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Protein

Lon protease homolog, mitochondrial

Gene

Lonp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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 promoters and RNA in a single-stranded, site-specific, and strand-specific manner. May regulate mitochondrial DNA replication and/or gene expression using site-specific, single-stranded DNA binding to target the degradation of regulatory proteins binding to adjacent sites in mitochondrial promoters.UniRule annotation2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei845 – 8451UniRule annotation
Active sitei888 – 8881UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi513 – 5208ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

  • aging Source: RGD
  • cellular protein complex assembly Source: RGD
  • cellular response to oxidative stress Source: Ensembl
  • misfolded or incompletely synthesized protein catabolic process Source: InterPro
  • mitochondrion organization Source: RGD
  • oxidation-dependent protein catabolic process Source: Ensembl
  • protein homooligomerization Source: Ensembl
  • proteolysis Source: RGD
  • response to aluminum ion Source: RGD
  • response to hormone Source: RGD
  • response to hypoxia Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Protein family/group databases

MEROPSiS16.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Lon protease homolog, mitochondrialUniRule annotation (EC:3.4.21.-UniRule annotation)
Alternative name(s):
Lon protease-like proteinUniRule annotation
Short name:
LONPUniRule annotation
Mitochondrial ATP-dependent protease LonUniRule annotation
Serine protease 15UniRule annotation
Gene namesi
Name:Lonp1
Synonyms:Lon, Prss15
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi621598. Lonp1.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: Ensembl
  • mitochondrial matrix Source: RGD
  • mitochondrial nucleoid Source: Ensembl
  • mitochondrion Source: RGD
  • nucleoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6565MitochondrionUniRule annotationAdd
BLAST
Chaini66 – 950885Lon protease homolog, mitochondrialPRO_0000254962Add
BLAST

Proteomic databases

PaxDbiQ924S5.
PRIDEiQ924S5.

PTM databases

iPTMnetiQ924S5.
PhosphoSiteiQ924S5.

Expressioni

Inductioni

By hypoxia or ER stress.1 Publication

Gene expression databases

GenevisibleiQ924S5. RN.

Interactioni

Subunit structurei

Homohexamer or homoheptamer. Organized in a ring with a central cavity. DNA and RNA binding is stimulated by substrate and inhibited by ATP binding. Interacts with PEO1 and mitochondrial DNA polymerase subunit POLG.UniRule annotation

Protein-protein interaction databases

IntActiQ924S5. 1 interaction.
STRINGi10116.ENSRNOP00000066618.

Structurei

3D structure databases

ProteinModelPortaliQ924S5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini112 – 358247Lon N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini749 – 939191Lon proteolyticPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S16 family.UniRule annotation
Contains 1 Lon N-terminal domain.PROSITE-ProRule annotation
Contains 1 Lon proteolytic domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2004. Eukaryota.
COG0466. LUCA.
GeneTreeiENSGT00530000063553.
HOVERGENiHBG000798.
InParanoidiQ924S5.
KOiK08675.
OMAiNCLILPV.
OrthoDBiEOG7HQN7C.
PhylomeDBiQ924S5.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_03120. lonm_euk.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR004815. Lon_bac/euk-typ.
IPR027065. Lon_Prtase.
IPR003111. LON_substr-bd_dom.
IPR027503. Lonm_euk.
IPR027417. P-loop_NTPase.
IPR008269. Pept_S16_C.
IPR008268. Peptidase_S16_AS.
IPR015947. PUA-like_domain.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERiPTHR10046. PTHR10046. 2 hits.
PfamiPF00004. AAA. 1 hit.
PF05362. Lon_C. 1 hit.
PF02190. LON_substr_bdg. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM00464. LON. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR00763. lon. 1 hit.
PROSITEiPS51787. LON_N. 1 hit.
PS51786. LON_PROTEOLYTIC. 1 hit.
PS01046. LON_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q924S5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASTGYVRL WAAARCWVLR RPLLAVTGGR VPSASGSWLR RGCRVCDTST
60 70 80 90 100
PWGGRVPMGG GQWRGLWDAG SRGGSDETSE GGVEDGATAS SGEGPVVTAL
110 120 130 140 150
APMTVPDVFP HLPLIAISRN PVFPRFIKIV EVKNKKLVEL LRRKVRLAQP
160 170 180 190 200
YVGVFLKRDD NNESDVVESL DEIYHTGTFA QIHEMQDLGD KLRMIVTGHR
210 220 230 240 250
RIHISRQLEV EPEGLEPEAE NKQKSRRKLK RGKKEVGDEL GAKPQLEMVT
260 270 280 290 300
EATSDTSKEV LMVEVENVAH EDFQVTEEVK ALTAEIVKTI RDIIALNPLY
310 320 330 340 350
RESVLQMMQA GQRVVDNPIY LSDMGAALTG AESHELQDVL EETNILKRLY
360 370 380 390 400
KALSLLKKEF ELSKLQQRLG REVEEKIKQT HRKYLLQEQL KIIKKELGLE
410 420 430 440 450
KDDKDAIEEK FRERLKELVV PKHVMDVVDE ELSKLALLDN HSSEFNVTRN
460 470 480 490 500
YLDWLTSIPW GRQSDENLDL ARAQSVLEED HYGMEDVKKR VLEFIAVSQL
510 520 530 540 550
RGSTQGKILC FHGPPGVGKT SIARSIARAL GREYFRFSVG GMTDVAEIKG
560 570 580 590 600
HRRTYVGAMP GKIIQCLKKT KTENPLVLID EVDKIGRGYQ GDPSSALLEL
610 620 630 640 650
LDPEQNANFL DHYLDVPVDL SKVLFICTAN VTDTIPEPLR DRMEMINVSG
660 670 680 690 700
YVAQEKLAIA ERYLVPQART LCGLDESKAQ LSATVLTLLI KQYCRESGVR
710 720 730 740 750
NLQKQVEKVL RKAAYKIVSG EAQTVHVTPE NLQDFVGKPV FTVERMYDVT
760 770 780 790 800
PPGVVMGLAW TAMGGSTLFV ETSLRRPQPS GSKEDKDGSL EVTGQLGDVM
810 820 830 840 850
KESARIAYTF ARAFLMEQDP ENDFLVTSHI HLHVPEGATP KDGPSAGCTI
860 870 880 890 900
VTALLSLALG QPVLQNLAMT GEVSLTGKVL PVGGIKEKTI AAKRAGVTCI
910 920 930 940 950
ILPAENRKDF SDLAPFITEG LEVHFVEHYR DIFRIAFPLR EHQEALAVER
Length:950
Mass (Da):105,793
Last modified:December 1, 2001 - v1
Checksum:iD505C3D851B6F0E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB064323 mRNA. Translation: BAB62423.1.
RefSeqiNP_596895.1. NM_133404.1.
UniGeneiRn.146805.

