ID A0A2R9AR28_PANPA Unreviewed; 808 AA.
AC A0A2R9AR28;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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:ENSPPAP00000019613.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000019613.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000019613.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000019613.1}
RP IDENTIFICATION.
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; AJFE02068016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02068017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02068018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02068019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02068020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003819850.1; XM_003819802.2.
DR AlphaFoldDB; A0A2R9AR28; -.
DR Ensembl; ENSPPAT00000042382.1; ENSPPAP00000019613.1; ENSPPAG00000033002.1.
DR GeneTree; ENSGT00530000063553; -.
DR Proteomes; UP000240080; Chromosome 16.
DR Bgee; ENSPPAG00000033002; Expressed in liver and 6 other cell types or tissues.
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: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 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; 3.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 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:UP000240080};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03121}.
FT DOMAIN 13..251
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 607..793
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT MOTIF 806..808
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121"
FT ACT_SITE 699
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 742
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 331..338
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 808 AA; 89646 MW; A3BF955B911222A1 CRC64;
MSSVSPIQIP SRLPLLLTHE GVLLPGSTMR TSVDSARNLQ LVRSRLLKGT SLQSTILGVI
PNTPDPASDA QDLPPLHRIG TAALAVQVVG SNWPKPHYTL LITGLCRFQI VQVLKEKPYP
IAEVEQLDRL EEFPNTCKMR EELGELSEQF YKYAVQILDA VSLEERFKMT IPLLVRQIEG
LKLLQKTRKP KQDDDKRVIA IRPIRRITHI SGTLEDEDED EDNDDIVMLE KKIRTSSMPE
QAHKVCVKEI KRLKKMPQSM PEYALTRNYL ELMVELPWNK STTDRLDIRA ARILLDNDHY
AMEKLKKRVL EYLAVRQLKN NLKGPILCFV GPPGVGKTSV GRSVAKTLGR EFHRIALGGV
CDQSDIRGHR RTYVGSMPGR IINGLKTVGV NNPVFLLDEV DKLGKSLQGD PAAALLEVLD
PEQNHNFTDH YLNVAFDLSQ VLFIATANTT ATIPAALLDR MEIIQVPGYT QEEKIEIAHR
HLIPKQLEQH GLTPQQIQIP QVTTLDIITR YTREAGVRSL DRKLGAICRA VAVKVAEGQH
KEAKLDRSDV TEREGCREHI LEDEKPESIS DTTDLALPPE MPILIDFHAL KDILGPPMYE
MEVSQRLSQP GVAIGLAWTP LGGEIMFVEA SRMDGEGQLT LTGQLGDVMK ESAHLAISWL
RSNAKKYQLT NAFGSFDLLD NTDVHLHFPA GAVTKDGPSA GVTIVTCLAS LFSGRLVRSD
VAMTGEITLR GLVLPVGGIK DKVLAAHRAG LKQVIIPRRN EKDLEGIPGN VRQDLSFVTA
SCLDEVLNAA FDGGFTVKTR PGLLNSKL
//
