Search Results

Overview

Uniprot IDP33121
Protein NameLong-chain-fatty-acid--CoA ligase 1
Gene NameACSL1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
113 GPCLGSRKPDQPYEW
205 VFVDKPEKAKLLLEG
207 VDKPEKAKLLLEGVE
284 SGTTGNPKGAMVTHR
386 GQANTTLKRWLLDFA
397 LDFASKRKEAELRSG
419 WDRLIFHKVQSSLGG
521 NVFQGYLKDPAKTAE
525 GYLKDPAKTAEALDK
532 KTAEALDKDGWLHTG
561 DRKKHIFKLAQGEYI
572 GEYIAPEKIENIYMR
632 CRNKDVKKAILEDMV
643 EDMVRLGKDSGLKPF
648 LGKDSGLKPFEQVKG
675 GLLTPTMKAKRPELR
677 LTPTMKAKRPELRNY

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 (PubMed:21242590, PubMed:22633490, PubMed:24269233). Preferentially uses palmitoleate, oleate and linoleate (PubMed:24269233). Preferentially activates arachidonate than epoxyeicosatrienoic acids (EETs) or hydroxyeicosatrienoic acids (HETEs) (By similarity)

Protein Sequence

10 MQAHELFRYF 20 RMPELVDFRQ 30 YVRTLPTNTL 40 MGFGAFAALT 50 TFWYATRPKP 60 LKPPCDLSMQ 70 SVEVAGSGGA 80 RRSALLDSDE 90 PLVYFYDDVT 100 TLYEGFQRGI 110 QVSNNGPCLG 120 SRKPDQPYEW 130 LSYKQVAELS 140 ECIGSALIQK 150 GFKTAPDQFI 160 GIFAQNRPEW 170 VIIEQGCFAY 180 SMVIVPLYDT 190 LGNEAITYIV 200 NKAELSLVFV 210 DKPEKAKLLL 220 EGVENKLIPG 230 LKIIVVMDAY 240 GSELVERGQR 250 CGVEVTSMKA 260 MEDLGRANRR 270 KPKPPAPEDL 280 AVICFTSGTT 290 GNPKGAMVTH 300 RNIVSDCSAF 310 VKATENTVNP 320 CPDDTLISFL 330 PLAHMFERVV 340 ECVMLCHGAK 350 IGFFQGDIRL 360 LMDDLKVLQP 370 TVFPVVPRLL 380 NRMFDRIFGQ 390 ANTTLKRWLL 400 DFASKRKEAE 410 LRSGIIRNNS 420 LWDRLIFHKV 430 QSSLGGRVRL 440 MVTGAAPVSA 450 TVLTFLRAAL 460 GCQFYEGYGQ 470 TECTAGCCLT 480 MPGDWTAGHV 490 GAPMPCNLIK 500 LVDVEEMNYM 510 AAEGEGEVCV 520 KGPNVFQGYL 530 KDPAKTAEAL 540 DKDGWLHTGD 550 IGKWLPNGTL 560 KIIDRKKHIF 570 KLAQGEYIAP 580 EKIENIYMRS 590 EPVAQVFVHG 600 ESLQAFLIAI 610 VVPDVETLCS 620 WAQKRGFEGS 630 FEELCRNKDV 640 KKAILEDMVR 650 LGKDSGLKPF 660 EQVKGITLHP 670 ELFSIDNGLL 680 TPTMKAKRPE 690 LRNYFRSQID DLYSTIKV

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005783 endoplasmic reticulum
Cellular Component GO:0005789 endoplasmic reticulum membrane
Cellular Component GO:0016020 membrane
Cellular Component GO:0005741 mitochondrial outer membrane
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005778 peroxisomal membrane
Molecular Function GO:0047676 arachidonate-CoA ligase activity
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0004467 long-chain fatty acid-CoA ligase activity
Molecular Function GO:0090434 oleoyl-CoA ligase activity
Molecular Function GO:0090433 palmitoyl-CoA ligase activity
Molecular Function GO:0050197 phytanate-CoA ligase activity
Molecular Function GO:0070251 pristanate-CoA ligase activity
Molecular Function GO:0043539 protein serine/threonine kinase activator activity
Biological Process GO:0006633 fatty acid biosynthetic process
Biological Process GO:0015908 fatty acid transport
Biological Process GO:0008610 lipid biosynthetic process
Biological Process GO:0044539 long-chain fatty acid import into cell
Biological Process GO:0001676 long-chain fatty acid metabolic process
Biological Process GO:0035338 long-chain fatty-acyl-CoA biosynthetic process
Biological Process GO:0120162 positive regulation of cold-induced thermogenesis
Biological Process GO:0010747 positive regulation of long-chain fatty acid import across plasma membrane
Biological Process GO:0007584 response to nutrient
Biological Process GO:0034201 response to oleic acid
Biological Process GO:0019432 triglyceride biosynthetic process
Biological Process GO:0000038 very long-chain fatty acid metabolic process
Biological Process GO:0042178 xenobiotic catabolic process

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[4] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.