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Lon protease homolog, mitochondrial (EC 3.4.21.53) (LONHs) (Lon protease-like protein) (LONP) (Mitochondrial ATP-dependent protease Lon) (Serine protease 15)

 LONM_HUMAN              Reviewed;         959 AA.
P36776; B3KPH8; D6W635; E5KMH8; F5GZ27; P36777; Q8N8K8; Q9UQ95;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
05-DEC-2018, entry version 188.
RecName: Full=Lon protease homolog, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03120};
EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03120};
AltName: Full=LONHs;
AltName: Full=Lon protease-like protein {ECO:0000255|HAMAP-Rule:MF_03120};
Short=LONP {ECO:0000255|HAMAP-Rule:MF_03120};
AltName: Full=Mitochondrial ATP-dependent protease Lon {ECO:0000255|HAMAP-Rule:MF_03120};
AltName: Full=Serine protease 15 {ECO:0000255|HAMAP-Rule:MF_03120};
Flags: Precursor;
Name=LONP1 {ECO:0000255|HAMAP-Rule:MF_03120}; Synonyms=PRSS15;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
TISSUE=Brain;
PubMed=8248235; DOI=10.1073/pnas.90.23.11247;
Wang N., Gottesman S., Willingham M.C., Gottesman M.M., Maurizi M.R.;
"A human mitochondrial ATP-dependent protease that is highly
homologous to bacterial Lon protease.";
Proc. Natl. Acad. Sci. U.S.A. 90:11247-11251(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-911.
PubMed=20843780; DOI=10.1093/nar/gkq750;
Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R.,
Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W.,
Mindrinos M., Speed T.P., Scharfe C.;
"Identification of rare DNA variants in mitochondrial disorders with
improved array-based sequencing.";
Nucleic Acids Res. 39:44-58(2011).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Huang N.N., Maurizi M.R., Torres R.R., Polymeropoulos M.H.,
Lennon G.G., Gottesman M.M.;
"Chromosomal mapping and genomic organization of the ATP-dependent
human LON protease gene.";
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-959 (ISOFORM 1), AND VARIANT ILE-911.
TISSUE=Brain;
PubMed=8119403; DOI=10.1016/0014-5793(94)80166-5;
Amerik A.Y., Petukhova G.V., Grigorenko V.G., Lykov I.P.,
Yarovoi S.V., Lipkin V.M., Gorbalenya A.E.;
"Cloning and sequence analysis of cDNA for a human homolog of
eubacterial ATP-dependent Lon proteases.";
FEBS Lett. 340:25-28(1994).
[9]
SUBCELLULAR LOCATION.
PubMed=7961901;
Wang N., Maurizi M.R., Emmert-Buck L., Gottesman M.M.;
"Synthesis, processing, and localization of human Lon protease.";
J. Biol. Chem. 269:29308-29313(1994).
[10]
DNA-BINDING.
PubMed=9485316; DOI=10.1021/bi970928c;
Fu G.K., Markovitz D.M.;
"The human LON protease binds to mitochondrial promoters in a single-
stranded, site-specific, strand-specific manner.";
Biochemistry 37:1905-1909(1998).
[11]
FUNCTION.
PubMed=12198491; DOI=10.1038/ncb836;
Bota D.A., Davies K.J.;
"Lon protease preferentially degrades oxidized mitochondrial aconitase
by an ATP-stimulated mechanism.";
Nat. Cell Biol. 4:674-680(2002).
[12]
DNA-BINDING, MUTAGENESIS OF SER-855, SUBUNIT, AND INTERACTION WITH
TWNK AND POLG.
PubMed=14739292; DOI=10.1074/jbc.M309642200;
Liu T., Lu B., Lee I., Ondrovicova G., Kutejova E., Suzuki C.K.;
"DNA and RNA binding by the mitochondrial lon protease is regulated by
nucleotide and protein substrate.";
J. Biol. Chem. 279:13902-13910(2004).
[13]
FUNCTION.
