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Protein

Lon protease homolog, mitochondrial

Gene

Lonp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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 annotation1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei844 – 8441UniRule annotation
Active sitei887 – 8871UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi512 – 5198ATPUniRule annotation

GO - Molecular functioni

  • ADP binding Source: MGI
  • ATPase activity Source: MGI
  • ATP binding Source: MGI
  • ATP-dependent peptidase activity Source: MGI
  • DNA polymerase binding Source: MGI
  • G-quadruplex DNA binding Source: MGI
  • mitochondrial light strand promoter anti-sense binding Source: MGI
  • sequence-specific DNA binding Source: MGI
  • serine-type endopeptidase activity Source: UniProtKB-HAMAP
  • single-stranded DNA binding Source: MGI
  • single-stranded RNA binding Source: MGI

GO - Biological processi

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:Prss15
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1921392. Lonp1.

Subcellular locationi

  • Mitochondrion matrix UniRule annotation1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3259486.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6565MitochondrionUniRule annotationAdd
BLAST
Chaini66 – 949884Lon protease homolog, mitochondrialPRO_0000254961Add
BLAST

Proteomic databases

EPDiQ8CGK3.
MaxQBiQ8CGK3.
PaxDbiQ8CGK3.
PeptideAtlasiQ8CGK3.
PRIDEiQ8CGK3.

2D gel databases

REPRODUCTION-2DPAGEQ8CGK3.
Q9DBP9.

PTM databases

iPTMnetiQ8CGK3.
SwissPalmiQ8CGK3.

Expressioni

Tissue specificityi

Detected in liver > heart > kidney > testis.1 Publication

Gene expression databases

BgeeiQ8CGK3.
CleanExiMM_LONP1.
GenevisibleiQ8CGK3. MM.

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi216521. 1 interaction.
IntActiQ8CGK3. 3 interactions.
MINTiMINT-1540850.
STRINGi10090.ENSMUSP00000041814.

Structurei

3D structure databases

ProteinModelPortaliQ8CGK3.
SMRiQ8CGK3. Positions 277-397, 408-940.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini112 – 357246Lon N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini748 – 938191Lon 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.
HOGENOMiHOG000261409.
HOVERGENiHBG000798.
InParanoidiQ8CGK3.
KOiK08675.
OMAiNCLILPV.
OrthoDBiEOG7HQN7C.
PhylomeDBiQ8CGK3.
TreeFamiTF105001.

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.

Q8CGK3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASTGYVRL WAAARCWVLR RPLLAVTGGR VPSASGSWLR RGCRACDMSA
60 70 80 90 100
PWGGRVLPGG VQWRGLWDSG NRGGSDETSE GGAEDGATAS TGEGPVVTAL
110 120 130 140 150
APMTVPDVFP HLPLIAITRN PVFPRFIKIV EVKNKKLVEL LRRKVRLAQP
160 170 180 190 200
YVGVFLKRDD NNESDVVESL DEIYHTGTFA QIHEMQDLGD KLRMIVTGHR
210 220 230 240 250
RIHISRQLEV EPEGLEPEAE KQKSRRKLKR GKKEVEDELG PKPQLEMVTE
260 270 280 290 300
AATDTSKEVL MVEVENVAHE DFQVTEEVKA LTAEIVKTIR DIIALNPLYR
310 320 330 340 350
ESVLQMMQAG QRVVDNPIYL SDMGAALTGA ESHELQDVLE ETNILKRLYK
360 370 380 390 400
ALSLLKKEFE LSKLQQRLGR EVEEKIKQTH RKYLLQEQLK IIKKELGLEK
410 420 430 440 450
DDKDAIEEKF RERLRELVVP KHVMDVVDEE LSKLALLDNH SSEFNVTRNY
460 470 480 490 500
LDWLTSIPWG RQSDENLDLA RAQAVLEEDH YGMEDVKKRV LEFIAVSQLR
510 520 530 540 550
GSTQGKILCF HGPPGVGKTS IARSIARALG REYFRFSVGG MTDVAEIKGH
560 570 580 590 600
RRTYVGAMPG KIIQCLKKTK TENPLVLIDE VDKIGRGYQG DPSSALLELL
610 620 630 640 650
DPEQNANFLD HYLDVPVDLS KVLFICTANV IDTIPEPLRD RMEMINVSGY
660 670 680 690 700
VAQEKLAIAE RYLVPQARTL CGLDESKAQL SAAVLTLLIK QYCRESGVRN
710 720 730 740 750
LQKQVEKVLR KAAYKIVSGE AQTVQVTPEN LQDFVGKPVF TVERMYEVTP
760 770 780 790 800
PGVVMGLAWT AMGGSTLFVE TSLRRPQPSG SKEDKDGSLE VTGQLGDVMK
810 820 830 840 850
ESARIAYTYA RAFLMEQDPE NDFLVTSHIH LHVPEGATPK DGPSAGCTIV
860 870 880 890 900
TALLSLALGQ PVLQNLAMTG EVSLTGKVLP VGGIKEKTIA AKRAGVTCII
910 920 930 940
LPAENRKDYS DLAPFITEGL EVHFVEHYRD IFPIAFPRRE HREALAVER
Length:949
Mass (Da):105,843
Last modified:October 31, 2006 - v2
Checksum:i4622E900C8D90369
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901S → G in BAB23591 (PubMed:16141072).Curated
Sequence conflicti99 – 991A → T in BAE34094 (PubMed:16141072).Curated
Sequence conflicti202 – 2021I → T in BAB23591 (PubMed:16141072).Curated
Sequence conflicti214 – 2141G → R in AAN85210 (PubMed:12657466).Curated
Sequence conflicti240 – 2401G → S in BAE34094 (PubMed:16141072).Curated
Sequence conflicti248 – 2481V → L in BAE34094 (PubMed:16141072).Curated
Sequence conflicti271 – 2711D → Y in BAB23591 (PubMed:16141072).Curated
Sequence conflicti368 – 3681L → P in BAB23591 (PubMed:16141072).Curated
Sequence conflicti424 – 4241M → I in BAE36666 (PubMed:16141072).Curated
Sequence conflicti449 – 4491N → K in BAE34972 (PubMed:16141072).Curated
Sequence conflicti636 – 6361E → K in BAE34094 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY190302 mRNA. Translation: AAN85210.1.
AK004820 mRNA. Translation: BAB23591.1.
AK157474 mRNA. Translation: BAE34094.1.
AK159302 mRNA. Translation: BAE34972.1.
AK160071 mRNA. Translation: BAE35606.1.
AK161983 mRNA. Translation: BAE36666.1.
CCDSiCCDS28910.1.
RefSeqiNP_083058.2. NM_028782.2.
UniGeneiMm.329136.

