ID H0V1V1_CAVPO Unreviewed; 852 AA.
AC H0V1V1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Lon protease homolog 2, peroxisomal {ECO:0000256|HAMAP-Rule:MF_03121};
DE EC=3.4.21.- {ECO:0000256|HAMAP-Rule:MF_03121};
DE AltName: Full=Lon protease-like protein 2 {ECO:0000256|HAMAP-Rule:MF_03121};
DE Short=Lon protease 2 {ECO:0000256|HAMAP-Rule:MF_03121};
DE AltName: Full=Peroxisomal Lon protease {ECO:0000256|HAMAP-Rule:MF_03121};
GN Name=LONP2 {ECO:0000256|HAMAP-Rule:MF_03121,
GN ECO:0000313|Ensembl:ENSCPOP00000003484.2};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000003484.2, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000003484.2}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000003484.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|HAMAP-Rule:MF_03121}.
CC -!- SUBUNIT: Interacts with PEX5. Interacts with TYSND1.
CC {ECO:0000256|HAMAP-Rule:MF_03121}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000256|ARBA:ARBA00004253,
CC ECO:0000256|HAMAP-Rule:MF_03121}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC Rule:MF_03121, ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}.
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DR EMBL; AAKN02033478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02033479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003469479.1; XM_003469431.3.
DR AlphaFoldDB; H0V1V1; -.
DR STRING; 10141.ENSCPOP00000003484; -.
DR MEROPS; S16.006; -.
DR Ensembl; ENSCPOT00000003903.3; ENSCPOP00000003484.2; ENSCPOG00000003859.4.
DR GeneID; 100716541; -.
DR KEGG; cpoc:100716541; -.
DR CTD; 83752; -.
DR VEuPathDB; HostDB:ENSCPOG00000003859; -.
DR eggNOG; KOG2004; Eukaryota.
DR GeneTree; ENSGT00530000063553; -.
DR HOGENOM; CLU_004109_4_2_1; -.
DR InParanoid; H0V1V1; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 1103874at2759; -.
DR TreeFam; TF317215; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000003859; Expressed in liver and 13 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
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:0002020; F:protease binding; IEA:Ensembl.
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; IEA:UniProtKB-UniRule.
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; IEA:Ensembl.
DR GO; GO:0031998; P:regulation of fatty acid beta-oxidation; IEA:Ensembl.
DR CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF24; LON PROTEASE HOMOLOG 2, PEROXISOMAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 2.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03121};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03121, ECO:0000256|PIRNR:PIRNR001174};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03121,
KW ECO:0000256|PIRNR:PIRNR001174};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140, ECO:0000256|HAMAP-
KW Rule:MF_03121};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_03121};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03121}.
FT DOMAIN 13..220
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 651..837
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT MOTIF 850..852
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121"
FT ACT_SITE 743
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 786
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 375..382
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 852 AA; 94206 MW; D56A9AEBE0C6DF32 CRC64;
MSSVNPIQIP SRLPLLLTHE GVLLPGSTMR TSVDTARNLQ LVRSRLLKGT SLQSTILGVI
PNTPDPASDA QDLPPLHRIG TAALAVQVVG SNWPKPHYTL LITGLCRFQI VQVLKEKPYP
VAEVEQLDRL EEFPNTCQSR EELGELSEQF YKYAVQLVEM LDMSVPAVAK LRRLLDSLPR
EALPDILTSI IRTSNKEKLQ ILDAVSLEER FKMTIPLLVR QIEGLKLLQK TRKPKQDDDK
RVIAIRPIRR IAHIPSTLED EDEDEENDDI VMLEKKIRAS SMPEQAHKVC VKEIKRLKKM
PQSMPEYALT RNYLELMVEL PWNKSTTDRL DIRAARVLLD NDHYAMEKLK KRVLEYLAVR
QLKNNLKGPI LCFVGPPGVG KTSVGRSVAK TLGREFHRIA LGGVCDQSDI RGHRRTYVGS
MPGRIINGLK TVGVNNPVFL LDEVDKLGKS LQGDPAAALL EVLDPEQNHN FTDHYLNVAF
DLSQVLFIAT ANTTATIPPA LLDRMEIIPV PGYSQEEKLE IAHRHLIPKQ LEQHGLTPQQ
IQIPQVTTLT IISRYTREAG VRSLDRKLGA ICRAVAVKVA EGQSKDAKLD RADVAAGEGC
REHVIEDTKH ESVSDATDLA LPPEMPIVID SHALKDILGP PMYEMEVSER LSQPGVAIGL
AWTPLGGKIM FVEASRMDGD GQLTLTGQLG DVMKESAHLA ISWLRSNAKR FHLTNAFGSF
DLLDNTDIHL HFPAGAVTKD GPSAGVTIVT CLASLFSGRL VRSDVAMTGE ITLRGLVLPV
GGIKDKVLAA HRAGLKRIII PQRNEKDLEE LPSNVRQDLS FVPASCLDEV LNAAFDGGFS
VKARPGLVNS KL
//
