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Overview

Uniprot IDA0A8I5ZWG5
Protein NamePresequence protease, mitochondrial
Gene NamePitrm1
OrganismRattus norvegicus

Kla Sites from experimental identification

Position Flanking peptide
1010 PENSKLAKDPSWIIR

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 MVHHKVWREK 20 SDQACDRALQ 30 YKVGEKIHGF 40 TVNQVTPVPE 50 LFLTAVKLSH 60 DNTGARYLHL 70 AREDNNNLFS 80 VQFRTTPMDS 90 TGVPHVLEHT 100 VLCGSQKYPC 110 RDPFFKMLNR 120 SLSTFMNAFT 130 ASDYTMYPFS 140 TQNPKDFQNL 150 LSVYLDATFF 160 PCLRELDFWQ 170 EGWRLEHEDP 180 SDPQTPLIFK 190 GVVFNEMKGA 200 FTDNERIFSQ 210 HLQNKLLPDH 220 TYSVVSGGDP 230 LCIPELTWEQ 240 LKQFHTTHYH 250 PSNARFFTYG 260 NFPLEDHLKQ 270 IHEEALSKFQ 280 KMEESTAVPA 290 QKYWDKPREF 300 HITCGPDSLA 310 TDATKQTTVS 320 VSFLLPDITN 330 TFEAFTLNLL 340 SSLLISGPNS 350 PFYKALIESG 360 LGTDFSPDVG 370 YNGYTREAYF 380 SVGLQGIAEN 390 DVKTVRELVD 400 RTIEEVIEKG 410 FEDDQIEALL 420 HKIEIQMKHQ 430 SASFGMALTS 440 YIASCWNHDG 450 DPVELLQMGS 460 QLTKFRKCLK 470 ENPKFLQEKV 480 EQYFKNNPHR 490 LTLSMKPDDR 500 YYEKQTQMET 510 EKLEQKVNSL 520 SQADKKQIYE 530 KGLELQKQQS 540 KHQDASCLPA 550 LKVSDIEPTM 560 PFTKFDIALS 570 AGDVPVQYCP 580 QPTNGIVYFR 590 AFSSLNTLPE 600 ELRPFVPLFC 610 TVLTKLGCGI 620 LNYREQAQQI 630 ELKTGGMTVT 640 PHVLPDDSQL 650 DTYEQGVLFS 660 SLCLERNLPD 670 MMHLWSEIFN 680 NPCFEEEEHF 690 KVLVRMSAQE 700 LSNGIPDSGH 710 LYAALRAGKT 720 LTPAGDLQET 730 FSGMDQVKVM 740 KRIAEMTDIK 750 PILRKLPRIK 760 KYLLNCDNMR 770 CSVNATPQQM 780 PQAEKEVENF 790 LRNVGRSKKE 800 RKPVRPHIVE 810 KPTPSGPSGG 820 AHADGSQIIR 830 KLITDPTFKP 840 CQMKTHFVLP 850 FPVNYVGECV 860 RTVPYADPDH 870 ASLKILARLM 880 TAKFLHTEIR 890 EKGGAYGGGA 900 KVTHTGIFTL 910 YSYRDPNSIE 920 TLQSFGKAID 930 WAKSGKFTQQ 940 DIDEAKLSVF 950 SAVDSPVAPS 960 DKGMDHFLYG 970 LSDEMKQTYR 980 EQLFAVTHDK 990 LTSVSHKYLG 1000 IGKSTHGLAI 1010 LGPENSKLAK DPSWIIR

Gene Ontology

Classification GO ID Description
Biological Process GO:0006508 proteolysis
Cellular Component GO:0005759 mitochondrial matrix
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0008237 metallopeptidase activity

Reference

[1] Chen Y, Sun W, Sun Z, Zhao H, Wu T et al.. Effect of electroacupuncture on hippocampal protein lactylation in a rat model of vascular dementia.. Front Neurol 16:1629474. 2025. PMID: 40963935.