Genome annotation databases

EnsembliENSMUST00000047226; ENSMUSP00000041814; ENSMUSG00000041168.
GeneIDi74142.
KEGGimmu:74142.
UCSCiuc008dcp.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY190302 mRNA. Translation: AAN85210.1.
AK004820 mRNA. Translation: BAB23591.1.
AK157474 mRNA. Translation: BAE34094.1.
AK159302 mRNA. Translation: BAE34972.1.
AK160071 mRNA. Translation: BAE35606.1.
AK161983 mRNA. Translation: BAE36666.1.
CCDSiCCDS28910.1.
RefSeqiNP_083058.2. NM_028782.2.
UniGeneiMm.329136.

3D structure databases

ProteinModelPortaliQ8CGK3.
SMRiQ8CGK3. Positions 277-397, 408-940.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi216521. 1 interaction.
IntActiQ8CGK3. 3 interactions.
MINTiMINT-1540850.
STRINGi10090.ENSMUSP00000041814.

Chemistry

ChEMBLiCHEMBL3259486.

Protein family/group databases

MEROPSiS16.002.

PTM databases

iPTMnetiQ8CGK3.
SwissPalmiQ8CGK3.

2D gel databases

REPRODUCTION-2DPAGEQ8CGK3.
Q9DBP9.

Proteomic databases

EPDiQ8CGK3.
MaxQBiQ8CGK3.
PaxDbiQ8CGK3.
PeptideAtlasiQ8CGK3.
PRIDEiQ8CGK3.

Protocols and materials databases

DNASUi74142.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000047226; ENSMUSP00000041814; ENSMUSG00000041168.
GeneIDi74142.
KEGGimmu:74142.
UCSCiuc008dcp.2. mouse.

Organism-specific databases

CTDi9361.
MGIiMGI:1921392. Lonp1.

Phylogenomic databases

eggNOGiKOG2004. Eukaryota.
COG0466. LUCA.
GeneTreeiENSGT00530000063553.
HOGENOMiHOG000261409.
HOVERGENiHBG000798.
InParanoidiQ8CGK3.
KOiK08675.
OMAiNCLILPV.
OrthoDBiEOG7HQN7C.
PhylomeDBiQ8CGK3.
TreeFamiTF105001.

Miscellaneous databases

ChiTaRSiLonp1. mouse.
PROiQ8CGK3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CGK3.
CleanExiMM_LONP1.
GenevisibleiQ8CGK3. MM.

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

« Hide 'large scale' publications
  1. "The ATP-dependent Lon protease of Mus musculus is a DNA-binding protein that is functionally conserved between yeast and mammals."
    Lu B., Liu T., Crosby J.A., Thomas-Wohlever J., Lee I., Suzuki C.K.
    Gene 306:45-55(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: BALB/cJ.
    Tissue: Kidney.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Lung, Ovary and Spleen.
  3. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 434-448; 490-500 AND 930-938, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiLONM_MOUSE
AccessioniPrimary (citable) accession number: Q8CGK3
Secondary accession number(s): Q3TSK9
, Q3TVL2, Q3TXE4, Q3TZW3, Q9DBP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: July 6, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.