LONM_HUMAN
ID LONM_HUMAN Reviewed; 959 AA.
AC P36776; B3KPH8; D6W635; E5KMH8; F5GZ27; P36777; Q8N8K8; Q9UQ95;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 209.
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=LONHs;
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=8248235; DOI=10.1073/pnas.90.23.11247;
RA Wang N., Gottesman S., Willingham M.C., Gottesman M.M., Maurizi M.R.;
RT "A human mitochondrial ATP-dependent protease that is highly homologous to
RT bacterial Lon protease.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11247-11251(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-911.
RX PubMed=20843780; DOI=10.1093/nar/gkq750;
RA Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R.,
RA Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W., Mindrinos M.,
RA Speed T.P., Scharfe C.;
RT "Identification of rare DNA variants in mitochondrial disorders with
RT improved array-based sequencing.";
RL Nucleic Acids Res. 39:44-58(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Huang N.N., Maurizi M.R., Torres R.R., Polymeropoulos M.H., Lennon G.G.,
RA Gottesman M.M.;
RT "Chromosomal mapping and genomic organization of the ATP-dependent human
RT LON protease gene.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-959 (ISOFORM 1), AND VARIANT ILE-911.
RC TISSUE=Brain;
RX PubMed=8119403; DOI=10.1016/0014-5793(94)80166-5;
RA Amerik A.Y., Petukhova G.V., Grigorenko V.G., Lykov I.P., Yarovoi S.V.,
RA Lipkin V.M., Gorbalenya A.E.;
RT "Cloning and sequence analysis of cDNA for a human homolog of eubacterial
RT ATP-dependent Lon proteases.";
RL FEBS Lett. 340:25-28(1994).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=7961901; DOI=10.1016/s0021-9258(19)62045-4;
RA Wang N., Maurizi M.R., Emmert-Buck L., Gottesman M.M.;
RT "Synthesis, processing, and localization of human Lon protease.";
RL J. Biol. Chem. 269:29308-29313(1994).
RN [10]
RP DNA-BINDING.
RX PubMed=9485316; DOI=10.1021/bi970928c;
RA Fu G.K., Markovitz D.M.;
RT "The human LON protease binds to mitochondrial promoters in a single-
RT stranded, site-specific, strand-specific manner.";
RL Biochemistry 37:1905-1909(1998).
RN [11]
RP FUNCTION.
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).
RN [12]
RP DNA-BINDING, MUTAGENESIS OF SER-855, SUBUNIT, AND INTERACTION WITH TWNK AND
RP POLG.
RX PubMed=14739292; DOI=10.1074/jbc.m309642200;
RA Liu T., Lu B., Lee I., Ondrovicova G., Kutejova E., Suzuki C.K.;
RT "DNA and RNA binding by the mitochondrial lon protease is regulated by
RT nucleotide and protein substrate.";
RL J. Biol. Chem. 279:13902-13910(2004).
RN [13]
RP FUNCTION.
RX PubMed=15870080; DOI=10.1074/jbc.m502796200;
RA Ondrovicova G., Liu T., Singh K., Tian B., Li H., Gakh O., Perecko D.,
RA Janata J., Granot Z., Orly J., Kutejova E., Suzuki C.K.;
RT "Cleavage site selection within a folded substrate by the ATP-dependent lon
RT protease.";
RL J. Biol. Chem. 280:25103-25110(2005).
RN [14]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=17420247; DOI=10.1074/jbc.m611540200;
RA Lu B., Yadav S., Shah P.G., Liu T., Tian B., Pukszta S., Villaluna N.,
RA Kutejova E., Newlon C.S., Santos J.H., Suzuki C.K.;
RT "Roles for the human ATP-dependent Lon protease in mitochondrial DNA
RT maintenance.";
RL J. Biol. Chem. 282:17363-17374(2007).
RN [15]
RP SUBSTRATE.
RX PubMed=17579211; DOI=10.1210/me.2005-0458;
RA Granot Z., Kobiler O., Melamed-Book N., Eimerl S., Bahat A., Lu B.,
RA Braun S., Maurizi M.R., Suzuki C.K., Oppenheim A.B., Orly J.;
RT "Turnover of mitochondrial steroidogenic acute regulatory (StAR) protein by
RT Lon protease: the unexpected effect of proteasome inhibitors.";
RL Mol. Endocrinol. 21:2164-2177(2007).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP MUTAGENESIS OF LYS-529; TRP-770; THR-880 AND 893-GLY-GLY-894.
RX PubMed=24520911; DOI=10.1111/febs.12740;
RA Ambro L., Pevala V., Ondrovicova G., Bellova J., Kunova N., Kutejova E.,
RA Bauer J.;
RT "Mutations to a glycine loop in the catalytic site of human Lon changes its
RT protease, peptidase and ATPase activities.";
RL FEBS J. 281:1784-1797(2014).
RN [19]
RP SUBUNIT.
RX PubMed=25369343;
RA Kereiche S., Kovacik L., Pevala V., Ambro L., Bellova J., Kutejova E.,
RA Raska I.;
RT "Three-dimensional reconstruction of the S885A mutant of human
RT mitochondrial Lon protease.";
RL Folia Biol. (Praha) 60:62-65(2014).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP INVOLVEMENT IN CODASS, AND VARIANTS CODASS TYR-631; SER-676; GLY-721 AND
RP VAL-724.