PubMed=15870080; DOI=10.1074/jbc.M502796200;
Ondrovicova G., Liu T., Singh K., Tian B., Li H., Gakh O., Perecko D.,
Janata J., Granot Z., Orly J., Kutejova E., Suzuki C.K.;
"Cleavage site selection within a folded substrate by the ATP-
dependent lon protease.";
J. Biol. Chem. 280:25103-25110(2005).
[14]
FUNCTION, AND DNA-BINDING.
PubMed=17420247; DOI=10.1074/jbc.M611540200;
Lu B., Yadav S., Shah P.G., Liu T., Tian B., Pukszta S., Villaluna N.,
Kutejova E., Newlon C.S., Santos J.H., Suzuki C.K.;
"Roles for the human ATP-dependent Lon protease in mitochondrial DNA
maintenance.";
J. Biol. Chem. 282:17363-17374(2007).
[15]
SUBSTRATE.
PubMed=17579211; DOI=10.1210/me.2005-0458;
Granot Z., Kobiler O., Melamed-Book N., Eimerl S., Bahat A., Lu B.,
Braun S., Maurizi M.R., Suzuki C.K., Oppenheim A.B., Orly J.;
"Turnover of mitochondrial steroidogenic acute regulatory (StAR)
protein by Lon protease: the unexpected effect of proteasome
inhibitors.";
Mol. Endocrinol. 21:2164-2177(2007).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
MUTAGENESIS OF LYS-529; TRP-770; THR-880 AND 893-GLY-GLY-894.
PubMed=24520911; DOI=10.1111/febs.12740;
Ambro L., Pevala V., Ondrovicova G., Bellova J., Kunova N.,
Kutejova E., Bauer J.;
"Mutations to a glycine loop in the catalytic site of human Lon
changes its protease, peptidase and ATPase activities.";
FEBS J. 281:1784-1797(2014).
[19]
SUBUNIT.
PubMed=25369343;
Kereiche S., Kovacik L., Pevala V., Ambro L., Bellova J., Kutejova E.,
Raska I.;
"Three-dimensional reconstruction of the S885A mutant of human
mitochondrial Lon protease.";
Folia Biol. (Praha) 60:62-65(2014).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
INVOLVEMENT IN CODASS, AND VARIANTS CODASS TYR-631; SER-676; GLY-721
AND VAL-724.
PubMed=25574826; DOI=10.1016/j.ajhg.2014.12.003;
Strauss K.A., Jinks R.N., Puffenberger E.G., Venkatesh S., Singh K.,
Cheng I., Mikita N., Thilagavathi J., Lee J., Sarafianos S.,
Benkert A., Koehler A., Zhu A., Trovillion V., McGlincy M., Morlet T.,
Deardorff M., Innes A.M., Prasad C., Chudley A.E., Lee I.N.,
Suzuki C.K.;
"CODAS syndrome is associated with mutations of LONP1, encoding
mitochondrial AAA+ Lon protease.";
Am. J. Hum. Genet. 96:121-135(2015).
[22]
INVOLVEMENT IN CODASS, AND VARIANTS CODASS ALA-476; VAL-670; CYS-672;
HIS-679; SER-749; GLU-767 AND ILE-927 DEL.
PubMed=25808063; DOI=10.1002/ajmg.a.37029;
Dikoglu E., Alfaiz A., Gorna M., Bertola D., Chae J.H., Cho T.J.,
Derbent M., Alanay Y., Guran T., Kim O.H., Llerenar J.C. Jr.,
Yamamoto G., Superti-Furga G., Reymond A., Xenarios I., Stevenson B.,
Campos-Xavier B., Bonafe L., Superti-Furga A., Unger S.;
"Mutations in LONP1, a mitochondrial matrix protease, cause CODAS
syndrome.";
Am. J. Med. Genet. A 167:1501-1509(2015).
[23]
CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLY-67, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[24]
SUBSTRATE.
PubMed=28377575; DOI=10.1038/s41598-017-00632-8;
Kunova N., Ondrovicova G., Bauer J.A., Bellova J., Ambro L.,
Martinakova L., Kotrasova V., Kutejova E., Pevala V.;
"The role of Lon-mediated proteolysis in the dynamics of mitochondrial
nucleic acid-protein complexes.";
Sci. Rep. 7:631-631(2017).
[25]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 753-959, AND SUBUNIT.
