Search Results

Overview

Uniprot IDQ5JRX3
Protein NamePresequence protease, mitochondrial
Gene NamePITRM1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1027 ILGPENPKIAKDPSW
550 ELRSQQSKPQDASCL
770 RKLPRIKKHLLNGDN

Function

Metalloendopeptidase of the mitochondrial matrix that functions in peptide cleavage and degradation rather than in protein processing (PubMed:10360838, PubMed:16849325, PubMed:19196155, PubMed:24931469). Has an ATP-independent activity (PubMed:16849325). Specifically cleaves peptides in the range of 5 to 65 residues (PubMed:19196155). Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference (PubMed:10360838, PubMed:19196155, PubMed:24931469). Degrades the transit peptides of mitochondrial proteins after their cleavage (PubMed:19196155). Also degrades other unstructured peptides (PubMed:19196155). It is also able to degrade amyloid-beta protein 40, one of the peptides produced by APP processing, when it accumulates in mitochondrion (PubMed:16849325, PubMed:24931469, PubMed:26697887). It is a highly efficient protease, at least toward amyloid-beta protein 40 (PubMed:24931469, PubMed:29383861, PubMed:29764912). Cleaves that peptide at a specific position and is probably not processive, releasing digested peptides intermediates that can be further cleaved subsequently (PubMed:24931469). It is also able to degrade amyloid-beta protein 42 (PubMed:29764912)

Protein Sequence

10 MWRCGGRQGL 20 CVLRRLSGGH 30 AHHRAWRWNS 40 NRACERALQY 50 KLGDKIHGFT 60 VNQVTSVPEL 70 FLTAVKLTHD 80 DTGARYLHLA 90 REDTNNLFSV 100 QFRTTPMDST 110 GVPHILEHTV 120 LCGSQKYPCR 130 DPFFKMLNRS 140 LSTFMNAFTA 150 SDYTLYPFST 160 QNPKDFQNLL 170 SVYLDATFFP 180 CLRELDFWQE 190 GWRLEHENPS 200 DPQTPLVFKG 210 VVFNEMKGAF 220 TDNERIFSQH 230 LQNRLLPDHT 240 YSVVSGGDPL 250 CIPELTWEQL 260 KQFHATHYHP 270 SNARFFTYGN 280 FPLEQHLKQI 290 HEEALSKFQK 300 IEPSTVVPAQ 310 TPWDKPREFQ 320 ITCGPDSFAT 330 DPSKQTTISV 340 SFLLPDITDT 350 FEAFTLSLLS 360 SLLTSGPNSP 370 FYKALIESGL 380 GTDFSPDVGY 390 NGYTREAYFS 400 VGLQGIAEKD 410 IETVRSLIDR 420 TIDEVVEKGF 430 EDDRIEALLH 440 KIEIQMKHQS 450 TSFGLMLTSY 460 IASCWNHDGD 470 PVELLKLGNQ 480 LAKFRQCLQE 490 NPKFLQEKVK 500 QYFKNNQHKL 510 TLSMRPDDKY 520 HEKQAQVEAT 530 KLKQKVEALS 540 PGDRQQIYEK 550 GLELRSQQSK 560 PQDASCLPAL 570 KVSDIEPTIP 580 VTELDVVLTA 590 GDIPVQYCAQ 600 PTNGMVYFRA 610 FSSLNTLPEE 620 LRPYVPLFCS 630 VLTKLGCGLL 640 DYREQAQQIE 650 LKTGGMSASP 660 HVLPDDSHMD 670 TYEQGVLFSS 680 LCLDRNLPDM 690 MQLWSEIFNN 700 PCFEEEEHFK 710 VLVKMTAQEL 720 ANGIPDSGHL 730 YASIRAGRTL 740 TPAGDLQETF 750 SGMDQVRLMK 760 RIAEMTDIKP 770 ILRKLPRIKK 780 HLLNGDNMRC 790 SVNATPQQMP 800 QTEKAVEDFL 810 RSIGRSKKER 820 RPVRPHTVEK 830 PVPSSSGGDA 840 HVPHGSQVIR 850 KLVMEPTFKP 860 WQMKTHFLMP 870 FPVNYVGECI 880 RTVPYTDPDH 890 ASLKILARLM 900 TAKFLHTEIR 910 EKGGAYGGGA 920 KLSHNGIFTL 930 YSYRDPNTIE 940 TLQSFGKAVD 950 WAKSGKFTQQ 960 DIDEAKLSVF 970 STVDAPVAPS 980 DKGMDHFLYG 990 LSDEMKQAHR 1000 EQLFAVSHDK 1010 LLAVSDRYLG 1020 TGKSTHGLAI 1030 LGPENPKIAK DPSWIIQ

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005739 mitochondrion
Molecular Function GO:0008047 enzyme activator activity
Molecular Function GO:0004222 metalloendopeptidase activity
Molecular Function GO:0008237 metallopeptidase activity
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0006626 protein targeting to mitochondrion
Biological Process GO:0006508 proteolysis
Biological Process GO:0051603 proteolysis involved in protein catabolic 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.