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Overview

Uniprot IDP51659
Protein NamePeroxisomal multifunctional enzyme type 2
Gene NameHSD17B4
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
139 RAAWEHMKKQKYGRI
184 SLAIEGRKSNIHCNT
260 LGAIVRQKNHPMTPE
270 PMTPEAVKANWKKIC
275 AVKANWKKICDFENA
415 EQYLELYKPLPRAGK
424 LPRAGKLKCEAVVAD
46 NDLGGDFKGVGKGSL
50 GDFKGVGKGSLAADK
565 AIKARFAKPVYPGQT
57 KGSLAADKVVEEIRR
614 PTSGTSAKTPSEGGK
621 KTPSEGGKLQSTFVF
636 EEIGRRLKDIGPEVV
644 DIGPEVVKKVNAVFE
645 IGPEVVKKVNAVFEW
663 KGGNIGAKWTIDLKS
674 DLKSGSGKVYQGPAK
68 EIRRRGGKAVANYDS
707 LGKLDPQKAFFSGRL
725 GNIMLSQKLQMILKD
731 QKLQMILKDYAKL**
81 DSVEEGEKVVKTALD
84 EEGEKVVKTALDAFG

Function

Bifunctional enzyme acting on the peroxisomal fatty acid beta-oxidation pathway. Catalyzes two of the four reactions in fatty acid degradation: hydration of 2-enoyl-CoA (trans-2-enoyl-CoA) to produce (3R)-3-hydroxyacyl-CoA, and dehydrogenation of (3R)-3-hydroxyacyl-CoA to produce 3-ketoacyl-CoA (3-oxoacyl-CoA), which is further metabolized by SCPx. Can use straight-chain and branched-chain fatty acids, as well as bile acid intermediates as substrates. May play a role in peroxisomal beta-oxidation step in polyunsaturated fatty acids (PUFAs) biosynthesis. Possibly regulates systemic levels of docosahexaenoic acid (DHA, C22:6n-3) through a process involving endoplasmic reticulum desaturation and elongation of alpha-linolenic acid (ALA, C18:3n-3) to form tetracosahexaenoic acid (THA, C24:6n-3), which is then beta-oxidized to DHA in peroxisomes

Protein Sequence

10 MGSPLRFDGR 20 VVLVTGAGAG 30 LGRAYALAFA 40 ERGALVVVND 50 LGGDFKGVGK 60 GSLAADKVVE 70 EIRRRGGKAV 80 ANYDSVEEGE 90 KVVKTALDAF 100 GRIDVVVNNA 110 GILRDRSFAR 120 ISDEDWDIIH 130 RVHLRGSFQV 140 TRAAWEHMKK 150 QKYGRIIMTS 160 SASGIYGNFG 170 QANYSAAKLG 180 LLGLANSLAI 190 EGRKSNIHCN 200 TIAPNAGSRM 210 TQTVMPEDLV 220 EALKPEYVAP 230 LVLWLCHESC 240 EENGGLFEVG 250 AGWIGKLRWE 260 RTLGAIVRQK 270 NHPMTPEAVK 280 ANWKKICDFE 290 NASKPQSIQE 300 STGSIIEVLS 310 KIDSEGGVSA 320 NHTSRATSTA 330 TSGFAGAIGQ 340 KLPPFSYAYT 350 ELEAIMYALG 360 VGASIKDPKD 370 LKFIYEGSSD 380 FSCLPTFGVI 390 IGQKSMMGGG 400 LAEIPGLSIN 410 FAKVLHGEQY 420 LELYKPLPRA 430 GKLKCEAVVA 440 DVLDKGSGVV 450 IIMDVYSYSE 460 KELICHNQFS 470 LFLVGSGGFG 480 GKRTSDKVKV 490 AVAIPNRPPD 500 AVLTDTTSLN 510 QAALYRLSGD 520 WNPLHIDPNF 530 ASLAGFDKPI 540 LHGLCTFGFS 550 ARRVLQQFAD 560 NDVSRFKAIK 570 ARFAKPVYPG 580 QTLQTEMWKE 590 GNRIHFQTKV 600 QETGDIVISN 610 AYVDLAPTSG 620 TSAKTPSEGG 630 KLQSTFVFEE 640 IGRRLKDIGP 650 EVVKKVNAVF 660 EWHITKGGNI 670 GAKWTIDLKS 680 GSGKVYQGPA 690 KGAADTTIIL 700 SDEDFMEVVL 710 GKLDPQKAFF 720 SGRLKARGNI 730 MLSQKLQMIL KDYAKL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0016020 membrane
Cellular Component GO:0005782 peroxisomal matrix
Cellular Component GO:0005778 peroxisomal membrane
Cellular Component GO:0005777 peroxisome
Molecular Function GO:0080023 (2E)-enoyl-CoA hydratase activity
Molecular Function GO:0106386 (3R)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
Molecular Function GO:0003857 (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
Molecular Function GO:0018812 3-hydroxyacyl-CoA dehydratase activity
Molecular Function GO:0033989 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity
Molecular Function GO:0004300 enoyl-CoA hydratase activity
Molecular Function GO:0004303 estradiol 17-beta-dehydrogenase [NAD(P)+] activity
Molecular Function GO:0016853 isomerase activity
Molecular Function GO:0042803 protein homodimerization activity
Biological Process GO:0008209 androgen metabolic process
Biological Process GO:0008210 estrogen metabolic process
Biological Process GO:0006635 fatty acid beta-oxidation
Biological Process GO:0033540 fatty acid beta-oxidation using acyl-CoA oxidase
Biological Process GO:0006633 fatty acid biosynthetic process
Biological Process GO:0036112 medium-chain fatty-acyl-CoA metabolic process
Biological Process GO:0001649 osteoblast differentiation
Biological Process GO:0036111 very long-chain fatty-acyl-CoA 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.

[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 J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.