PubMed=20222013; DOI=10.1002/pro.376;
Garcia-Nafria J., Ondrovicova G., Blagova E., Levdikov V.M.,
Bauer J.A., Suzuki C.K., Kutejova E., Wilkinson A.J., Wilson K.S.;
"Structure of the catalytic domain of the human mitochondrial Lon
protease: proposed relation of oligomer formation and activity.";
Protein Sci. 19:987-999(2010).
[26]
CRYO-ELECTRON MICROSCOPY (15 ANGSTROMS) OF MUTANT ALA-855, SUBUNIT,
AND DOMAIN.
PubMed=27632940; DOI=10.1038/srep33631;
Kereiche S., Kovacik L., Bednar J., Pevala V., Kunova N.,
Ondrovicova G., Bauer J., Ambro L., Bellova J., Kutejova E., Raska I.;
"The N-terminal domain plays a crucial role in the structure of a
full-length human mitochondrial Lon protease.";
Sci. Rep. 6:33631-33631(2016).
-!- FUNCTION: ATP-dependent serine protease that mediates the
selective degradation of misfolded, unassembled or oxidatively
damaged polypeptides as well as certain short-lived regulatory
proteins in the mitochondrial matrix. May also have a chaperone
function in the assembly of inner membrane protein complexes.
Participates in the regulation of mitochondrial gene expression
and in the maintenance of the integrity of the mitochondrial
genome. Binds to mitochondrial promoters and RNA in a single-
stranded, site-specific, and strand-specific manner. May regulate
mitochondrial DNA replication and/or gene expression using site-
specific, single-stranded DNA binding to target the degradation of
regulatory proteins binding to adjacent sites in mitochondrial
promoters (PubMed:12198491, PubMed:15870080, PubMed:17420247,
PubMed:8248235). Endogenous substrates include mitochondrial
steroidogenic acute regulatory (StAR) protein, helicase Twinkle
(TWNK) and the large ribosomal subunit protein bL32m. bL32m is
protected from degradation by LONP1 when it is bound to a nucleic
acid (RNA), but TWNK is not (PubMed:17579211, PubMed:28377575).
{ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:12198491,
ECO:0000269|PubMed:15870080, ECO:0000269|PubMed:17420247,
ECO:0000269|PubMed:17579211, ECO:0000269|PubMed:28377575,
ECO:0000269|PubMed:8248235}.
-!- CATALYTIC ACTIVITY:
Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
Evidence={ECO:0000255|HAMAP-Rule:MF_03120};
-!- ACTIVITY REGULATION: Peptidase activity is subject to substrate
inhibition by ATP. {ECO:0000269|PubMed:24520911}.
-!- SUBUNIT: Homohexamer (PubMed:14739292, PubMed:25369343,
PubMed:20222013). Organized in a ring with a central cavity
(PubMed:25369343, PubMed:20222013). The ATP-binding and
proteolytic domains (AP-domain) form a hexameric chamber, while
the N-terminal domain is arranged as a trimer of dimers
(PubMed:27632940). DNA and RNA binding is stimulated by substrate
and inhibited by ATP binding. Interacts with TWNK and
mitochondrial DNA polymerase subunit POLG (PubMed:14739292).
{ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:14739292,
ECO:0000269|PubMed:20222013, ECO:0000269|PubMed:25369343,
ECO:0000269|PubMed:27632940}.
-!- INTERACTION:
P02666:CSN2 (xeno); NbExp=6; IntAct=EBI-357448, EBI-5260183;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
Rule:MF_03120, ECO:0000269|PubMed:7961901}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P36776-1; Sequence=Displayed;
Name=2;
IsoId=P36776-2; Sequence=VSP_054617;
Note=No experimental confirmation available.;
Name=3;
IsoId=P36776-3; Sequence=VSP_055310;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Duodenum, heart, lung and liver, but not
thymus.
-!- DOMAIN: The Lon N-terminal domains are crucial for the overall
structure of the protein, maintaining it in a conformation
allowing its proper functioning. {ECO:0000269|PubMed:27632940}.
-!- DOMAIN: The AP-domain (ATP-binding and proteolytic domains) has a
closed-ring conformation in the presence of AMP-PNP and its N-
terminal entry gate appears closed. Upon ADP binding, it switches
to a lock-washer conformation and its N-terminal gate opens.
