CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017278
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Presequence protease, mitochondrial 
Protein Synonyms/Alias
 Pitrilysin metalloproteinase 1 
Gene Name
 Pitrm1 
Gene Synonyms/Alias
 Kiaa1104; Ntup1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
41CERALQYKVGEKIHGacetylation[1, 2]
41CERALQYKVGEKIHGsuccinylation[2]
84LHLAREDKNNLFSVQacetylation[3]
305PAQPHWDKPREFHITacetylation[4]
483KCLKENPKFLQEKVEacetylation[1]
488NPKFLQEKVEQYFKNacetylation[1]
505HKLTLSMKPDDKYYEacetylation[4]
550ELQTQQSKHQDASCLacetylation[1, 2]
747FSGMDQVKVMKRIAEacetylation[3]
759IAEMTDIKPILRKLPacetylation[1, 2, 3, 5]
770RKLPRIKKYLLNCDNacetylation[1, 2, 6]
770RKLPRIKKYLLNCDNsuccinylation[2]
811GRSKKERKPVRPHIVacetylation[1]
840SGSQIVRKLVTDPTFacetylation[1]
848LVTDPTFKPCQMKTHacetylation[1, 2, 4, 5]
848LVTDPTFKPCQMKTHsuccinylation[2]
883DPDHASLKILARLMTacetylation[1, 2, 3, 4, 5, 6]
883DPDHASLKILARLMTsuccinylation[2]
892LARLMTAKFLHTEIRacetylation[1]
942GKAVDWAKSGKFTQQacetylation[2, 4, 6]
942GKAVDWAKSGKFTQQsuccinylation[2]
945VDWAKSGKFTQQDIDacetylation[1, 2, 4, 5, 6, 7]
945VDWAKSGKFTQQDIDsuccinylation[2]
1006KLTSVSHKYLGIGKSacetylation[1]
1026ILGPENSKIAKDPSWacetylation[2]
1026ILGPENSKIAKDPSWsuccinylation[2]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [6] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [7] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758] 
Functional Description
 ATP-independent protease that degrades mitochondrial transit peptides after their cleavage. Also degrades other unstructured peptides. Specific for peptides in the range of 10 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference (By similarity). 
Sequence Annotation
 ACT_SITE 107 107 Proton acceptor (By similarity).
 METAL 104 104 Zinc; catalytic (By similarity).
 METAL 108 108 Zinc; catalytic (By similarity).
 METAL 205 205 Zinc; catalytic (By similarity).
 DISULFID 119 556 By similarity.  
Keyword
 Alternative splicing; Complete proteome; Disulfide bond; Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease; Reference proteome; Transit peptide; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1036 AA 
Protein Sequence
MWRFSGRRGL CAVQRLSCGR VHHRVWREKS DQACERALQY KVGEKIHGFT VNQVTPVPEL 60
FLTAVKLSHD NTGARYLHLA REDKNNLFSV QFRTTPMDST GVPHVLEHTV LCGSQKYPCR 120
DPFFKMLNRS LSTFMNAMTA SDYTIYPFST QNPKDFQNLL SVYLDATFFP CLRELDFWQE 180
GWRLEHENPR DPQTPLIFKG VVFNEMKGAF TDNERIFSQH LQNKLLPDHT YSVVSGGDPL 240
CIPELTWEQL KQFHATHYHP SNARFFTYGN FQLEGHLKQI HEEALSKFQR LEQSTAVPAQ 300
PHWDKPREFH ITCGPDSLAT ETAKQTTVSV SFLLPDITDT FEAFTLSLLS SLLIAGPNSP 360
FYKALIESGL GTDFSPDVGY NGYTREAYFS VGLQGIAEKD VKTVRELVDR TIEEVIEKGF 420
EDDRIEALLH KIEIQTKHQS ASFGLTLTSY IASCWNHDGD PVELLQIGSQ LTRFRKCLKE 480
NPKFLQEKVE QYFKNNQHKL TLSMKPDDKY YEKQTQMETE KLEQKVNSLS PADKQQIYEK 540
GLELQTQQSK HQDASCLPAL KVSDIEPSMP FTKLDIGLAA GDIPVQYCPQ PTNGMVYFRA 600
FSSLNTLPED LRPIVPLFCS VLTKLGCGIL NYREQAQQIE LKTGGMSVTP HVLPDDSQLD 660
TYEQGVLFSS LCLERNLPDM MHLWSEIFNN PCFEEEEHFK VLVKMTAQEL SNGISDSGHL 720
YAALRASKTL TPSGDLQETF SGMDQVKVMK RIAEMTDIKP ILRKLPRIKK YLLNCDNMRC 780
SVNATPQQMP QAEKEVENFL RNVGRSKKER KPVRPHIVEK PTPSGPSGAA HVSGSQIVRK 840
LVTDPTFKPC QMKTHFVLPF PVNYIGECVR TVPYADPDHA SLKILARLMT AKFLHTEIRE 900
KGGAYGGGAK LTHSGIFTLY SYRDPNSIET LQSFGKAVDW AKSGKFTQQD IDEAKLSVFS 960
TVDSPVAPSD KGMDHFLYGL SDEMKQAYRE QLFAVNHDKL TSVSHKYLGI GKSTHGLAIL 1020
GPENSKIAKD PSWIIK 1036 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
 GO:0006508; P:proteolysis; ISS:UniProtKB. 
Interpro
 IPR011249; Metalloenz_LuxS/M16.
 IPR011237; Pept_M16_dom.
 IPR011765; Pept_M16_N.
 IPR007863; Peptidase_M16_C.
 IPR013578; Peptidase_M16C_assoc. 
Pfam
 PF08367; M16C_assoc
 PF00675; Peptidase_M16
 PF05193; Peptidase_M16_C 
SMART
  
PROSITE
 PS00143; INSULINASE 
PRINTS