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Q3MIB4 (LONP2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 2, peroxisomal

EC=3.4.21.-
Alternative name(s):
Lon protease-like protein 2
Short name=Lon protease 2
Peroxisomal Lon protease
Gene names
Name:Lonp2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length852 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the peroxisomal matrix. Necessary for type 2 peroxisome targeting signal (PTS2)-containing protein processing and facilitates peroxisome matrix protein import. May indirectly regulate peroxisomal fatty acid beta-oxidation through degradation of the self-processed forms of TYSND1 By similarity. HAMAP-Rule MF_03121

Subunit structure

Interacts with PEX5 By similarity. Interacts with TYSND1 By similarity. HAMAP-Rule MF_03121

Subcellular location

Peroxisome matrix Ref.3.

Sequence similarities

Belongs to the peptidase S16 family.

Contains 1 Lon domain.

Ontologies

Keywords
   Cellular componentPeroxisome
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
Protease
Serine protease
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from Biological aspect of Ancestor. Source: GOC

misfolded or incompletely synthesized protein catabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein import into peroxisome matrix

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protein processing

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of fatty acid beta-oxidation

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from expression pattern PubMed 17929048. Source: RGD

signal peptide processing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentnucleoid

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleus

Inferred from electronic annotation. Source: Ensembl

peroxisomal matrix

Inferred from direct assay Ref.3. Source: RGD

peroxisome

Inferred from direct assay Ref.3. Source: RGD

   Molecular_functionATP binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

ATP-dependent peptidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

sequence-specific DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

serine-type endopeptidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 852851Lon protease homolog 2, peroxisomal HAMAP-Rule MF_03121
PRO_0000287642

Regions

Domain13 – 219207Lon
Nucleotide binding375 – 3828ATP Potential
Motif850 – 8523Microbody targeting signal Potential

Sites

Active site7431 By similarity
Active site7861 By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3MIB4 [UniParc].

Last modified May 15, 2007. Version 2.
Checksum: CB9D9D05F8D5E040

FASTA85294,393
        10         20         30         40         50         60 
MSSVNPIQIP SRLPLLLTHE SVLLPGSTMR TSVDTARNLQ LVRSRLLKGT SLQSTILGVI 

        70         80         90        100        110        120 
PNTPDPASDS QDLPPLHRIG TAALAVQVVG SNWPKPHYTL LITGLCRFQI VQVLKEKPYP 

       130        140        150        160        170        180 
VAEVEQLDRL EEFPNTCKTR EELGELSEQF YRYSVQLVEM LDMSVPAVAK LRRLLDSLPR 

       190        200        210        220        230        240 
EALPDILTSI IRTSNKEKLQ ILDAVSLEDR FKMTIPLLVR QIEGLKLLQK TRKPKQDDDK 

       250        260        270        280        290        300 
RVIAIRPIRR ITHIPGALED EEEEEDNDDI VMLEKKIRTS SMPEQAHKVC VKEIKRLKKM 

       310        320        330        340        350        360 
PQSMPEYALT RNYLELMVEL PWNKSTTDRL DIRAARILLD NDHYAMEKLK RRVLEYLAVR 

       370        380        390        400        410        420 
QLKNNLKGPI LCFVGPPGVG KTSVGRSVAK TLGREFHRIA LGGVCDQSDI RGHRRTYVGS 

       430        440        450        460        470        480 
MPGRIINGLK TVGVNNPVFL LDEVDKLGKS LQGDPAAALL EVLDPEQNHN FTDHYLNVAF 

       490        500        510        520        530        540 
DLSQVLFIAT ANTTATIPPA LLDRMEIIQV PGYTQEEKIE IAHRHLIPKQ LEQHGLTPQQ 

       550        560        570        580        590        600 
IQIPQLTTLA IITRYTREAG VRSLDRKFGA ICRAVAVKVA EGQHKEAKLD RSDVADGEGC 

       610        620        630        640        650        660 
KEHVLEDAKP ESIGDAADLA LPPEMPILID SHALKDILGP PLYELEVSER LSQPGVAIGL 

       670        680        690        700        710        720 
AWTPLGGKIM FVEASRMDGE GQLTLTGQLG DVMKESAHLA ISWLRSNAKK YHLTNAFGSF 

       730        740        750        760        770        780 
DLLDNTDIHL HFPAGAVTKD GPSAGVTIVT CLASLFSGRL VRSDVAMTGE ITLRGLVLPV 

       790        800        810        820        830        840 
GGIKDKVLAA HRAGLKHIII PQRNEKDLEE IPSNVKQDLS FVTASCLDEV LNAAFDGGFT 

       850 
VKTRPGLTDS KL 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 297-852.
Tissue: Ovary.
[3]"Proteomic analysis of rat liver peroxisome: presence of peroxisome-specific isozyme of Lon protease."
Kikuchi M., Hatano N., Yokota S., Shimozawa N., Imanaka T., Taniguchi H.
J. Biol. Chem. 279:421-428(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03113833 Genomic DNA. No translation available.
AABR03113838 Genomic DNA. No translation available.
AABR03114515 Genomic DNA. No translation available.
AABR03113506 Genomic DNA. No translation available.
BC103718 mRNA. Translation: AAI03719.1.
RefSeqXP_006255300.1. XM_006255238.1.
UniGeneRn.228635.

3D structure databases

ProteinModelPortalQ3MIB4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000020770.

Protein family/group databases

MEROPSS16.006.

Proteomic databases

PaxDbQ3MIB4.
PRIDEQ3MIB4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000020770; ENSRNOP00000020770; ENSRNOG00000015162.
GeneID291922.

Organism-specific databases

RGD1305466. Lonp2.

Phylogenomic databases

eggNOGCOG0466.
GeneTreeENSGT00530000063553.
HOGENOMHOG000261408.
HOVERGENHBG000798.
InParanoidQ3MIB4.
OMADQREYFL.
OrthoDBEOG77T13V.
PhylomeDBQ3MIB4.
TreeFamTF317215.

Gene expression databases

GenevestigatorQ3MIB4.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPMF_03121. lonp2_euk.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR004815. Lon_bac/euk-typ.
IPR027065. Lon_Prtase.
IPR027501. Lonp2_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.
[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...

Other

PROQ3MIB4.

Entry information

Entry nameLONP2_RAT
AccessionPrimary (citable) accession number: Q3MIB4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: April 16, 2014
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries