LONP2_MOUSE
ID LONP2_MOUSE Reviewed; 852 AA.
AC Q9DBN5; Q3TEG8; Q3TFY6; Q3TGR0; Q3UAE1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Lon protease homolog 2, peroxisomal {ECO:0000255|HAMAP-Rule:MF_03121};
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03121};
DE AltName: Full=Lon protease-like protein 2 {ECO:0000255|HAMAP-Rule:MF_03121};
DE Short=Lon protease 2 {ECO:0000255|HAMAP-Rule:MF_03121};
DE AltName: Full=Peroxisomal Lon protease {ECO:0000255|HAMAP-Rule:MF_03121};
GN Name=Lonp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Amnion, Bone marrow, Liver, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of misfolded and unassembled polypeptides in the
CC peroxisomal matrix. Necessary for type 2 peroxisome targeting signal
CC (PTS2)-containing protein processing and facilitates peroxisome matrix
CC protein import. May indirectly regulate peroxisomal fatty acid beta-
CC oxidation through degradation of the self-processed forms of TYSND1.
CC {ECO:0000255|HAMAP-Rule:MF_03121}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03121};
CC -!- SUBUNIT: Interacts with PEX5. Interacts with TYSND1 (By similarity).
CC May interact with enzymes involved in beta-oxidation of fatty acids,
CC including ACOX1/AOX (By similarity). {ECO:0000250|UniProtKB:Q86WA8,
CC ECO:0000255|HAMAP-Rule:MF_03121}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:Q86WA8,
CC ECO:0000255|HAMAP-Rule:MF_03121}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9DBN5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DBN5-2; Sequence=VSP_025577, VSP_025578;
CC Name=3;
CC IsoId=Q9DBN5-3; Sequence=VSP_025576;
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_03121}.
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DR EMBL; AK004843; BAB23609.1; -; mRNA.
DR EMBL; AK050231; BAC34137.1; -; mRNA.
DR EMBL; AK151103; BAE30113.1; -; mRNA.
DR EMBL; AK151406; BAE30373.1; -; mRNA.
DR EMBL; AK168791; BAE40624.1; -; mRNA.
DR EMBL; AK168628; BAE40488.1; -; mRNA.
DR EMBL; AK168956; BAE40762.1; -; mRNA.
DR EMBL; AK169656; BAE41280.1; -; mRNA.
DR EMBL; BC049090; AAH49090.1; -; mRNA.
DR CCDS; CCDS22503.1; -. [Q9DBN5-1]
DR RefSeq; NP_001162063.1; NM_001168591.1.
DR RefSeq; NP_080103.1; NM_025827.3. [Q9DBN5-1]
DR AlphaFoldDB; Q9DBN5; -.
DR SMR; Q9DBN5; -.
DR BioGRID; 211789; 3.
DR STRING; 10090.ENSMUSP00000034141; -.
DR iPTMnet; Q9DBN5; -.
DR PhosphoSitePlus; Q9DBN5; -.
DR SwissPalm; Q9DBN5; -.
DR EPD; Q9DBN5; -.
DR jPOST; Q9DBN5; -.
DR MaxQB; Q9DBN5; -.
DR PaxDb; Q9DBN5; -.
DR PeptideAtlas; Q9DBN5; -.
DR PRIDE; Q9DBN5; -.
DR ProteomicsDB; 290051; -. [Q9DBN5-1]
DR ProteomicsDB; 290052; -. [Q9DBN5-2]
DR ProteomicsDB; 290053; -. [Q9DBN5-3]
DR Antibodypedia; 1715; 138 antibodies from 27 providers.
DR DNASU; 66887; -.
DR Ensembl; ENSMUST00000034141; ENSMUSP00000034141; ENSMUSG00000047866. [Q9DBN5-1]
DR Ensembl; ENSMUST00000122188; ENSMUSP00000113834; ENSMUSG00000047866. [Q9DBN5-3]
DR Ensembl; ENSMUST00000155433; ENSMUSP00000118737; ENSMUSG00000047866. [Q9DBN5-2]
DR GeneID; 66887; -.
DR KEGG; mmu:66887; -.
DR UCSC; uc009mqm.3; mouse. [Q9DBN5-1]
DR CTD; 83752; -.
DR MGI; MGI:1914137; Lonp2.
DR VEuPathDB; HostDB:ENSMUSG00000047866; -.