{ECO:0000269|PubMed:27632940}.
-!- DOMAIN: The proteolytic site is connected to the ATP binding site
through the GG loop (Gly-893 and Gly-894) and the loop containing
Trp-770. Binding of a protein substrate such as beta-casein
appears to trigger movement of both these loops as part of the
conformational changes which lead to enhanced ATPase and peptidase
activities. {ECO:0000305|PubMed:24520911}.
-!- DISEASE: CODAS syndrome (CODASS) [MIM:600373]: A rare syndrome
characterized by the combination of cerebral, ocular, dental,
auricular, and skeletal features. These include developmental
delay, craniofacial anomalies, cataracts, ptosis, median nasal
groove, delayed tooth eruption, hearing loss, short stature,
delayed epiphyseal ossification, metaphyseal hip dysplasia, and
vertebral coronal clefts. {ECO:0000269|PubMed:25574826,
ECO:0000269|PubMed:25808063}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peptidase S16 family.
{ECO:0000255|HAMAP-Rule:MF_03120}.
-!- SEQUENCE CAUTION:
Sequence=CAA52291.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; U02389; AAA61616.1; -; mRNA.
EMBL; HQ204946; ADP90374.1; -; Genomic_DNA.
EMBL; HQ204947; ADP90375.1; -; Genomic_DNA.
EMBL; HQ204948; ADP90376.1; -; Genomic_DNA.
EMBL; HQ204949; ADP90377.1; -; Genomic_DNA.
EMBL; HQ204950; ADP90378.1; -; Genomic_DNA.
EMBL; HQ204951; ADP90379.1; -; Genomic_DNA.
EMBL; HQ204952; ADP90380.1; -; Genomic_DNA.
EMBL; HQ204953; ADP90381.1; -; Genomic_DNA.
EMBL; HQ204954; ADP90382.1; -; Genomic_DNA.
EMBL; HQ204955; ADP90383.1; -; Genomic_DNA.
EMBL; HQ204956; ADP90384.1; -; Genomic_DNA.
EMBL; HQ204957; ADP90385.1; -; Genomic_DNA.
EMBL; HQ204958; ADP90386.1; -; Genomic_DNA.
EMBL; HQ204959; ADP90387.1; -; Genomic_DNA.
EMBL; HQ204960; ADP90388.1; -; Genomic_DNA.
EMBL; HQ204961; ADP90389.1; -; Genomic_DNA.
EMBL; HQ204962; ADP90390.1; -; Genomic_DNA.
EMBL; HQ204963; ADP90391.1; -; Genomic_DNA.
EMBL; HQ204964; ADP90392.1; -; Genomic_DNA.
EMBL; HQ204965; ADP90393.1; -; Genomic_DNA.
EMBL; HQ204966; ADP90394.1; -; Genomic_DNA.
EMBL; HQ204968; ADP90396.1; -; Genomic_DNA.
EMBL; HQ204969; ADP90397.1; -; Genomic_DNA.
EMBL; HQ204970; ADP90398.1; -; Genomic_DNA.
EMBL; HQ204971; ADP90399.1; -; Genomic_DNA.
EMBL; HQ204972; ADP90400.1; -; Genomic_DNA.
EMBL; HQ204973; ADP90401.1; -; Genomic_DNA.
EMBL; HQ204974; ADP90402.1; -; Genomic_DNA.
EMBL; HQ204975; ADP90403.1; -; Genomic_DNA.
EMBL; HQ204976; ADP90404.1; -; Genomic_DNA.
EMBL; HQ204977; ADP90405.1; -; Genomic_DNA.
EMBL; HQ204978; ADP90406.1; -; Genomic_DNA.
EMBL; HQ204979; ADP90407.1; -; Genomic_DNA.
EMBL; HQ204980; ADP90408.1; -; Genomic_DNA.
EMBL; HQ204981; ADP90409.1; -; Genomic_DNA.
EMBL; HQ204982; ADP90410.1; -; Genomic_DNA.
EMBL; HQ204983; ADP90411.1; -; Genomic_DNA.
EMBL; HQ204984; ADP90412.1; -; Genomic_DNA.
