIRALDFGNG LQMLGQKPKA NIAIFCETRA EWMIAAQACF 180
MYNFQLVTLY ATLGGPAIVH GLNETEVTNI ITSKELLQTK LKDIVSLVPR LRHIITVDGK 240
PPTWSEFPKG VIVHTMAAVQ ALGVKADVDK KAHSKPLPSD IAVIMYTSGS TGIPKGVMIS 300
HSNIIASITG MARRIPRLGE EDVYIGYLPL AHVLELSAEL VCLSHGCRIG YSSPQTLADQ 360
SSKIKKGSKG DTSVLKPTLM AAVPEIMDRI YKNVMNKVNE MSAFQRNLFI LAYNYKMEQI 420
SKGCSTPLCD RFVFRNVRRL LGGNIRVLLC GGAPLSATTQ RFMNICFCCP VGQGYGLTES 480
TGAGTITEVW DYNTGRVGAP LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQNVTMGYY 540
KNEAKTKADF FEDENGQRWL CTGDIGEFDP DGCLKIIDRK KDLVKLQAGE YVSLGKVEAA 600
LKNLPLIDNI CAYANSYHSY VIGFVVPNQK ELTELARTKG FNGTWEELCN SSEMENEVLK 660
VLSEAAISAS LEKFEIPLKI RLSPDPWTPE TGLVTDAFKL KRKELKTHYQ ADIERMYGRK 720 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0005794; C:Golgi apparatus; IEA:Compara.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005811; C:lipid particle; IEA:Compara.
 GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
 GO:0003987; F:acetate-CoA ligase activity; TAS:RGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:RGD.
 GO:0007420; P:brain development; IEP:RGD.
 GO:0006633; P:fatty acid biosynthetic process; IDA:RGD.
 GO:0044539; P:long-chain fatty acid import; IEA:Compara.
 GO:0042998; P:positive regulation of Golgi to plasma membrane protein transport; IEA:Compara.
 GO:2001247; P:positive regulation of phosphatidylcholine biosynthetic process; IEA:Compara.
 GO:0051047; P:positive regulation of secretion; IEA:Compara.
 GO:0007584; P:response to nutrient; IEP:RGD.
 GO:0014070; P:response to organic cyclic compound; IEP:RGD.
 GO:0034379; P:very-low-density lipoprotein particle assembly; IEA:Compara. 
Interpro
 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig. 
Pfam
 PF00501; AMP-binding 
SMART
  
PROSITE
 PS00455; AMP_BINDING 
PRINTS