CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022591
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Long-chain-fatty-acid--CoA ligase 4 
Protein Synonyms/Alias
 Long-chain acyl-CoA synthetase 4; LACS 4; mACS4 
Gene Name
 Acsl4 
Gene Synonyms/Alias
 Acs4; Facl4 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
54KAKPTSDKPGSPYRSubiquitination[1]
148GLTALGLKPKNTIAIubiquitination[1]
354TLSDQSSKIKKGSKGubiquitination[1]
360SKIKKGSKGDCTVLKubiquitination[1]
397QEMNYVQKTLFKIGYubiquitination[1]
401YVQKTLFKIGYDYKLubiquitination[1]
500ICCEIKLKDWQEGGYubiquitination[1]
536GYFKNEEKTAEDYCVubiquitination[1]
587GEYVSLGKVEAALKNubiquitination[1]
621SFVVPNQKKLTLLAQubiquitination[1]
651AMEAEILKEIREAANubiquitination[1]
661REAANAMKLERFEIPubiquitination[1]
670ERFEIPIKVRLSPEPubiquitination[1]
702ELKNHYLKDIERMYGubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses arachidonate and eicosapentaenoate as substrates. 
Sequence Annotation
  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; Endoplasmic reticulum; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Membrane; Microsome; Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding; Peroxisome; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 711 AA 
Protein Sequence
MNLKLNVLTI ILLPVHLLIT IYSALIFIPW YFLTNAKKKN AMAKRIKAKP TSDKPGSPYR 60
SVTHFDSLAV IDIPGADTLD KLFDHAVAKF GKKDSLGTRE ILSEENEMQP NGKVFKKLIL 120
GNYKWINYLE VNCRVNNFGS GLTALGLKPK NTIAIFCETR AEWMIAAQTC FKYNFPLVTL 180
YATLGREAVV HGLNESEASY LITSVELLES KLKAALVDIN CVKHIIYVDN KTINRAEYPE 240
GLEIHSMQSV EELGAKPENL SVPPSRPTPS DMAIVMYTSG STGRPKGVMM HHSNLIAGMT 300
GQCERIPGLG PKDTYIGYLP LAHVLELTAE ISCFTYGCRI GYSSPLTLSD QSSKIKKGSK 360
GDCTVLKPTL MAAVPEIMDR IYKNVMSKVQ EMNYVQKTLF KIGYDYKLEQ IKKGYDAPLC 420
NLILFKKVKA LLGGNVRMML SGGAPLSPQT HRFMNVCFCC PIGQGYGLTE SCGAGTVTEV 480
TDYTTGRVGA PLICCEIKLK DWQEGGYTVH DKPNPRGEIV IGGQNISMGY FKNEEKTAED 540
YCVDENGQRW FCTGDIGEFH PDGCLQIIDR KKDLVKLQAG EYVSLGKVEA ALKNCPLIDN 600
ICAFAKSDQS YVISFVVPNQ KKLTLLAQQK GVEGSWVDIC NNPAMEAEIL KEIREAANAM 660
KLERFEIPIK VRLSPEPWTP ETGLVTDAFK LKRKELKNHY LKDIERMYGG K 711 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 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:0005739; C:mitochondrion; IDA:MGI.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
 GO:0047676; F:arachidonate-CoA ligase activity; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004467; F:long-chain fatty acid-CoA ligase activity; ISA:MGI.
 GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IEA:Compara.
 GO:0060996; P:dendritic spine development; IEA:Compara.
 GO:0060136; P:embryonic process involved in female pregnancy; IMP:MGI.
 GO:0015908; P:fatty acid transport; IEA:Compara.
 GO:0008610; P:lipid biosynthetic process; IEA:Compara.
 GO:0032307; P:negative regulation of prostaglandin secretion; IEA:Compara.
 GO:0030307; P:positive regulation of cell growth; IEA:Compara.
 GO:0019217; P:regulation of fatty acid metabolic process; TAS:MGI.
 GO:0070672; P:response to interleukin-15; IEA:Compara.
 GO:0007584; P:response to nutrient; IEA:Compara.
 GO:0006641; P:triglyceride metabolic process; IEA:Compara. 
Interpro
 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig. 
Pfam
 PF00501; AMP-binding 
SMART
  
PROSITE
 PS00455; AMP_BINDING 
PRINTS