EMBL; HQ204985; ADP90413.1; -; Genomic_DNA.
EMBL; AF059309; AAD24414.1; -; Genomic_DNA.
EMBL; AF059296; AAD24414.1; JOINED; Genomic_DNA.
EMBL; AF059297; AAD24414.1; JOINED; Genomic_DNA.
EMBL; AF059298; AAD24414.1; JOINED; Genomic_DNA.
EMBL; AF059299; AAD24414.1; JOINED; Genomic_DNA.
EMBL; AF059300; AAD24414.1; JOINED; Genomic_DNA.
EMBL; AF059301; AAD24414.1; JOINED; Genomic_DNA.
EMBL; AF059302; AAD24414.1; JOINED; Genomic_DNA.
EMBL; AF059303; AAD24414.1; JOINED; Genomic_DNA.
EMBL; AF059304; AAD24414.1; JOINED; Genomic_DNA.
EMBL; AF059305; AAD24414.1; JOINED; Genomic_DNA.
EMBL; AF059306; AAD24414.1; JOINED; Genomic_DNA.
EMBL; AF059307; AAD24414.1; JOINED; Genomic_DNA.
EMBL; AF059308; AAD24414.1; JOINED; Genomic_DNA.
EMBL; AK056366; BAG51690.1; -; mRNA.
EMBL; AK096626; BAC04829.1; -; mRNA.
EMBL; AC011499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471139; EAW69151.1; -; Genomic_DNA.
EMBL; CH471139; EAW69154.1; -; Genomic_DNA.
EMBL; BC000235; AAH00235.1; -; mRNA.
EMBL; X74215; CAA52291.1; ALT_INIT; mRNA.
EMBL; X76040; CAA53625.1; -; mRNA.
CCDS; CCDS12148.1; -. [P36776-1]
CCDS; CCDS62507.1; -. [P36776-3]
CCDS; CCDS62508.1; -. [P36776-2]
PIR; S42366; S42366.
PIR; S57342; S57342.
RefSeq; NP_001263408.1; NM_001276479.1. [P36776-2]
RefSeq; NP_001263409.1; NM_001276480.1. [P36776-3]
RefSeq; NP_004784.2; NM_004793.3. [P36776-1]
UniGene; Hs.350265; -.
PDB; 2X36; X-ray; 2.00 A; A/B/C/D/E/F=753-959.
PDBsum; 2X36; -.
ProteinModelPortal; P36776; -.
SMR; P36776; -.
BioGrid; 114762; 77.
IntAct; P36776; 47.
MINT; P36776; -.
STRING; 9606.ENSP00000353826; -.
MEROPS; S16.002; -.
MoonDB; P36776; Curated.
iPTMnet; P36776; -.
PhosphoSitePlus; P36776; -.
SwissPalm; P36776; -.
DMDM; 12644239; -.
EPD; P36776; -.
MaxQB; P36776; -.
PaxDb; P36776; -.
PeptideAtlas; P36776; -.
PRIDE; P36776; -.
ProteomicsDB; 55221; -.
DNASU; 9361; -.
Ensembl; ENST00000360614; ENSP00000353826; ENSG00000196365. [P36776-1]
Ensembl; ENST00000540670; ENSP00000441523; ENSG00000196365. [P36776-3]
Ensembl; ENST00000593119; ENSP00000468541; ENSG00000196365. [P36776-2]
GeneID; 9361; -.
KEGG; hsa:9361; -.
UCSC; uc002mcx.5; human. [P36776-1]
CTD; 9361; -.
DisGeNET; 9361; -.
EuPathDB; HostDB:ENSG00000196365.11; -.
GeneCards; LONP1; -.
HGNC; HGNC:9479; LONP1.
HPA; HPA002034; -.
HPA; HPA002192; -.
MalaCards; LONP1; -.
MIM; 600373; phenotype.
MIM; 605490; gene.
neXtProt; NX_P36776; -.
OpenTargets; ENSG00000196365; -.
Orphanet; 1458; CODAS syndrome.
PharmGKB; PA162394145; -.
eggNOG; KOG2004; Eukaryota.
eggNOG; COG0466; LUCA.
