CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019181
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Metalloendopeptidase OMA1, mitochondrial 
Protein Synonyms/Alias
 Metalloprotease-related protein 1; MPRP-1; Overlapping with the m-AAA protease 1 homolog 
Gene Name
 OMA1 
Gene Synonyms/Alias
 MPRP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
230SKLLLLGKEQFRLLSubiquitination[1]
478PDPRLLFKLSTKHFLubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 Metalloprotease that is part of the quality control system in the inner membrane of mitochondria. Following stress conditions that induce loss of mitochondrial membrane potential, mediates cleavage of OPA1 at S1 position, leading to OPA1 inactivation and negative regulation of mitochondrial fusion. Its role in mitochondrial quality control is essential for regulating lipid metabolism as well as to maintain body temperature and energy expenditure under cold-stress conditions. 
Sequence Annotation
 ACT_SITE 328 328 By similarity.
 METAL 327 327 Zinc; catalytic (By similarity).
 METAL 331 331 Zinc; catalytic (Probable).
 METAL 392 392 Zinc; catalytic (By similarity).  
Keyword
 Alternative splicing; Complete proteome; Hydrolase; Membrane; Metal-binding; Metalloprotease; Mitochondrion; Mitochondrion inner membrane; Polymorphism; Protease; Reference proteome; Transit peptide; Transmembrane; Transmembrane helix; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 524 AA 
Protein Sequence
MSFICGLQSA ARNHVFFRFN SLSNWRKCNT LASTSRGCHQ VQVNHIVNKY QGLGVNQCDR 60
WSFLPGNFHF YSTFNNKRTG GLSSTKSKEI WRITSKCTVW NDAFSRQLLI KEVTAVPSLS 120
VLHPLSPASI RAIRNFHTSP RFQAAPVPLL LMILKPVQKL FAIIVGRGIR KWWQALPPNK 180
KEVVKENIRK NKWKLFLGLS SFGLLFVVFY FTHLEVSPIT GRSKLLLLGK EQFRLLSELE 240
YEAWMEEFKN DMLTEKDARY LAVKEVLCHL IECNKDVPGI SQINWVIHVV DSPIINAFVL 300
PNGQMFVFTG FLNSVTDIHQ LSFLLGHEIA HAVLGHAAEK AGMVHLLDFL GMIFLTMIWA 360
ICPRDSLALL CQWIQSKLQE YMFNRPYSRK LEAEADKIGL LLAAKACADI RASSVFWQQM 420
EFVDSLHGQP KMPEWLSTHP SHGNRVEYLD RLIPQALKIR EMCNCPPLSN PDPRLLFKLS 480
TKHFLEESEK EDLNITKKQK MDTLPIQKQE QIPLTYIVEK RTGS 524 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
 GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004222; F:metalloendopeptidase activity; IMP:UniProtKB.
 GO:0042407; P:cristae formation; IEA:Compara.
 GO:0002024; P:diet induced thermogenesis; IMP:UniProtKB.
 GO:0097009; P:energy homeostasis; IMP:UniProtKB.
 GO:0006006; P:glucose metabolic process; IMP:UniProtKB.
 GO:0006629; P:lipid metabolic process; IMP:UniProtKB.
 GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IMP:UniProtKB.
 GO:0034982; P:mitochondrial protein processing; IEA:Compara.
 GO:0010637; P:negative regulation of mitochondrial fusion; IMP:UniProtKB.
 GO:0006950; P:response to stress; IDA:UniProtKB. 
Interpro
 IPR001915; Peptidase_M48. 
Pfam
 PF01435; Peptidase_M48 
SMART
  
PROSITE
 PS00142; ZINC_PROTEASE 
PRINTS