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Overview

Uniprot IDQ99424
Protein NamePeroxisomal acyl-coenzyme A oxidase 2
Gene NameACOX2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
52 QNTALRRKVESIIHS
66 SYPEFSCKDNYFMTQ

Function

Involved in peroxisomal beta-oxidation of branched-chain fatty acids (BCFAs) and bile acids intermediates. Catalyzes the initial and rate-limiting dehydrogenation step that removes two hydrogen molecules and introduces a trans double bond between the alpha and beta carbons of the acyl CoA molecules while generating hydrogen peroxide as a by-product. Oxidizes its substrates in a stereospecific way and can only desaturate isomers carrying (2S)-methyl groups (By similarity) (PubMed:29287774). In brown adipose tissue peroxisomes, mediates beta-oxidation of monomethyl branched-chain fatty acids with iso configuration (mmBCFAs) as part of a substrate synthesis and oxidation cycle fueled by FASN-dependent de novo mmBCFA synthesis. The mmBCFA catabolism is coupled to AMPK activation and mitochondrial ATP production as a thermogenic adaptation mechanism to maintain the body temperature in cold environment (By similarity). Metabolizes multi-methyl-branched fatty acyl-CoA esters such as (2S)-pristanoyl-CoA, displaying redundancy with ACOX3 (PubMed:29287774). In the liver, mediates side-chain beta-oxidation of C27 bile acyl-CoA intermediates carrying a (25S)-methyl group to yield 24,25-trans unsaturated derivatives as part of peroxisomal bile acid synthesis pathway (PubMed:27884763, PubMed:29287774). Can oxidize straight-chain fatty acyl CoAs such as C10-CoA and C16-CoA with low efficiency (PubMed:29287774)

Protein Sequence

10 MGSPVHRVSL 20 GDTWSRQMHP 30 DIESERYMQS 40 FDVERLTNIL 50 DGGAQNTALR 60 RKVESIIHSY 70 PEFSCKDNYF 80 MTQNERYKAA 90 MRRAFHIRLI 100 ARRLGWLEDG 110 RELGYAYRAL 120 SGDVALNIHR 130 VFVRALRSLG 140 SEEQIAKWDP 150 LCKNIQIIAT 160 YAQTELGHGT 170 YLQGLETEAT 180 YDAATQEFVI 190 HSPTLTATKW 200 WPGDLGRSAT 210 HALVQAQLIC 220 SGARRGMHAF 230 IVPIRSLQDH 240 TPLPGIIIGD 250 IGPKMDFDQT 260 DNGFLQLNHV 270 RVPRENMLSR 280 FAQVLPDGTY 290 VKLGTAQSNY 300 LPMVVVRVEL 310 LSGEILPILQ 320 KACVIAMRYS 330 VIRRQSRLRP 340 SDPEAKVLDY 350 QTQQQKLFPQ 360 LAISYAFHFL 370 AVSLLEFFQH 380 SYTAILNQDF 390 SFLPELHALS 400 TGMKAMMSEF 410 CTQGAEMCRR 420 ACGGHGYSKL 430 SGLPSLVTKL 440 SASCTYEGEN 450 TVLYLQVARF 460 LVKSYLQTQM 470 SPGSTPQRSL 480 SPSVAYLTAP 490 DLARCPAQRA 500 ADFLCPELYT 510 TAWAHVAVRL 520 IKDSVQHLQT 530 LTQSGADQHE 540 AWNQTTVIHL 550 QAAKVHCYYV 560 TVKGFTEALE 570 KLENEPAIQQ 580 VLKRLCDLHA 590 IHGILTNSGD 600 FLHDAFLSGA 610 QVDMARTAYL 620 DLLRLIRKDA 630 ILLTDAFDFT 640 DQCLNSALGC 650 YDGNVYERLF 660 QWAQKSPTNT 670 QENPAYEEYI 680 RPLLQSWRSK L

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005782 peroxisomal matrix
Cellular Component GO:0005777 peroxisome
Molecular Function GO:0033791 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase activity
Molecular Function GO:0071949 FAD binding
Molecular Function GO:0005504 fatty acid binding
Molecular Function GO:0050660 flavin adenine dinucleotide binding
Molecular Function GO:0120524 long-chain fatty acyl-CoA oxidase activity
Molecular Function GO:0042803 protein homodimerization activity
Biological Process GO:0006699 bile acid biosynthetic process
Biological Process GO:0033540 fatty acid beta-oxidation using acyl-CoA oxidase
Biological Process GO:0000038 very long-chain fatty acid metabolic 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.