Search Results

Overview

Uniprot IDA0A0G2K6D5
Protein NamePresequence protease, mitochondrial
Gene NamePitrm1
OrganismRattus norvegicus

Kla Sites from experimental identification

Position Flanking peptide
1028 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 MWRFSGRRGL 20 CAVQRLSSGV 30 HHKVWREKSD 40 QACDRALQYK 50 VGEKIHGFTV 60 NQVTPVPELF 70 LTAVKLSHDN 80 TGARYLHLAR 90 EDNNNLFSVQ 100 FRTTPMDSTG 110 VPHVLEHTVL 120 CGSQKYPCRD 130 PFFKMLNRSL 140 STFMNAFTAS 150 DYTMYPFSTQ 160 NPKDFQNLLS 170 VYLDATFFPC 180 LRELDFWQEG 190 WRLEHEDPSD 200 PQTPLIFKGV 210 VFNEMKGAFT 220 DNERIFSQHL 230 QNKLLPDHTY 240 SVVSGGDPLC 250 IPELTWEQLK 260 QFHTTHYHPS 270 NARFFTYGNF 280 PLEDHLKQIH 290 EEALSKFQKM 300 EESTAVPAQK 310 YWDKPREFHI 320 TCGPDSLATD 330 ATKQTTVSVS 340 FLLPDITNTF 350 EAFTLNLLSS 360 LLISGPNSPF 370 YKALIESGLG 380 TDFSPDVGYN 390 GYTREAYFSV 400 GLQGIAENDV 410 KTVRELVDRT 420 IEEVIEKGFE 430 DDQIEALLHK 440 IEIQMKHQSA 450 SFGMALTSYI 460 ASCWNHDGDP 470 VELLQMGSQL 480 TKFRKCLKEN 490 PKFLQEKVEQ 500 YFKNNPHRLT 510 LSMKPDDRYY 520 EKQTQMETEK 530 LEQKVNSLSQ 540 ADKKQIYEKG 550 LELQKQQSKH 560 QDASCLPALK 570 VSDIEPTMPF 580 TKFDIALSAG 590 DVPVQYCPQP 600 TNGIVYFRAF 610 SSLNTLPEEL 620 RPFVPLFCTV 630 LTKLGCGILN 640 YREQAQQIEL 650 KTGGMTVTPH 660 VLPDDSQLDT 670 YEQGVLFSSL 680 CLERNLPDMM 690 HLWSEIFNNP 700 CFEEEEHFKV 710 LVRMSAQELS 720 NGIPDSGHLY 730 AALRAGKTLT 740 PAGDLQETFS 750 GMDQVKVMKR 760 IAEMTDIKPI 770 LRKLPRIKKY 780 LLNCDNMRCS 790 VNATPQQMPQ 800 AEKEVENFLR 810 NVGRSKKERK 820 PVRPHIVEKP 830 TPSGPSGGAH 840 ADGSQIIRKL 850 ITDPTFKPCQ 860 MKTHFVLPFP 870 VNYVGECVRT 880 VPYADPDHAS 890 LKILARLMTA 900 KFLHTEIREK 910 GGAYGGGAKV 920 THTGIFTLYS 930 YRDPNSIETL 940 QSFGKAIDWA 950 KSGKFTQQDI 960 DEAKLSVFSA 970 VDSPVAPSDK 980 GMDHFLYGLS 990 DEMKQTYREQ 1000 LFAVTHDKLT 1010 SVSHKYLGIG 1020 KSTHGLAILG 1030 PENSKLAKDP SWIIR

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005759 mitochondrial matrix
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
Cellular Component GO:0005739 mitochondrion
Molecular Function GO:0004222 metalloendopeptidase 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.