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Q86WA8

- LONP2_HUMAN

UniProt

Q86WA8 - LONP2_HUMAN

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Protein

Lon protease homolog 2, peroxisomal

Gene
LONP2, LONP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 TYSND1.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei743 – 7431 By similarity
Active sitei786 – 7861 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi375 – 3828ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. ATP-dependent peptidase activity Source: RefGenome
  3. enzyme binding Source: UniProtKB
  4. peptidase activity Source: UniProtKB
  5. protease binding Source: UniProtKB
  6. protein binding Source: UniProtKB
  7. receptor binding Source: UniProtKB
  8. serine-type endopeptidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. misfolded or incompletely synthesized protein catabolic process Source: RefGenome
  3. peroxisome organization Source: UniProtKB
  4. protein import into peroxisome matrix Source: UniProtKB-HAMAP
  5. protein processing Source: UniProtKB
  6. protein targeting to peroxisome Source: UniProtKB
  7. regulation of fatty acid beta-oxidation Source: UniProtKB
  8. response to organic cyclic compound Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_16907. Association of TriC/CCT with target proteins during biosynthesis.

Protein family/group databases

MEROPSiS16.006.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:LONP2
Synonyms:LONP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:20598. LONP2.

Subcellular locationi

Peroxisome matrix 2 Publications

GO - Cellular componenti

  1. nucleus Source: Ensembl
  2. peroxisomal matrix Source: RefGenome
  3. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi743 – 7431S → A: Reduces degradation of self-processed forms of TYSND1. 1 Publication

Organism-specific databases

PharmGKBiPA162394186.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 852851Lon protease homolog 2, peroxisomalUniRule annotationPRO_0000287640Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ86WA8.
PaxDbiQ86WA8.
PRIDEiQ86WA8.

PTM databases

PhosphoSiteiQ86WA8.

Expressioni

Gene expression databases

ArrayExpressiQ86WA8.
BgeeiQ86WA8.
CleanExiHS_LONP2.
GenevestigatoriQ86WA8.

Organism-specific databases

HPAiHPA008862.

Interactioni

Subunit structurei

Interacts with PEX5. Interacts with TYSND1.1 Publication

Protein-protein interaction databases

BioGridi123755. 4 interactions.
IntActiQ86WA8. 5 interactions.
STRINGi9606.ENSP00000285737.

Structurei

3D structure databases

ProteinModelPortaliQ86WA8.
SMRiQ86WA8. Positions 269-835.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 219207LonAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi850 – 8523Microbody targeting signal Reviewed prediction

Sequence similaritiesi

Belongs to the peptidase S16 family.
Contains 1 Lon domain.

Phylogenomic databases

eggNOGiCOG0466.
HOGENOMiHOG000261408.
HOVERGENiHBG000798.
InParanoidiQ86WA8.
KOiK01338.
OMAiDQREYFL.
OrthoDBiEOG77T13V.
PhylomeDBiQ86WA8.
TreeFamiTF317215.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_03121. lonp2_euk.
InterProiIPR003593. 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]
PANTHERiPTHR10046. PTHR10046. 1 hit.
PfamiPF00004. AAA. 1 hit.
PF02190. LON. 1 hit.
PF05362. Lon_C. 1 hit.
[Graphical view]
PIRSFiPIRSF001174. Lon_proteas. 1 hit.
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR00763. lon. 1 hit.
PROSITEiPS01046. LON_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q86WA8-1 [UniParc]FASTAAdd to Basket

