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Q9M9L7 (LONM4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lon protease homolog 4, chloroplastic/mitochondrial

Short name=AtLon4
EC=3.4.21.-
Gene names
Name:LON4
Ordered Locus Names:At3g05790
ORF Names:F10A16.8
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length942 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

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 By similarity. HAMAP-Rule MF_03120

Subunit structure

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

Subcellular location

Mitochondrion matrix. Plastidchloroplast thylakoid membrane; Peripheral membrane protein; Stromal side Ref.3.

Sequence similarities

Belongs to the peptidase S16 family.

Contains 1 Lon domain.

Ontologies

Keywords
   Cellular componentChloroplast
Membrane
Mitochondrion
Plastid
Thylakoid
   DomainTransit peptide
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionHydrolase
Protease
Serine protease
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

cellular response to oxidative stress

Inferred from Biological aspect of Ancestor. Source: RefGenome

chaperone-mediated protein complex assembly

Inferred from Biological aspect of Ancestor. Source: RefGenome

misfolded or incompletely synthesized protein catabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

mitochondrion organization

Inferred from Biological aspect of Ancestor. Source: RefGenome

oxidation-dependent protein catabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein homooligomerization

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of mitochondrial DNA replication

Inferred from electronic annotation. Source: UniProtKB-HAMAP

response to hypoxia

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentchloroplast

Inferred from direct assay Ref.3. Source: TAIR

chloroplast thylakoid membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial nucleoid

Inferred from Biological aspect of Ancestor. Source: RefGenome

mitochondrion

Inferred from direct assay Ref.3. Source: TAIR

   Molecular_functionATP binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

ATP-dependent peptidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

mitochondrial light strand promoter anti-sense binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

sequence-specific DNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

serine-type endopeptidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

single-stranded DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

single-stranded RNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Chloroplast and mitochondrion Potential
Chain? – 942Lon protease homolog 4, chloroplastic/mitochondrial HAMAP-Rule MF_03120PRO_0000045425

Regions

Domain79 – 299221Lon
Nucleotide binding456 – 4638ATP By similarity

Sites

Active site8461 By similarity
Active site8891 By similarity

Amino acid modifications

Modified residue541Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9M9L7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 90F3238714F4C52E

FASTA942104,925
        10         20         30         40         50         60 
MLKFLTPTAY ASHHVTPATR FRSTPVKNLL FKQLTLLTGW NRSSYELGRR SFSSDLDSDT 

        70         80         90        100        110        120 
KSSTTTVSAK PHLDDCLTVI ALPLPHKPLI PGFYMPIYVK DPKVLAALQE SRRQQAPYAG 

       130        140        150        160        170        180 
AFLLKDDASS DSSSSSETEN ILEKLKGKEL INRIHEVGTL AQISSIQGEQ VILIGHRQLR 

       190        200        210        220        230        240 
ITEMVSESED PLTVKVDHLK DKPYDKDDDV IKATYFQVMS TLRDVLKTTS LWRDHVRTYT 

       250        260        270        280        290        300 
QACSLHIWHC LRHIGEFNYP KLADFGAGIS GANKHQNQGV LEELDVHKRL ELTLELVKKE 

       310        320        330        340        350        360 
VEINKIQESI AKAVEEKFSG DRRRIILKEQ INAIKKELGG ETDSKSALSE KFRGRIDPIK 

       370        380        390        400        410        420 
DKIPGHVLKV IEEELKKLQL LETSSSEFDV TCNYLDWLTV LPWGNFSDEN FNVLRAEKIL 

       430        440        450        460        470        480 
DEDHYGLSDV KERILEFIAV GGLRGTSQGK IICLSGPTGV GKTSIGRSIA RALDRKFFRF 

       490        500        510        520        530        540 
SVGGLSDVAE IKGHRRTYIG AMPGKMVQCL KNVGTENPLV LIDEIDKLGV RGHHGDPASA 

       550        560        570        580        590        600 
MLELLDPEQN ANFLDHYLDV PIDLSKVLFV CTANVTDTIP GPLLDRMEVI TLSGYITDEK 

       610        620        630        640        650        660 
MHIARDYLEK TARRDCGIKP EQVDVSDAAF LSLIEHYCRE AGVRNLQKQI EKIFRKIALK 

       670        680        690        700        710        720 
LVRKAASTEV PRISDDVTTD TEETKSLAKT DLESPETSAE GSTVLTDELA TGDPTESTTE 

       730        740        750        760        770        780 
QSGEVAETVE KYMIDESNLS DYVGKPVFQE EKIYEQTPVG VVMGLAWTSM GGSTLYIETT 

       790        800        810        820        830        840 
FVEEGEGKGG LHITGRLGDV MKESAEIAHT VARRIMLEKE PENKLFANSK LHLHVPAGAT 

       850        860        870        880        890        900 
PKDGPSAGCT MITSLLSLAL KKPVRKDLAM TGEVTLTGRI LAIGGVKEKT IAARRSQVKV 

       910        920        930        940 
IIFPEANRRD FDELARNVKE GLEVHFVDEY EQIFELAFGY DH 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Multiple intracellular locations of Lon protease in Arabidopsis: evidence for the localization of AtLon4 to chloroplasts."
Ostersetzer O., Kato Y., Adam Z., Sakamoto W.
Plant Cell Physiol. 48:881-885(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC012393 Genomic DNA. Translation: AAF26081.1.
CP002686 Genomic DNA. Translation: AEE74297.1.
RefSeqNP_566259.1. NM_111453.1.
UniGeneAt.53196.

3D structure databases

ProteinModelPortalQ9M9L7.
SMRQ9M9L7. Positions 347-938.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT3G05790.1-P.

Protein family/group databases

MEROPSS16.A02.

Proteomic databases

PaxDbQ9M9L7.
PRIDEQ9M9L7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G05790.1; AT3G05790.1; AT3G05790.
GeneID819748.
KEGGath:AT3G05790.

Organism-specific databases

GeneFarm1770. 137.
TAIRAT3G05790.

Phylogenomic databases

eggNOGCOG0466.
HOGENOMHOG000261409.
InParanoidQ9M9L7.
KOK08675.
OMAMKESVGA.
PhylomeDBQ9M9L7.
ProtClustDBCLSN2917104.

Enzyme and pathway databases

BioCycARA:AT3G05790-MONOMER.

Gene expression databases

GenevestigatorQ9M9L7.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPMF_03120. lonm_euk.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR004815. Lon_bac/euk-typ.
IPR027065. Lon_Prtase.
IPR027503. Lonm_euk.
IPR027417. P-loop_NTPase.
IPR008269. Pept_S16_C.
IPR003111. Pept_S16_N.
IPR008268. Peptidase_S16_AS.
IPR015947. PUA-like_domain.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERPTHR10046. PTHR10046. 1 hit.
PfamPF00004. AAA. 1 hit.
PF02190. LON. 1 hit.
PF05362. Lon_C. 1 hit.
[Graphical view]
PIRSFPIRSF001174. Lon_proteas. 1 hit.
SMARTSM00382. AAA. 1 hit.
SM00464. LON. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsTIGR00763. lon. 1 hit.
PROSITEPS01046. LON_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLONM4_ARATH
AccessionPrimary (citable) accession number: Q9M9L7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names