ID W5Q5X1_SHEEP Unreviewed; 909 AA.
AC W5Q5X1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
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:ENSOARP00000018111.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000018111.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000018111.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000018111.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000018111.1}
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; AMGL01027637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5Q5X1; -.
DR SMR; W5Q5X1; -.
DR STRING; 9940.ENSOARP00000018111; -.
DR PaxDb; 9940-ENSOARP00000018111; -.
DR Ensembl; ENSOART00000018367.1; ENSOARP00000018111.1; ENSOARG00000016864.1.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_4_0_1; -.
DR OMA; GAWQVVD; -.
DR Proteomes; UP000002356; Chromosome 14.
DR Bgee; ENSOARG00000016864; Expressed in metanephros cortex and 56 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; 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:UP000002356};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03121}.
FT DOMAIN 70..277
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 708..894
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 907..909
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121"
FT ACT_SITE 800
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 843
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 432..439
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 909 AA; 99715 MW; 297FF74EFE6B5318 CRC64;
MCTAPGGGGG GGWGRVSGLS GPEAAARPSQ ILGRRRGGRA KPGVGLPGTV PARRGVAMSS
VSPIQIPSRL PLLLTHEGVL LPGSTMRTSV DSARNLQLVR SRLLKGTSLQ STILGVIPNT
PDPASDAQDL PPLHRIGTAA LAVQVVGSNW PKPHYTLLIT GLCRFQIIQV VKEKPYPVAE
VEQLDRLEEF PNTCKTREEL GELSEQFYKY AVQLVEMLDM SVPAVAKLRR LLDSLPREAL
PDILTSIIRT SNKEKLQILD AVSLEERFKM TIPLLVRQIE GLKLLQKTRK HKQDDDKRVI
AIRPMRRITH VSGALADEDE DEDNDDIVML EKKIRTSSMP EQAHKVCVKE IKRLKKMPQS
MPEYALTRNY LELMVELPWN KSTTDRLDIR AARVLLDNDH YAMEKLKKRV LEYLAVRQLK
NNLKGPILCF VGPPGVGKTS VGRSVAKTLG REFHRIALGG VCDQSDIRGH RRTYVGSMPG
RIINGLKTVG VNNPVFLLDE VDKLGKSLQG DPAAALLEVL DPEQNHNFTD HYLNVAFDLS
QVLFIATANT TATIPPALLD RMEIIQVPGY TQEEKIEIAH RHLIPKQLEQ HGLTPQQIQI
PQVTTLDIIT RYTREAGVRS LDRKLGAICR AVAVKVAEGQ HREARLDRPD AAEGEGCKEH
ILEDGKSNPV SDTTDLALPP EMPILIDFHA LKDILGPPMY EMEVSERLSQ PGVAIGLAWT
PLGGEIMFVE ASRMDGEGQL TLTGQLGNVM KESAHLAISW LRSNAKKYHL TNASGSFDLL
ENTDIHLHFP AGAVTKDGPS AGVTIATCLA SLFSGRLVRS DVAMTGEITL RGLVLPVGGI
KDKALAAHRA GLKRVIIPQR NEKDLEEIPA NVRQDLSFIT ASCLDEVLNA AFDGGFTVKA
RPGLLNSKL
//
