F8PXN2 · F8PXN2_SERL3

Function

function

ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.

Catalytic activity

  • Hydrolysis of proteins in presence of ATP.
    EC:3.4.21.53 (UniProtKB | ENZYME | Rhea)

Features

Showing features for binding site, active site.

110841002003004005006007008009001,000
Type
IDPosition(s)Description
Binding site577-584ATP (UniProtKB | ChEBI)
Active site976
Active site1019

GO annotations

AspectTerm
Cellular Componentmitochondrial matrix
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent peptidase activity
Molecular Functionsequence-specific DNA binding
Molecular Functionserine-type endopeptidase activity
Molecular Functionsingle-stranded DNA binding
Biological Processcellular response to oxidative stress
Biological Processchaperone-mediated protein complex assembly
Biological Processmitochondrion organization
Biological Processoxidation-dependent protein catabolic process
Biological Processprotein quality control for misfolded or incompletely synthesized proteins

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lon protease homolog, mitochondrial
  • EC number

Gene names

    • Name
      PIM1
    • ORF names
      SERLA73DRAFT_160369

Organism names

Accessions

  • Primary accession
    F8PXN2

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homohexamer or homoheptamer. Organized in a ring with a central cavity.

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias56-82Polar residues
Region56-155Disordered
Compositional bias83-109Basic and acidic residues
Compositional bias114-135Polar residues
Compositional bias136-150Pro residues
Domain165-424Lon N-terminal
Region276-304Disordered
Region792-851Disordered
Compositional bias799-840Polar residues
Domain884-1071Lon proteolytic

Sequence similarities

Belongs to the peptidase S16 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,084
  • Mass (Da)
    118,003
  • Last updated
    2011-09-21 v1
  • Checksum
    0400FA49ABAD73E6
MAFAGSFRATTASCSKQICARQARVPRTSSSWIPQSSVPLGSQLVSRIIDRRSFSSSISNPARPSQSLFYSPRWSNNKNPEADTSENDPKAQEDGDVEKKNDTVRLDGPEDENAPGASSNSTPPSSSSSGDNNDSADPPPAPPPTTPPSPSSIAKQSVPEIYPQVLALPIARRPLFPGFYKAVVVRNPAVVAAIKEMMKRGQPYLGAFLLKDENTDSDIITDINSVHPVGVFAQITSVFAANSGSGDDKEEGLTAVLYPHRRIKVTELIKAGESPSVAKVTDEDEAAKAQTVAPPTPPPEPEATRIQAGPLQTSFLHKHAISIVQVDNLITQPYNKDDQYIRAFMSEIVSVFKDIAQLNPLFRDQITNFSINQVASNVFDEPDKLADFAAAVSTGEVGELQDVLESLVVDDRLRKALLVLKKELINAQLQSKLSRDVDTKIAKRQREYYLMEQLKGIKKELGMESDGKDKLIEKFKERAATLKMPESVRKVFDEELNKLMGLEPAASEANVTRNYLEWLTQIPWGQHSPENYSIGHAQTVLDEDHYGLKDVKDRILEFLAVGKLRGTVEGKIICLVGPPGVGKTSIGKSIARALNRQFFRFSVGGLTDVAEIKGHRRTYVGALPGKIIQALKRVGTENPLVLIDEVDKIGRGINGDPASALLEMLDPEQNNGFLDHYMDVPVDLSRVLFVCTANNLDTIPAPLLDRMEVLEVSGYVSEEKSVIADKYLGPQAKESSGLKEADVLLDPTAVDVLIKYYCRESGVRNLKKHIDKIYRKAALKLILDLGEDVFPEPSSPAPTSVPAESSTVGPQPKTVESQEPLPNEPDTTATPEATSDNEAEKVVTTQERKPLKIPDSVHVRITPENLKDYVGPPVYHKDRMYTTPPPPGVSSGLGYLGNGSGAVMPVEATAMPGKGGLQLTGKLGEVIRESAQIGLSWVKAHAYELGITQSPDEQFLTDRDIHVHMPEGSIGKEGPSAGTAILSAFVSLFTKTKINPDIAMTGEISLVGQVLPVGGLKEKILAAHRAGIKTILAPAANRADIEENVPESVKDGIRFVYVEDVKEVLHEVFKGEPITERWKDTLSI

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias56-82Polar residues
Compositional bias83-109Basic and acidic residues
Compositional bias114-135Polar residues
Compositional bias136-150Pro residues
Compositional bias799-840Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GL945480
EMBL· GenBank· DDBJ
EGN98645.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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