« Hide

MSSVSPIQIP SRLPLLLTHE GVLLPGSTMR TSVDSARNLQ LVRSRLLKGT    50
SLQSTILGVI PNTPDPASDA QDLPPLHRIG TAALAVQVVG SNWPKPHYTL 100
LITGLCRFQI VQVLKEKPYP IAEVEQLDRL EEFPNTCKMR EELGELSEQF 150
YKYAVQLVEM LDMSVPAVAK LRRLLDSLPR EALPDILTSI IRTSNKEKLQ 200
ILDAVSLEER FKMTIPLLVR QIEGLKLLQK TRKPKQDDDK RVIAIRPIRR 250
ITHISGTLED EDEDEDNDDI VMLEKKIRTS SMPEQAHKVC VKEIKRLKKM 300
PQSMPEYALT RNYLELMVEL PWNKSTTDRL DIRAARILLD NDHYAMEKLK 350
KRVLEYLAVR QLKNNLKGPI LCFVGPPGVG KTSVGRSVAK TLGREFHRIA 400
LGGVCDQSDI RGHRRTYVGS MPGRIINGLK TVGVNNPVFL LDEVDKLGKS 450
LQGDPAAALL EVLDPEQNHN FTDHYLNVAF DLSQVLFIAT ANTTATIPAA 500
LLDRMEIIQV PGYTQEEKIE IAHRHLIPKQ LEQHGLTPQQ IQIPQVTTLD 550
IITRYTREAG VRSLDRKLGA ICRAVAVKVA EGQHKEAKLD RSDVTEREGC 600
REHILEDEKP ESISDTTDLA LPPEMPILID FHALKDILGP PMYEMEVSQR 650
LSQPGVAIGL AWTPLGGEIM FVEASRMDGE GQLTLTGQLG DVMKESAHLA 700
ISWLRSNAKK YQLTNAFGSF DLLDNTDIHL HFPAGAVTKD GPSAGVTIVT 750
CLASLFSGRL VRSDVAMTGE ITLRGLVLPV GGIKDKVLAA HRAGLKQVII 800
PRRNEKDLEG IPGNVRQDLS FVTASCLDEV LNAAFDGGFT VKTRPGLLNS 850
KL 852
Length:852
Mass (Da):94,617
Last modified:June 1, 2003 - v1
Checksum:i00444E4FF47417AC
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti255 – 2551S → A in AAI10435. 1 Publication
Sequence conflicti628 – 6281L → F in BAC11201. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS10734.1.
RefSeqiNP_113678.2. NM_031490.2.
UniGeneiHs.731827.

Genome annotation databases

EnsembliENST00000285737; ENSP00000285737; ENSG00000102910.
GeneIDi83752.
KEGGihsa:83752.
UCSCiuc002efi.1. human.

Polymorphism databases

DMDMi74727668.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS10734.1.
RefSeqi NP_113678.2. NM_031490.2.
UniGenei Hs.731827.

3D structure databases

ProteinModelPortali Q86WA8.
SMRi Q86WA8. Positions 269-835.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123755. 4 interactions.
IntActi Q86WA8. 5 interactions.
STRINGi 9606.ENSP00000285737.

Protein family/group databases

MEROPSi S16.006.

PTM databases

PhosphoSitei Q86WA8.

Polymorphism databases

DMDMi 74727668.

Proteomic databases

MaxQBi Q86WA8.
PaxDbi Q86WA8.
PRIDEi Q86WA8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000285737 ; ENSP00000285737 ; ENSG00000102910 .
GeneIDi 83752.
KEGGi hsa:83752.
UCSCi uc002efi.1. human.

Organism-specific databases

CTDi 83752.
GeneCardsi GC16P048278.
H-InvDB HIX0173249.
HGNCi HGNC:20598. LONP2.
HPAi HPA008862.
neXtProti NX_Q86WA8.
PharmGKBi PA162394186.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0466.
HOGENOMi HOG000261408.
HOVERGENi HBG000798.
InParanoidi Q86WA8.
KOi K01338.
OMAi DQREYFL.
OrthoDBi EOG77T13V.
PhylomeDBi Q86WA8.
TreeFami TF317215.

Enzyme and pathway databases

Reactomei REACT_16907. Association of TriC/CCT with target proteins during biosynthesis.

Miscellaneous databases

GenomeRNAii 83752.
NextBioi 72777.
PROi Q86WA8.

Gene expression databases

ArrayExpressi Q86WA8.
Bgeei Q86WA8.
CleanExi HS_LONP2.
Genevestigatori Q86WA8.

Family and domain databases

Gene3Di 3.30.230.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPi MF_03121. lonp2_euk.
InterProi IPR003593. 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 ]
PANTHERi PTHR10046. PTHR10046. 1 hit.
Pfami PF00004. AAA. 1 hit.
PF02190. LON. 1 hit.
PF05362. Lon_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF001174. Lon_proteas. 1 hit.
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsi TIGR00763. lon. 1 hit.
PROSITEi PS01046. LON_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLONP2_HUMAN
AccessioniPrimary (citable) accession number: Q86WA8
Secondary accession number(s): Q0D2H6
, Q8N3B9, Q8NCE9, Q96K43
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: June 1, 2003
Last modified: September 3, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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