CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020980
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Mitochondrial-processing peptidase subunit alpha 
Protein Synonyms/Alias
 Alpha-MPP; P-55 
Gene Name
 Pmpca 
Gene Synonyms/Alias
 Inpp5e 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
298QYTGGIIKVERDMSNacetylation[1]
459VLATHSRKLPHELCTacetylation[2]
472CTLIRNVKPEDIKRVacetylation[1]
477NVKPEDIKRVASKMLacetylation[1, 3]
Reference
 [1] 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]
 [2] 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]
 [3] 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
Functional Description
 Cleaves presequences (transit peptides) from mitochondrial protein precursors (By similarity). 
Sequence Annotation
 MOD_RES 298 298 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Complete proteome; Direct protein sequencing; Hydrolase; Metalloprotease; Mitochondrion; Protease; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 524 AA 
Protein Sequence
MATAVWAAAR LLRGSAVLCA RPRFGSPAHR RFSSGATYPN IPLSSPLPGV PKPIFATVDG 60
QEKFETKVTT LDNGLRVASQ NKFGQFCTVG ILINSGSRYE AKYLSGIAHF LEKLAFSSTA 120
RFDSKDEILL TLEKHGGICD CQTSRDTTMY AVSADSKGLD TVVDLLADVV LHPRLTDEEI 180
EMTRMAVQFE LEDLNMRPDP EPLLTEMIHE AAFRENTVGL HRFCPVENIA KIDREVLHSY 240
LKNYYTPDRM VLAGVGVEHE HLVECARKYL VGAEPAWGAP GTVDVDRSVA QYTGGIIKVE 300
RDMSNVSLGP TPIPELTHIM VGLESCSFLE DDFIPFAVLN MMMGGGGSFS AGGPGKGMFS 360
RLYLNVLNRH HWMYNATSYH HSYEDTGLLC IHASADPRQV REMVEIITKE FILMGRTVDL 420
VELERAKTQL MSMLMMNLES RPVIFEDVGR QVLATHSRKL PHELCTLIRN VKPEDIKRVA 480
SKMLRGKPAV AALGDLTDLP TYEHIQAALS SRNGHLPRSY RLFR 524 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0046872; F:metal ion binding; IEA:InterPro.
 GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR011249; Metalloenz_LuxS/M16.
 IPR011237; Pept_M16_dom.
 IPR011765; Pept_M16_N.
 IPR001431; Pept_M16_Zn_BS.
 IPR007863; Peptidase_M16_C. 
Pfam
 PF00675; Peptidase_M16
 PF05193; Peptidase_M16_C 
SMART
  
PROSITE
 PS00143; INSULINASE 
PRINTS