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Overview

Uniprot IDI3L7T4
Protein NameLon protease homolog, mitochondrial
Gene NameLONP1
OrganismSus scrofa

Kla Sites from experimental identification

Position Flanking peptide
141 PVFPRFIKIVEVKNK
393 KIKQTHRKYLLQEQL
578 GKIIQCLKKTKTENP
688 QCGLDESKAKLSSDV

Function

ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single-stranded, site-specific, and strand-specific manner. May regulate mitochondrial DNA replication and/or gene expression using site-specific, single-stranded DNA binding to target the degradation of regulatory proteins binding to adjacent sites in mitochondrial promoters

Protein Sequence

10 MAAGAGCVRL 20 WGAARWWALR 30 RPLLAAAAGR 40 VPTAVRAWLP 50 RGRRACDASP 60 PWAQWGQGPA 70 AAGHWRGLWE 80 ANNRSSGGAF 90 SGGEDAPEGG 100 AEDGASGVGG 110 NAGGGEGPVI 120 TALTPMTIPD 130 VFPHLPLIAV 140 TRNPVFPRFI 150 KIVEVKNKKL 160 VELLRRKVRL 170 AQPYAGVFLK 180 RDDNNESDVV 190 ESLDEIYHTG 200 TFVQIHEMQD 210 LGDKLRMIVM 220 GHRRVHINRQ 230 LEVEPEEPEG 240 EKQKPRRKPK 250 RSKKEVEEDG 260 GAKQQVEVVV 270 EPGLSPTGEV 280 LMVEVENVVH 290 EDFQVTEEVK 300 ALTAEIVKTI 310 RDIIALNPLY 320 RESVLQMMQA 330 GHRVVDNPIY 340 LSDMGAALTG 350 AESHELQDVL 360 EETNIPKRLY 370 KALSLLKKEF 380 ELSKLQQRLG 390 REVEEKIKQT 400 HRKYLLQEQL 410 KIIKKELGLE 420 KDDKDAIEEK 430 FRERLKELVV 440 PKHVMDVVDE 450 ELSKLGLLDN 460 HSSEFNVTRN 470 YLDWLTSIPW 480 GKYSDENLDL 490 ARAQAVLEED 500 HYGMEDVKKR 510 ILEFIAVSQL 520 RGSTQGKILC 530 FYGPPGVGKT 540 SIARSIARAL 550 NREYFRFSVG 560 GMTDVAEIKG 570 HRRTYVGAMP 580 GKIIQCLKKT 590 KTENPLVLID 600 EVDKIGRGYQ 610 GDPSSALLEL 620 LDPEQNANFL 630 DHYLDVPVDL 640 SKVLFICTAN 650 ITETIPEPLR 660 DRMEMINVSG 670 YVAQEKLAIA 680 ERYLVPQARA 690 QCGLDESKAK 700 LSSDVLTLLI 710 KQYCRESGVR 720 NLQKQVEKVL 730 RKSAYKIVSG 740 EAEFVEVTPE 750 NLQDFVGKPV 760 FTVERMYDVT 770 PPGVVMGLAW 780 TAMGGSTLFV 790 ETSLRRPRDR 800 DSTKGDKDGS 810 LEVTGQLGEV 820 MKESARIAYT 830 FARAFLMQHD 840 PTNEYLVTSH 850 IHLHVPEGAT 860 PKDGPSAGCT 870 IVTALLSLAM 880 DRPVRQNLAM 890 TGEVSLTGKV 900 LPVGGIKEKT 910 IAAKRAGVTC 920 IVLPAENKKD 930 FYDLAAFITE 940 GLEVHFVEHY 950 REIFDIAFPE 960 EQAEALAVER

Gene Ontology

Classification GO ID Description
Molecular Function GO:0042802 identical protein binding
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0042645 mitochondrial nucleoid
Molecular Function GO:0043531 ADP binding
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0004176 ATP-dependent peptidase activity
Molecular Function GO:0070182 DNA polymerase binding
Molecular Function GO:0051880 G-quadruplex DNA binding
Molecular Function GO:0043560 insulin receptor substrate binding
Molecular Function GO:0001018 mitochondrial promoter sequence-specific DNA binding
Molecular Function GO:0042731 PH domain binding
Molecular Function GO:0004252 serine-type endopeptidase activity
Molecular Function GO:0003697 single-stranded DNA binding
Molecular Function GO:0003727 single-stranded RNA binding
Biological Process GO:0034599 cellular response to oxidative stress
Biological Process GO:0051131 chaperone-mediated protein complex assembly
Biological Process GO:0035694 mitochondrial protein catabolic process
Biological Process GO:0007005 mitochondrion organization
Biological Process GO:0070407 oxidation-dependent protein catabolic process
Biological Process GO:0006515 protein quality control for misfolded or incompletely synthesized proteins
Biological Process GO:0001666 response to hypoxia

Reference

[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.