GeneTree; ENSGT00530000063553; -.
HOGENOM; HOG000261409; -.
HOVERGEN; HBG000798; -.
InParanoid; P36776; -.
KO; K08675; -.
OMA; AKIAYTF; -.
OrthoDB; EOG091G01TN; -.
PhylomeDB; P36776; -.
TreeFam; TF105001; -.
BRENDA; 3.4.21.53; 2681.
ChiTaRS; LONP1; human.
EvolutionaryTrace; P36776; -.
GeneWiki; LONP1; -.
GenomeRNAi; 9361; -.
PRO; PR:P36776; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000196365; Expressed in 220 organ(s), highest expression level in right adrenal gland.
CleanEx; HS_LONP1; -.
ExpressionAtlas; P36776; baseline and differential.
Genevisible; P36776; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; IMP:UniProtKB.
GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0043531; F:ADP binding; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0004176; F:ATP-dependent peptidase activity; IDA:UniProtKB.
GO; GO:0070182; F:DNA polymerase binding; IPI:UniProtKB.
GO; GO:0051880; F:G-quadruplex DNA binding; IDA:UniProtKB.
GO; GO:0001018; F:mitochondrial promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0034599; P:cellular response to oxidative stress; IDA:UniProtKB.
GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
GO; GO:0032042; P:mitochondrial DNA metabolic process; NAS:UniProtKB.
GO; GO:0000002; P:mitochondrial genome maintenance; NAS:UniProtKB.
GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
GO; GO:0070407; P:oxidation-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IDA:UniProtKB.
GO; GO:0010044; P:response to aluminum ion; IEA:Ensembl.
GO; GO:0009725; P:response to hormone; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEP:UniProtKB.
Gene3D; 3.30.230.10; -; 1.
HAMAP; MF_03120; lonm_euk; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR004815; Lon_bac/euk-typ.
InterPro; IPR008269; Lon_proteolytic.
InterPro; IPR027065; Lon_Prtase.
InterPro; IPR003111; Lon_substr-bd.
InterPro; IPR027503; Lonm_euk.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008268; Peptidase_S16_AS.
InterPro; IPR015947; PUA-like_sf.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
PANTHER; PTHR43718; PTHR43718; 1.
Pfam; PF00004; AAA; 1.
Pfam; PF05362; Lon_C; 1.
Pfam; PF02190; LON_substr_bdg; 1.
SMART; SM00382; AAA; 1.
SMART; SM00464; LON; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF88697; SSF88697; 1.
TIGRFAMs; TIGR00763; lon; 1.
PROSITE; PS51787; LON_N; 1.
PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PROSITE; PS01046; LON_SER; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cataract;
Complete proteome; Deafness; Disease mutation; DNA-binding; Dwarfism;
Hydrolase; Mitochondrion; Nucleotide-binding; Polymorphism; Protease;
Reference proteome; Serine protease; Transit peptide.
TRANSIT 1 67 Mitochondrion.
{ECO:0000244|PubMed:25944712,
ECO:0000255|HAMAP-Rule:MF_03120}.
CHAIN 68 959 Lon protease homolog, mitochondrial.
/FTId=PRO_0000026734.
DOMAIN 124 368 Lon N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU01123}.
DOMAIN 759 949 Lon proteolytic. {ECO:0000255|PROSITE-
ProRule:PRU01122}.
NP_BIND 523 530 ATP. {ECO:0000255|HAMAP-Rule:MF_03120}.
ACT_SITE 855 855 {ECO:0000255|HAMAP-Rule:MF_03120}.
ACT_SITE 898 898 {ECO:0000255|HAMAP-Rule:MF_03120}.
VAR_SEQ 1 196 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055310.
VAR_SEQ 42 105 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054617.
VARIANT 87 87 E -> D (in dbSNP:rs34413649).
/FTId=VAR_051564.
VARIANT 241 241 R -> Q (in dbSNP:rs11085147).
/FTId=VAR_051565.
VARIANT 476 476 E -> A (in CODASS).
{ECO:0000269|PubMed:25808063}.
/FTId=VAR_073338.
VARIANT 631 631 S -> Y (in CODASS; dbSNP:rs879255248).
{ECO:0000269|PubMed:25574826}.