DR eggNOG; KOG2004; Eukaryota.
DR GeneTree; ENSGT00530000063553; -.
DR HOGENOM; CLU_004109_4_2_1; -.
DR InParanoid; Q9DBN5; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 528132at2759; -.
DR PhylomeDB; Q9DBN5; -.
DR TreeFam; TF317215; -.
DR BRENDA; 3.6.4.7; 3474.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR BioGRID-ORCS; 66887; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Lonp2; mouse.
DR PRO; PR:Q9DBN5; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9DBN5; protein.
DR Bgee; ENSMUSG00000047866; Expressed in left lobe of liver and 261 other tissues.
DR ExpressionAtlas; Q9DBN5; baseline and differential.
DR Genevisible; Q9DBN5; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005782; C:peroxisomal matrix; ISS:HGNC-UCL.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IEA:UniProtKB-UniRule.
DR GO; GO:0016485; P:protein processing; ISO:MGI.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR GO; GO:0006625; P:protein targeting to peroxisome; ISO:MGI.
DR GO; GO:0031998; P:regulation of fatty acid beta-oxidation; ISO:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR Gene3D; 2.30.130.40; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03121; lonp2_euk; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR004815; Lon_bac/euk-typ.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR027501; Lonp2_euk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10046; PTHR10046; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00763; lon; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Hydrolase;
KW Nucleotide-binding; Peroxisome; Protease; Reference proteome;
KW Serine protease.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q86WA8"
FT CHAIN 2..852
FT /note="Lon protease homolog 2, peroxisomal"
FT /id="PRO_0000287641"
FT DOMAIN 13..220
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 651..837
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT MOTIF 850..852
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT ACT_SITE 743
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT ACT_SITE 786
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT BINDING 375..382
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WA8"
FT VAR_SEQ 178..319
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025576"
FT VAR_SEQ 648..659
FT /note="SERLSQPGVAIG -> MILISMFTLVLA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025577"
FT VAR_SEQ 660..852
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025578"
FT CONFLICT 87
FT /note="Q -> P (in Ref. 1; BAE30373)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="K -> E (in Ref. 1; BAE40624/BAE40762)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="D -> V (in Ref. 1; BAE30373)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 852 AA; 94526 MW; 890BD7E654D04DC7 CRC64;
MSSVSPIQIP SRLPLLLTHE SVLLPGSTMR TSVDTARNLQ LVRSRLLKGT SLQSTILGVI
PNTPDPASDT QDLPPLHRIG TAALAVQVVG SNWPKPHYTL LITGLCRFQI VQVLKEKPYP
VAEVEQLDRL EEFPNICKSR EELGELSEQF YRYAVQLVEM LDMSVPAVAK LRRLLDNLPR
EALPDILTSI IRTSNKEKLQ ILDAVSLEDR FKMTIPLLVR QIEGLKLLQK TRKPKQDDDK
RVIAIRPIRR IPHIPGTLED EEEEEDNDDI VMLEKKIRTS SMPEQAHKVC VKEIKRLKKM
PQSMPEYALT RNYLELMVEL PWNKSTTDRL DIRAARILLD NDHYAMEKLK RRVLEYLAVR
QLKNNLKGPI LCFVGPPGVG KTSVGRSVAK TLGREFHRIA LGGVCDQSDI RGHRRTYVGS
MPGRIINGLK TVGVNNPVFL LDEVDKLGKS LQGDPAAALL EVLDPEQNHN FTDHYLNVAF
DLSQVLFIAT ANTTATIPPA LLDRMEIIQV PGYTQEEKIE IAHRHLIPKQ LEQHGLTPQQ
IQIPQHTTLA IITRYTREAG VRSLDRKFGA ICRAVAVKVA EGQHKEAKLD RSDVADGEGC
KEHVLEDAKP ESISDTADLA LPPEMPILID SHALKDILGP PLYELEVSER LSQPGVAIGL
AWTPLGGKIM FVEASRMDGE GQLTLTGQLG DVMKESAHLA ISWLRSNAKK YHLTNAFGSF
DLLDNTDIHL HFPAGAVTKD GPSAGVTIVT CLASLFSGRL VRSDVAMTGE ITLRGLVLPV
GGIKDKVLAA HRAGLKQIII PQRNEKDLEE IPSNVRQDLS FVTASCLDEV LNAAFDGGFP
VKTRPGLIDS KL
