LONM_BOVIN
ID LONM_BOVIN Reviewed; 961 AA.
AC Q59HJ6; A3KN23;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Lon protease homolog, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03120};
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03120};
DE AltName: Full=Lon protease-like protein {ECO:0000255|HAMAP-Rule:MF_03120};
DE Short=LONP {ECO:0000255|HAMAP-Rule:MF_03120};
DE AltName: Full=Mitochondrial ATP-dependent protease Lon {ECO:0000255|HAMAP-Rule:MF_03120};
DE AltName: Full=Serine protease 15 {ECO:0000255|HAMAP-Rule:MF_03120};
DE Flags: Precursor;
GN Name=LONP1 {ECO:0000255|HAMAP-Rule:MF_03120}; Synonyms=PRSS15;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Adrenal cortex;
RX PubMed=16287628; DOI=10.1080/10425170500289233;
RA Yamamoto M., Hiroi T., Kohno H., Yamamoto Y., Hara M., Tanaka T., Mamba K.,
RA Watabe S.;
RT "Nucleotide sequence for cDNA of bovine mitochondrial ATP-dependent
RT protease and determination of N-terminus of the mature enzyme from the
RT adrenal cortex.";
RL DNA Seq. 16:474-478(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, SUBSTRATE, AND SUBCELLULAR LOCATION.
RX PubMed=12198491; DOI=10.1038/ncb836;
RA Bota D.A., Davies K.J.;
RT "Lon protease preferentially degrades oxidized mitochondrial aconitase by
RT an ATP-stimulated mechanism.";
RL Nat. Cell Biol. 4:674-680(2002).
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of misfolded, unassembled or oxidatively damaged
CC polypeptides as well as certain short-lived regulatory proteins in the
CC mitochondrial matrix. May also have a chaperone function in the
CC assembly of inner membrane protein complexes. Participates in the
CC regulation of mitochondrial gene expression and in the maintenance of
CC the integrity of the mitochondrial genome. Binds to mitochondrial
CC promoters and RNA in a single-stranded, site-specific, and strand-
CC specific manner. May regulate mitochondrial DNA replication and/or gene
CC expression using site-specific, single-stranded DNA binding to target
CC the degradation of regulatory proteins binding to adjacent sites in
CC mitochondrial promoters (By similarity). Endogenous substrates include
CC oxidized aconitase. {ECO:0000255|HAMAP-Rule:MF_03120,
CC ECO:0000269|PubMed:12198491}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03120};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity. The
CC ATP-binding and proteolytic domains (AP-domain) form a hexameric
CC chamber, while the N-terminal domain is arranged as a trimer of dimers.
CC DNA and RNA binding is stimulated by substrate and inhibited by ATP
CC binding. Interacts with TWNK and mitochondrial DNA polymerase subunit
CC POLG. {ECO:0000255|HAMAP-Rule:MF_03120}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03120}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_03120}.
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DR EMBL; AB208555; BAD91492.1; -; mRNA.
DR EMBL; BC133505; AAI33506.1; -; mRNA.
DR RefSeq; NP_001015569.2; NM_001015569.3.
DR AlphaFoldDB; Q59HJ6; -.
DR SMR; Q59HJ6; -.
DR STRING; 9913.ENSBTAP00000002350; -.
DR MEROPS; S16.002; -.
DR PaxDb; Q59HJ6; -.
DR PeptideAtlas; Q59HJ6; -.
DR PRIDE; Q59HJ6; -.
DR GeneID; 510796; -.
DR KEGG; bta:510796; -.
DR CTD; 9361; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_1_0_1; -.
DR InParanoid; Q59HJ6; -.
DR OrthoDB; 528132at2759; -.
DR TreeFam; TF105001; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0070407; P:oxidation-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR Gene3D; 2.30.130.40; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03120; lonm_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; IPR027503; Lonm_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; PTHR43718; PTHR43718; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 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 ATP-binding; Direct protein sequencing; DNA-binding; Hydrolase;
KW Mitochondrion; Nucleotide-binding; Protease; Reference proteome;
KW Serine protease; Transit peptide.
FT TRANSIT 1..67
FT /note="Mitochondrion"
FT CHAIN 68..961
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000254960"
FT DOMAIN 125..369
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 760..951
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 76..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 857
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 900
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 524..531
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT CONFLICT 159
FT /note="H -> R (in Ref. 2; AAI33506)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 961 AA; 106670 MW; D638A978087B81AA CRC64;
MAGGTGCVRL WGAARCWTLR RPLLAAAGGR VPTAARAWLP RGRRACDASP PWALWGQSPA
AAGHWRGLWE ANNRSGGGAF SGGEDASEGG AEDGASGVGG SAGGGEGPVI TALTPMMIPD
VFPHLPLIAV TRNPVFPRFI KIVEVKNKKL VELLRRKVHL AQPYAGVFLK KDDNNESDVV
ENLDEIYHTG TFVQIHEMQD LGDKLRMIVM GHRRVHINRQ LEVEPEEPEG ENKQKLRKKP
KRGKKEAEED GATKRPLEVV VGPGPSPAGE VLMVEVENVA HEDFQVTEEV KALTAEIVKT
IRDIIALNPL YRESVLQMMQ AGHRVVDNPI YLSDMGAALT GAESHELQEV LEETNIPKRL
YKALSLLKKE FELSKLQQRL GREVEEKIKQ THRKYLLQEQ LKIIKKELGL EKDDKDAIEE
KFRERLKELV VPKHVMDVVD EELSKLGLLD NHSSEFNVTR NYLDWLTSIP WGKHSDENLD
LARAQAVLEE DHYGMEDVKK RILEFIAVSQ LRGSTQGKIL CFYGPPGVGK TSIARSIARA
LNREYFRFSV GGMTDVAEIK GHRRTYVGAM PGKIIQCLKK TKTENPLVLI DEVDKIGRGY
QGDPSSALLE LLDPEQNANF LDHYLDVPVD LSKVLFICTA NITETIPEPL RDRMEMINVS
GYVAQEKLAI AERYLVPQAR ALCGLDESKA KLSSDVLTLL IKQYCRESGV RNLQKQVEKV
LRKSAYKIVS GEAEFVEVTP ENLQDFVGKP VFTVERMYDV TPPGVVMGLA WTAMGGSTLF
VETSLRRPRD RDSDKGDKDG SLEVTGQLGE VMKESARIAY TFARAFLMQH DSANKFLVTS
HIHLHVPEGA TPKDGPSAGC TIVTALLSLA LDRPVRQNLA MTGEVSLTGK VLPVGGIKEK
TIAAKRAGVT CIVLPAENKK DFYDLAAFIT EGLEVHFVEH YREIFDIAFP EERAEALAVE
R