Genome annotation databases

EnsembliENSRNOT00000074253; ENSRNOP00000066618; ENSRNOG00000046502.
GeneIDi170916.
KEGGirno:170916.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB064323 mRNA. Translation: BAB62423.1.
RefSeqiNP_596895.1. NM_133404.1.
UniGeneiRn.146805.

3D structure databases

ProteinModelPortaliQ924S5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ924S5. 1 interaction.
STRINGi10116.ENSRNOP00000066618.

Protein family/group databases

MEROPSiS16.002.

PTM databases

iPTMnetiQ924S5.
PhosphoSiteiQ924S5.

Proteomic databases

PaxDbiQ924S5.
PRIDEiQ924S5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000074253; ENSRNOP00000066618; ENSRNOG00000046502.
GeneIDi170916.
KEGGirno:170916.

Organism-specific databases

CTDi9361.
RGDi621598. Lonp1.

Phylogenomic databases

eggNOGiKOG2004. Eukaryota.
COG0466. LUCA.
GeneTreeiENSGT00530000063553.
HOVERGENiHBG000798.
InParanoidiQ924S5.
KOiK08675.
OMAiNCLILPV.
OrthoDBiEOG7HQN7C.
PhylomeDBiQ924S5.

Miscellaneous databases

NextBioi621395.
PROiQ924S5.

Gene expression databases

GenevisibleiQ924S5. RN.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_03120. lonm_euk.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR004815. Lon_bac/euk-typ.
IPR027065. Lon_Prtase.
IPR003111. LON_substr-bd_dom.
IPR027503. Lonm_euk.
IPR027417. P-loop_NTPase.
IPR008269. Pept_S16_C.
IPR008268. Peptidase_S16_AS.
IPR015947. PUA-like_domain.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERiPTHR10046. PTHR10046. 2 hits.
PfamiPF00004. AAA. 1 hit.
PF05362. Lon_C. 1 hit.
PF02190. LON_substr_bdg. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM00464. LON. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR00763. lon. 1 hit.
PROSITEiPS51787. LON_N. 1 hit.
PS51786. LON_PROTEOLYTIC. 1 hit.
PS01046. LON_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Transmission of cell stress from endoplasmic reticulum to mitochondria: enhanced expression of Lon protease."
    Hori O., Ichinoda F., Tamatani T., Yamaguchi A., Sato N., Ozawa K., Kitao Y., Miyazaki M., Harding H.P., Ron D., Tohyama M., Stern D.M., Ogawa S.
    J. Cell Biol. 157:1151-1160(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
  2. "Synthesis, processing, and localization of human Lon protease."
    Wang N., Maurizi M.R., Emmert-Buck L., Gottesman M.M.
    J. Biol. Chem. 269:29308-29313(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  3. "Changes in rat liver mitochondria with aging. Lon protease-like reactivity and N(epsilon)-carboxymethyllysine accumulation in the matrix."
    Bakala H., Delaval E., Hamelin M., Bismuth J., Borot-Laloi C., Corman B., Friguet B.
    Eur. J. Biochem. 270:2295-2302(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  4. "Age-related impairment of mitochondrial matrix aconitase and ATP-stimulated protease in rat liver and heart."
    Delaval E., Perichon M., Friguet B.
    Eur. J. Biochem. 271:4559-4564(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiLONM_RAT
AccessioniPrimary (citable) accession number: Q924S5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.