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Q86WA8 (LONP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. 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 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
Synonyms:LONP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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 By similarity. May indirectly regulate peroxisomal fatty acid beta-oxidation through degradation of the self-processed forms of TYSND1. Ref.8

Subunit structure

Interacts with PEX5. Interacts with TYSND1. Ref.8

Subcellular location

Peroxisome matrix Ref.6 Ref.8.

Sequence similarities

Belongs to the peptidase S16 family.

Contains 1 Lon domain.

Sequence caution

The sequence BAB55278.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

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

peroxisome organization

Non-traceable author statement Ref.6. Source: UniProtKB

protein import into peroxisome matrix

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protein targeting to peroxisome

Non-traceable author statement. Source: UniProtKB

regulation of fatty acid beta-oxidation

Inferred from mutant phenotype Ref.8. Source: UniProtKB

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

signal peptide processing

Inferred from mutant phenotype. Source: UniProtKB

   Cellular_componentnucleus

Inferred from electronic annotation. Source: Ensembl

peroxisomal matrix

Inferred from Biological aspect of Ancestor. Source: RefGenome

peroxisome

Inferred from direct assay PubMed 18281296Ref.8. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

ATP-dependent peptidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

enzyme binding

Inferred from physical interaction PubMed 18281296. Source: UniProtKB

peptidase activity

Inferred from direct assay PubMed 18281296. Source: UniProtKB

protease binding

Inferred from physical interaction Ref.8. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 18281296. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 20178365. Source: UniProtKB

serine-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 852851Lon protease homolog 2, peroxisomal HAMAP-Rule MF_03121
PRO_0000287640

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 Ref.9

Experimental info

Mutagenesis7431S → A: Reduces degradation of self-processed forms of TYSND1. Ref.8
Sequence conflict2551S → A in AAI10435. Ref.4
Sequence conflict6281L → F in BAC11201. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q86WA8 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 00444E4FF47417AC

FASTA85294,617
        10         20         30         40         50         60 
MSSVSPIQIP SRLPLLLTHE GVLLPGSTMR TSVDSARNLQ LVRSRLLKGT SLQSTILGVI 

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

       130        140        150        160        170        180 
IAEVEQLDRL EEFPNTCKMR EELGELSEQF YKYAVQLVEM LDMSVPAVAK LRRLLDSLPR 

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

       250        260        270        280        290        300 
RVIAIRPIRR ITHISGTLED EDEDEDNDDI VMLEKKIRTS SMPEQAHKVC VKEIKRLKKM 

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

       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 ANTTATIPAA LLDRMEIIQV PGYTQEEKIE IAHRHLIPKQ LEQHGLTPQQ 

       550        560        570        580        590        600 
IQIPQVTTLD IITRYTREAG VRSLDRKLGA ICRAVAVKVA EGQHKEAKLD RSDVTEREGC 

       610        620        630        640        650        660 
REHILEDEKP ESISDTTDLA LPPEMPILID FHALKDILGP PMYEMEVSQR LSQPGVAIGL 

       670        680        690        700        710        720 
AWTPLGGEIM FVEASRMDGE GQLTLTGQLG DVMKESAHLA ISWLRSNAKK YQLTNAFGSF 

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

       790        800        810        820        830        840 
GGIKDKVLAA HRAGLKQVII PRRNEKDLEG IPGNVRQDLS FVTASCLDEV LNAAFDGGFT 

       850 
VKTRPGLLNS KL 

« Hide

References

« Hide 'large scale' references
[1]"A mammalian peroxisomal lon protease: cloning and characterization."
De Walque S., Van Veldhoven P.P.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Teratocarcinoma.
[3]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Tissue: Brain and Uterus.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 138-852.
Tissue: Melanoma.
[6]"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: SUBCELLULAR LOCATION.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Two proteases, trypsin domain-containing 1 (Tysnd1) and peroxisomal lon protease (PsLon), cooperatively regulate fatty acid beta-oxidation in peroxisomal matrix."
Okumoto K., Kametani Y., Fujiki Y.
J. Biol. Chem. 286:44367-44379(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PEX5 AND TYSND1, MUTAGENESIS OF SER-743.
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ548761 mRNA. Translation: CAD68987.1.
AK027666 mRNA. Translation: BAB55278.1. Different initiation.
AK074775 mRNA. Translation: BAC11201.1.
AC007600 Genomic DNA. No translation available.
AC023818 Genomic DNA. No translation available.
BC093910 mRNA. Translation: AAH93910.1.
BC093912 mRNA. Translation: AAH93912.1.
BC110434 mRNA. Translation: AAI10435.1.
AL834201 mRNA. Translation: CAD38889.1.
CCDSCCDS10734.1.
RefSeqNP_113678.2. NM_031490.2.
UniGeneHs.731827.

3D structure databases

ProteinModelPortalQ86WA8.
SMRQ86WA8. Positions 269-835.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123755. 4 interactions.
IntActQ86WA8. 5 interactions.
STRING9606.ENSP00000285737.

Protein family/group databases

MEROPSS16.006.

PTM databases

PhosphoSiteQ86WA8.

Polymorphism databases

DMDM74727668.

Proteomic databases

MaxQBQ86WA8.
PaxDbQ86WA8.
PRIDEQ86WA8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000285737; ENSP00000285737; ENSG00000102910.
GeneID83752.
KEGGhsa:83752.
UCSCuc002efi.1. human.

Organism-specific databases

CTD83752.
GeneCardsGC16P048278.
H-InvDBHIX0173249.
HGNCHGNC:20598. LONP2.
HPAHPA008862.
neXtProtNX_Q86WA8.
PharmGKBPA162394186.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0466.
HOGENOMHOG000261408.
HOVERGENHBG000798.
InParanoidQ86WA8.
KOK01338.
OMADQREYFL.
OrthoDBEOG77T13V.
PhylomeDBQ86WA8.
TreeFamTF317215.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ86WA8.
BgeeQ86WA8.
CleanExHS_LONP2.
GenevestigatorQ86WA8.

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

GenomeRNAi83752.
NextBio72777.
PROQ86WA8.

Entry information

Entry nameLONP2_HUMAN
AccessionPrimary (citable) accession number: Q86WA8
Secondary accession number(s): Q0D2H6 expand/collapse secondary AC list , Q8N3B9, Q8NCE9, Q96K43
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM