Search Results

Overview

Uniprot IDP24752
Protein NameAcetyl-CoA acetyltransferase, mitochondrial
Gene NameACAT1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
174 STPYGGVKLEDLIVK
181 KLEDLIVKDGLTDVY
190 GLTDVYNKIHMGSCA
202 SCAENTAKKLNIARN
223 INSYTRSKAAWEAGK
230 KAAWEAGKFGNEVIP
243 IPVTVTVKGQPDVVV
251 GQPDVVVKEDEEYKR
257 VKEDEEYKRVDFSKV
263 YKRVDFSKVPKLKTV
268 FSKVPKLKTVFQKEN
273 KLKTVFQKENGTVTA
78 AIQGAIEKAGIPKEE
83 IEKAGIPKEEVKEAY
87 GIPKEEVKEAYMGNV

Function

This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA (PubMed:1715688, PubMed:7728148, PubMed:9744475). Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms (PubMed:1715688, PubMed:7728148, PubMed:9744475). The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA (PubMed:17371050). Thereby, it plays a major role in ketone body metabolism (PubMed:1715688, PubMed:17371050, PubMed:7728148, PubMed:9744475)

Protein Sequence

10 MAVLAALLRS 20 GARSRSPLLR 30 RLVQEIRYVE 40 RSYVSKPTLK 50 EVVIVSATRT 60 PIGSFLGSLS 70 LLPATKLGSI 80 AIQGAIEKAG 90 IPKEEVKEAY 100 MGNVLQGGEG 110 QAPTRQAVLG 120 AGLPISTPCT 130 TINKVCASGM 140 KAIMMASQSL 150 MCGHQDVMVA 160 GGMESMSNVP 170 YVMNRGSTPY 180 GGVKLEDLIV 190 KDGLTDVYNK 200 IHMGSCAENT 210 AKKLNIARNE 220 QDAYAINSYT 230 RSKAAWEAGK 240 FGNEVIPVTV 250 TVKGQPDVVV 260 KEDEEYKRVD 270 FSKVPKLKTV 280 FQKENGTVTA 290 ANASTLNDGA 300 AALVLMTADA 310 AKRLNVTPLA 320 RIVAFADAAV 330 EPIDFPIAPV 340 YAASMVLKDV 350 GLKKEDIAMW 360 EVNEAFSLVV 370 LANIKMLEID 380 PQKVNINGGA 390 VSLGHPIGMS 400 GARIVGHLTH 410 ALKQGEYGLA 420 SICNGGGGAS AMLIQKL

Gene Ontology

Classification GO ID Description
Molecular Function GO:0003985 acetyl-CoA C-acetyltransferase activity
Cellular Component GO:0005783 endoplasmic reticulum
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005739 mitochondrion
Molecular Function GO:0016453 C-acetyltransferase activity
Molecular Function GO:0034736 cholesterol O-acyltransferase activity
Molecular Function GO:0120225 coenzyme A binding
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0030955 potassium ion binding
Biological Process GO:0006085 acetyl-CoA biosynthetic process
Biological Process GO:0046356 acetyl-CoA catabolic process
Biological Process GO:0060612 adipose tissue development
Biological Process GO:0015937 coenzyme A biosynthetic process
Biological Process GO:0015936 coenzyme A metabolic process
Biological Process GO:0006635 fatty acid beta-oxidation
Biological Process GO:0046952 ketone body catabolic process
Biological Process GO:1902224 ketone body metabolic process
Biological Process GO:0006550 L-isoleucine catabolic process
Biological Process GO:0001889 liver development
Biological Process GO:0072229 metanephric proximal convoluted tubule development
Biological Process GO:1902860 propionyl-CoA biosynthetic process
Biological Process GO:0009725 response to hormone
Biological Process GO:0042594 response to starvation

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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[4] 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.