/FTId=VAR_073339.
VARIANT 670 670 A -> V (in CODASS; dbSNP:rs770036526).
{ECO:0000269|PubMed:25808063}.
/FTId=VAR_073340.
VARIANT 672 672 R -> C (in CODASS; dbSNP:rs777009012).
{ECO:0000269|PubMed:25808063}.
/FTId=VAR_073341.
VARIANT 676 676 P -> S (in CODASS; dbSNP:rs879255247).
{ECO:0000269|PubMed:25574826}.
/FTId=VAR_073342.
VARIANT 679 679 R -> H (in CODASS; dbSNP:rs549574673).
{ECO:0000269|PubMed:25808063}.
/FTId=VAR_073343.
VARIANT 721 721 R -> G (in CODASS; dbSNP:rs147588238).
{ECO:0000269|PubMed:25574826}.
/FTId=VAR_073344.
VARIANT 724 724 A -> V (in CODASS; dbSNP:rs879255249).
{ECO:0000269|PubMed:25574826}.
/FTId=VAR_073345.
VARIANT 749 749 P -> S (in CODASS).
{ECO:0000269|PubMed:25808063}.
/FTId=VAR_073346.
VARIANT 767 767 G -> E (in CODASS; dbSNP:rs562553348).
{ECO:0000269|PubMed:25808063}.
/FTId=VAR_073347.
VARIANT 829 829 A -> T (in dbSNP:rs35804229).
/FTId=VAR_067708.
VARIANT 911 911 V -> I (in dbSNP:rs1062373).
{ECO:0000269|PubMed:20843780,
ECO:0000269|PubMed:8119403}.
/FTId=VAR_067709.
VARIANT 927 927 Missing (in CODASS).
{ECO:0000269|PubMed:25808063}.
/FTId=VAR_073348.
MUTAGEN 529 529 K->R: Abolishes ATPase activity, and
presumably ATP-driven protein unfolding,
but does not block access to the
proteolytic active site or prevent a
substrate from binding to it.
{ECO:0000269|PubMed:24520911}.
MUTAGEN 770 770 W->A: Has low basal, but normal
stimulated ATPase activity, and retains
peptidase activity.
{ECO:0000269|PubMed:24520911}.
MUTAGEN 770 770 W->P: Has normal basal, but low
stimulated ATPase activity, and abolishes
peptidase activity.
{ECO:0000269|PubMed:24520911}.
MUTAGEN 855 855 S->A: Lacks both ATPase and protease
activity, but retains DNA binding
activity. {ECO:0000269|PubMed:14739292,
ECO:0000269|PubMed:24520911}.
MUTAGEN 880 880 T->V: Enhances the basal, but not the
stimulated ATPase activity.
{ECO:0000269|PubMed:24520911}.
MUTAGEN 893 893 G->A: Has low basal, but normal
stimulated ATPase activity, and retains
peptidase activity.
{ECO:0000269|PubMed:24520911}.
MUTAGEN 893 893 G->P: Has normal basal, but low
stimulated ATPase activity, and abolishes
peptidase activity.
{ECO:0000269|PubMed:24520911}.
MUTAGEN 894 894 G->A,S: Enhances the basal, but not the
stimulated ATPase activity, and retains
peptidase activity.
{ECO:0000269|PubMed:24520911}.
MUTAGEN 894 894 G->P: Enhances the basal, but not the
stimulated ATPase activity, and abolishes
peptidase activity.
{ECO:0000269|PubMed:24520911}.
CONFLICT 1 55 MAASTGYVRLWGAARCWVLRRPMLAAAGGRVPTAAGAWLLR
GQRTCDASPPWALW -> MAGLWRRALATCDCGERRGAGCC
GGRCWPRRGAGSHCSRSVVAPRPADLRRLSSLGTV (in
Ref. 1; AAA61616). {ECO:0000305}.
CONFLICT 65 66 WR -> CG (in Ref. 1; AAA61616).
{ECO:0000305}.
CONFLICT 257 258 EL -> DV (in Ref. 1; AAA61616).
{ECO:0000305}.
CONFLICT 423 423 E -> G (in Ref. 4; BAG51690).
