Search Results

Overview

Uniprot IDQ709F0
Protein NameAcyl-CoA dehydrogenase family member 11
Gene NameACAD11
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
19 AEVLPQHKFDSKSLE
414 QNENSVDKWGKPLVI
663 QRIAFKKKLYAHEVV
683 ESRIAIEKIRLLTLK

Function

Participates in fatty acid beta-oxidation (FAO) and energy production in the central nervous system (CNS), and to a lesser extent in the liver (PubMed:21237683). Catalyzes the first step in FAO, which consists in the proR-proR stereospecific alpha,beta-dehydrogenation of fatty acyl-CoA thioesters using the electron transfer flavoprotein (ETF) as their physiologic electron acceptor, with maximal activity towards saturated docosanoyl-CoA (CoA 22:0) in both the cerebellum and the liver (PubMed:21237683). Among the different mitochondrial acyl-CoA dehydrogenases, its FAO activity overlaps with that of ACADV and ACADL, but plays a primary role in tissues where it is the main long-chain ACAD expressed, such as the CNS, where together with ACAD9, they accommodate the full spectrum of long chain fatty acid substrates (PubMed:21237683)

Protein Sequence

10 MKPGATGESD 20 LAEVLPQHKF 30 DSKSLEAYLN 40 QHLSGFGAER 50 EATLTIAQYR 60 AGKSNPTFYL 70 QKGFQTYVLR 80 KKPPGSLLPK 90 AHQIDREFKV 100 QKALFSIGFP 110 VPKPILYCSD 120 TSVIGTEFYV 130 MEHVQGRIFR 140 DLTIPGLSPA 150 ERSAIYVATV 160 ETLAQLHSLN 170 IQSLQLEGYG 180 IGAGYCKRQV 190 STWTKQYQAA 200 AHQDIPAMQQ 210 LSEWLMKNLP 220 DNDNEENLIH 230 GDFRLDNIVF 240 HPKECRVIAV 250 LDWELSTIGH 260 PLSDLAHFSL 270 FYFWPRTVPM 280 INQGSYSENS 290 GIPSMEELIS 300 IYCRCRGINS 310 ILPNWNFFLA 320 LSYFKMAGIA 330 QGVYSRYLLG 340 NNSSEDSFLF 350 ANIVQPLAET 360 GLQLSKRTFS 370 TVLPQIDTTG 380 QLFVQTRKGQ 390 EVLIKVKHFM 400 KQHILPAEKE 410 VTEFYVQNEN 420 SVDKWGKPLV 430 IDKLKEMAKV 440 EGLWNLFLPA 450 VSGLSHVDYA 460 LIAEETGKCF 470 FAPDVFNCQA 480 PDTGNMEVLH 490 LYGSEEQKKQ 500 WLEPLLQGNI 510 TSCFCMTEPD 520 VASSDATNIE 530 CSIQRDEDSY 540 VINGKKWWSS 550 GAGNPKCKIA 560 IVLGRTQNTS 570 LSRHKQHSMI 580 LVPMNTPGVK 590 IIRPLSVFGY 600 TDNFHGGHFE 610 IHFNQVRVPA 620 TNLILGEGRG 630 FEISQGRLGP 640 GRIHHCMRTV 650 GLAERALQIM 660 CERATQRIAF 670 KKKLYAHEVV 680 AHWIAESRIA 690 IEKIRLLTLK 700 AAHSMDTLGS 710 AGAKKEIAMI 720 KVAAPRAVSK 730 IVDWAIQVCG 740 GAGVSQDYPL 750 ANMYAITRVL 760 RLADGPDEVH 770 LSAIATMELR 780 DQAKRLTAKI

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005743 mitochondrial inner membrane
Cellular Component GO:0031966 mitochondrial membrane
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005777 peroxisome
Molecular Function GO:0003995 acyl-CoA dehydrogenase activity
Molecular Function GO:0050660 flavin adenine dinucleotide binding
Molecular Function GO:0004466 long-chain fatty acyl-CoA dehydrogenase activity
Molecular Function GO:0070991 medium-chain fatty acyl-CoA dehydrogenase activity
Molecular Function GO:0017099 very-long-chain fatty acyl-CoA dehydrogenase activity
Biological Process GO:0006635 fatty acid beta-oxidation
Biological Process GO:0033539 fatty acid beta-oxidation using acyl-CoA dehydrogenase

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] 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.

[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.