Search Results

Overview

Uniprot IDQ6P1M0
Protein NameLong-chain fatty acid transport protein 4
Gene NameSLC27A4
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
595 LHKTGTYKFQKTELR

Function

Mediates the levels of long-chain fatty acids (LCFA) in the cell by facilitating their transport across cell membranes (PubMed:10518211, PubMed:12556534, PubMed:20448275, PubMed:21395585, PubMed:22022213). Appears to be the principal fatty acid transporter in small intestinal enterocytes (PubMed:20448275). Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates, which prevents fatty acid efflux from cells and might drive more fatty acid uptake (PubMed:22022213, PubMed:24269233). Plays a role in the formation of the epidermal barrier. Required for fat absorption in early embryogenesis (By similarity). Probably involved in fatty acid transport across the blood barrier (PubMed:21395585). Indirectly inhibits RPE65 via substrate competition and via production of VLCFA derivatives like lignoceroyl-CoA. Prevents light-induced degeneration of rods and cones (By similarity)

Protein Sequence

10 MLLGASLVGV 20 LLFSKLVLKL 30 PWTQVGFSLL 40 FLYLGSGGWR 50 FIRVFIKTIR 60 RDIFGGLVLL 70 KVKAKVRQCL 80 QERRTVPILF 90 ASTVRRHPDK 100 TALIFEGTDT 110 HWTFRQLDEY 120 SSSVANFLQA 130 RGLASGDVAA 140 IFMENRNEFV 150 GLWLGMAKLG 160 VEAALINTNL 170 RRDALLHCLT 180 TSRARALVFG 190 SEMASAICEV 200 HASLDPSLSL 210 FCSGSWEPGA 220 VPPSTEHLDP 230 LLKDAPKHLP 240 SCPDKGFTDK 250 LFYIYTSGTT 260 GLPKAAIVVH 270 SRYYRMAALV 280 YYGFRMRPND 290 IVYDCLPLYH 300 SAGNIVGIGQ 310 CLLHGMTVVI 320 RKKFSASRFW 330 DDCIKYNCTI 340 VQYIGELCRY 350 LLNQPPREAE 360 NQHQVRMALG 370 NGLRQSIWTN 380 FSSRFHIPQV 390 AEFYGATECN 400 CSLGNFDSQV 410 GACGFNSRIL 420 SFVYPIRLVR 430 VNEDTMELIR 440 GPDGVCIPCQ 450 PGEPGQLVGR 460 IIQKDPLRRF 470 DGYLNQGANN 480 KKIAKDVFKK 490 GDQAYLTGDV 500 LVMDELGYLY 510 FRDRTGDTFR 520 WKGENVSTTE 530 VEGTLSRLLD 540 MADVAVYGVE 550 VPGTEGRAGM 560 AAVASPTGNC 570 DLERFAQVLE 580 KELPLYARPI 590 FLRLLPELHK 600 TGTYKFQKTE 610 LRKEGFDPAI 620 VKDPLFYLDA 630 QKGRYVPLDQ 640 EAYSRIQAGE EKL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005902 microvillus
Cellular Component GO:0031526 brush border membrane
Cellular Component GO:0005783 endoplasmic reticulum
Cellular Component GO:0005789 endoplasmic reticulum membrane
Cellular Component GO:0016020 membrane
Cellular Component GO:0005886 plasma membrane
Molecular Function GO:0047676 arachidonate-CoA ligase activity
Molecular Function GO:0015245 fatty acid transmembrane transporter activity
Molecular Function GO:0005324 long-chain fatty acid transmembrane transporter activity
Molecular Function GO:0004467 long-chain fatty acid-CoA ligase activity
Molecular Function GO:0000166 nucleotide binding
Molecular Function GO:0090434 oleoyl-CoA ligase activity
Molecular Function GO:0090433 palmitoyl-CoA ligase activity
Molecular Function GO:0031957 very long-chain fatty acid-CoA ligase activity
Biological Process GO:0006631 fatty acid metabolic process
Biological Process GO:0015908 fatty acid transport
Biological Process GO:0044381 glucose import in response to insulin stimulus
Biological Process GO:1990379 lipid transport across blood-brain barrier
Biological Process GO:0044539 long-chain fatty acid import into cell
Biological Process GO:0001676 long-chain fatty acid metabolic process
Biological Process GO:0015909 long-chain fatty acid transport
Biological Process GO:0001579 medium-chain fatty acid transport
Biological Process GO:0046627 negative regulation of insulin receptor signaling pathway
Biological Process GO:0043065 positive regulation of apoptotic process
Biological Process GO:0007584 response to nutrient
Biological Process GO:0150104 transport across blood-brain barrier

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[3] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[4] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[5] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[6] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[7] 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.

[8] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.