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Overview

Uniprot IDQ8K411
Protein NamePresequence protease, mitochondrial
Gene NamePitrm1
OrganismMus musculus

Kla Sites from experimental identification

Position Flanking peptide
1029 PENSKIAKDPSWIIK
945 VDWAKSGKFTQQDID

Function

Metalloendopeptidase of the mitochondrial matrix that functions in peptide cleavage and degradation rather than in protein processing. Has an ATP-independent activity. Specifically cleaves peptides in the range of 5 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference. Degrades the transit peptides of mitochondrial proteins after their cleavage. Also degrades other unstructured peptides. It is also able to degrade amyloid-beta protein 40, one of the peptides produced by APP processing, when it accumulates in mitochondrion. It is a highly efficient protease, at least toward amyloid-beta protein 40. Cleaves that peptide at a specific position and is probably not processive, releasing digested peptides intermediates that can be further cleaved subsequently. It is also able to degrade amyloid-beta protein 42

Protein Sequence

10 MWRFSGRRGL 20 CAVQRLSCGR 30 VHHRVWREKS 40 DQACERALQY 50 KVGEKIHGFT 60 VNQVTPVPEL 70 FLTAVKLSHD 80 NTGARYLHLA 90 REDKNNLFSV 100 QFRTTPMDST 110 GVPHVLEHTV 120 LCGSQKYPCR 130 DPFFKMLNRS 140 LSTFMNAMTA 150 SDYTIYPFST 160 QNPKDFQNLL 170 SVYLDATFFP 180 CLRELDFWQE 190 GWRLEHENPR 200 DPQTPLIFKG 210 VVFNEMKGAF 220 TDNERIFSQH 230 LQNKLLPDHT 240 YSVVSGGDPL 250 CIPELTWEQL 260 KQFHATHYHP 270 SNARFFTYGN 280 FQLEGHLKQI 290 HEEALSKFQR 300 LEQSTAVPAQ 310 PHWDKPREFH 320 ITCGPDSLAT 330 ETAKQTTVSV 340 SFLLPDITDT 350 FEAFTLSLLS 360 SLLIAGPNSP 370 FYKALIESGL 380 GTDFSPDVGY 390 NGYTREAYFS 400 VGLQGIAEKD 410 VKTVRELVDR 420 TIEEVIEKGF 430 EDDRIEALLH 440 KIEIQTKHQS 450 ASFGLTLTSY 460 IASCWNHDGD 470 PVELLQIGSQ 480 LTRFRKCLKE 490 NPKFLQEKVE 500 QYFKNNQHKL 510 TLSMKPDDKY 520 YEKQTQMETE 530 KLEQKVNSLS 540 PADKQQIYEK 550 GLELQTQQSK 560 HQDASCLPAL 570 KVSDIEPSMP 580 FTKLDIGLAA 590 GDIPVQYCPQ 600 PTNGMVYFRA 610 FSSLNTLPED 620 LRPIVPLFCS 630 VLTKLGCGIL 640 NYREQAQQIE 650 LKTGGMSVTP 660 HVLPDDSQLD 670 TYEQGVLFSS 680 LCLERNLPDM 690 MHLWSEIFNN 700 PCFEEEEHFK 710 VLVKMTAQEL 720 SNGISDSGHL 730 YAALRASKTL 740 TPSGDLQETF 750 SGMDQVKVMK 760 RIAEMTDIKP 770 ILRKLPRIKK 780 YLLNCDNMRC 790 SVNATPQQMP 800 QAEKEVENFL 810 RNVGRSKKER 820 KPVRPHIVEK 830 PTPSGPSGAA 840 HVSGSQIVRK 850 LVTDPTFKPC 860 QMKTHFVLPF 870 PVNYIGECVR 880 TVPYADPDHA 890 SLKILARLMT 900 AKFLHTEIRE 910 KGGAYGGGAK 920 LTHSGIFTLY 930 SYRDPNSIET 940 LQSFGKAVDW 950 AKSGKFTQQD 960 IDEAKLSVFS 970 TVDSPVAPSD 980 KGMDHFLYGL 990 SDEMKQAYRE 1000 QLFAVNHDKL 1010 TSVSHKYLGI 1020 GKSTHGLAIL 1030 GPENSKIAKD PSWIIK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005739 mitochondrion
Molecular Function GO:0004222 metalloendopeptidase activity
Molecular Function GO:0008237 metallopeptidase activity
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0006508 proteolysis
Biological Process GO:0051603 proteolysis involved in protein catabolic process

Reference

[1] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.

[2] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.