{ECO:0000305}.
CONFLICT 456 456 N -> D (in Ref. 1; AAA61616).
{ECO:0000305}.
CONFLICT 501 501 I -> V (in Ref. 4; BAG51690).
{ECO:0000305}.
CONFLICT 556 556 A -> T (in Ref. 1; AAA61616).
{ECO:0000305}.
CONFLICT 842 842 L -> P (in Ref. 1; AAA61616).
{ECO:0000305}.
CONFLICT 859 859 T -> A (in Ref. 1; AAA61616).
{ECO:0000305}.
STRAND 764 786 {ECO:0000244|PDB:2X36}.
STRAND 799 804 {ECO:0000244|PDB:2X36}.
HELIX 808 828 {ECO:0000244|PDB:2X36}.
HELIX 834 837 {ECO:0000244|PDB:2X36}.
STRAND 839 843 {ECO:0000244|PDB:2X36}.
TURN 850 852 {ECO:0000244|PDB:2X36}.
HELIX 853 856 {ECO:0000244|PDB:2X36}.
HELIX 857 869 {ECO:0000244|PDB:2X36}.
STRAND 877 879 {ECO:0000244|PDB:2X36}.
STRAND 887 890 {ECO:0000244|PDB:2X36}.
HELIX 895 904 {ECO:0000244|PDB:2X36}.
STRAND 909 913 {ECO:0000244|PDB:2X36}.
HELIX 914 916 {ECO:0000244|PDB:2X36}.
HELIX 917 921 {ECO:0000244|PDB:2X36}.
HELIX 925 928 {ECO:0000244|PDB:2X36}.
STRAND 932 938 {ECO:0000244|PDB:2X36}.
HELIX 939 946 {ECO:0000244|PDB:2X36}.
SEQUENCE 959 AA; 106489 MW; B5E03D9C27C220FF CRC64;
MAASTGYVRL WGAARCWVLR RPMLAAAGGR VPTAAGAWLL RGQRTCDASP PWALWGRGPA
IGGQWRGFWE ASSRGGGAFS GGEDASEGGA EEGAGGAGGS AGAGEGPVIT ALTPMTIPDV
FPHLPLIAIT RNPVFPRFIK IIEVKNKKLV ELLRRKVRLA QPYVGVFLKR DDSNESDVVE
SLDEIYHTGT FAQIHEMQDL GDKLRMIVMG HRRVHISRQL EVEPEEPEAE NKHKPRRKSK
RGKKEAEDEL SARHPAELAM EPTPELPAEV LMVEVENVVH EDFQVTEEVK ALTAEIVKTI
RDIIALNPLY RESVLQMMQA GQRVVDNPIY LSDMGAALTG AESHELQDVL EETNIPKRLY
KALSLLKKEF ELSKLQQRLG REVEEKIKQT HRKYLLQEQL KIIKKELGLE KDDKDAIEEK
FRERLKELVV PKHVMDVVDE ELSKLGLLDN HSSEFNVTRN YLDWLTSIPW GKYSNENLDL
ARAQAVLEED HYGMEDVKKR ILEFIAVSQL RGSTQGKILC FYGPPGVGKT SIARSIARAL
NREYFRFSVG GMTDVAEIKG HRRTYVGAMP GKIIQCLKKT KTENPLILID EVDKIGRGYQ
GDPSSALLEL LDPEQNANFL DHYLDVPVDL SKVLFICTAN VTDTIPEPLR DRMEMINVSG
YVAQEKLAIA ERYLVPQARA LCGLDESKAK LSSDVLTLLI KQYCRESGVR NLQKQVEKVL
RKSAYKIVSG EAESVEVTPE NLQDFVGKPV FTVERMYDVT PPGVVMGLAW TAMGGSTLFV
ETSLRRPQDK DAKGDKDGSL EVTGQLGEVM KESARIAYTF ARAFLMQHAP ANDYLVTSHI
HLHVPEGATP KDGPSAGCTI VTALLSLAMG RPVRQNLAMT GEVSLTGKIL PVGGIKEKTI
AAKRAGVTCI VLPAENKKDF YDLAAFITEG LEVHFVEHYR EIFDIAFPDE QAEALAVER


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