RX PubMed=25574826; DOI=10.1016/j.ajhg.2014.12.003;
RA Strauss K.A., Jinks R.N., Puffenberger E.G., Venkatesh S., Singh K.,
RA Cheng I., Mikita N., Thilagavathi J., Lee J., Sarafianos S., Benkert A.,
RA Koehler A., Zhu A., Trovillion V., McGlincy M., Morlet T., Deardorff M.,
RA Innes A.M., Prasad C., Chudley A.E., Lee I.N., Suzuki C.K.;
RT "CODAS syndrome is associated with mutations of LONP1, encoding
RT mitochondrial AAA+ Lon protease.";
RL Am. J. Hum. Genet. 96:121-135(2015).
RN [22]
RP INVOLVEMENT IN CODASS, AND VARIANTS CODASS ALA-476; VAL-670; CYS-672;
RP HIS-679; SER-749; GLU-767 AND ILE-927 DEL.
RX PubMed=25808063; DOI=10.1002/ajmg.a.37029;
RA Dikoglu E., Alfaiz A., Gorna M., Bertola D., Chae J.H., Cho T.J.,
RA Derbent M., Alanay Y., Guran T., Kim O.H., Llerenar J.C. Jr., Yamamoto G.,
RA Superti-Furga G., Reymond A., Xenarios I., Stevenson B., Campos-Xavier B.,
RA Bonafe L., Superti-Furga A., Unger S.;
RT "Mutations in LONP1, a mitochondrial matrix protease, cause CODAS
RT syndrome.";
RL Am. J. Med. Genet. A 167:1501-1509(2015).
RN [23]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLY-67, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [24]
RP SUBSTRATE.
RX PubMed=28377575; DOI=10.1038/s41598-017-00632-8;
RA Kunova N., Ondrovicova G., Bauer J.A., Bellova J., Ambro L.,
RA Martinakova L., Kotrasova V., Kutejova E., Pevala V.;
RT "The role of Lon-mediated proteolysis in the dynamics of mitochondrial
RT nucleic acid-protein complexes.";
RL Sci. Rep. 7:631-631(2017).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 753-959, AND SUBUNIT.
RX PubMed=20222013; DOI=10.1002/pro.376;
RA Garcia-Nafria J., Ondrovicova G., Blagova E., Levdikov V.M., Bauer J.A.,
RA Suzuki C.K., Kutejova E., Wilkinson A.J., Wilson K.S.;
RT "Structure of the catalytic domain of the human mitochondrial Lon protease:
RT proposed relation of oligomer formation and activity.";
RL Protein Sci. 19:987-999(2010).
RN [26]
RP STRUCTURE BY ELECTRON MICROSCOPY (15 ANGSTROMS) OF MUTANT ALA-855, SUBUNIT,
RP AND DOMAIN.
RX PubMed=27632940; DOI=10.1038/srep33631;
RA Kereiche S., Kovacik L., Bednar J., Pevala V., Kunova N., Ondrovicova G.,
RA Bauer J., Ambro L., Bellova J., Kutejova E., Raska I.;
RT "The N-terminal domain plays a crucial role in the structure of a full-
RT length human mitochondrial Lon protease.";
RL Sci. Rep. 6:33631-33631(2016).
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 (PubMed:12198491, PubMed:15870080,
CC PubMed:17420247, PubMed:8248235). Endogenous substrates include
CC mitochondrial steroidogenic acute regulatory (StAR) protein, helicase
CC Twinkle (TWNK) and the large ribosomal subunit protein bL32m. bL32m is
CC protected from degradation by LONP1 when it is bound to a nucleic acid
CC (RNA), but TWNK is not (PubMed:17579211, PubMed:28377575).
CC {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:12198491,
CC ECO:0000269|PubMed:15870080, ECO:0000269|PubMed:17420247,
CC ECO:0000269|PubMed:17579211, ECO:0000269|PubMed:28377575,
CC ECO:0000269|PubMed:8248235}.
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 -!- ACTIVITY REGULATION: Peptidase activity is subject to substrate
CC inhibition by ATP. {ECO:0000269|PubMed:24520911}.
CC -!- SUBUNIT: Homohexamer (PubMed:14739292, PubMed:25369343,
CC PubMed:20222013). Organized in a ring with a central cavity
CC (PubMed:25369343, PubMed:20222013). The ATP-binding and proteolytic
CC domains (AP-domain) form a hexameric chamber, while the N-terminal
CC domain is arranged as a trimer of dimers (PubMed:27632940). DNA and RNA
CC binding is stimulated by substrate and inhibited by ATP binding.
CC Interacts with TWNK and mitochondrial DNA polymerase subunit POLG
CC (PubMed:14739292). {ECO:0000255|HAMAP-Rule:MF_03120,
CC ECO:0000269|PubMed:14739292, ECO:0000269|PubMed:20222013,
CC ECO:0000269|PubMed:25369343, ECO:0000269|PubMed:27632940}.
CC -!- INTERACTION:
CC P36776; P02666: CSN2; Xeno; NbExp=6; IntAct=EBI-357448, EBI-5260183;
CC P36776-1; P36776-1: LONP1; NbExp=3; IntAct=EBI-25473602, EBI-25473602;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03120, ECO:0000269|PubMed:7961901}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P36776-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P36776-2; Sequence=VSP_054617;
CC Name=3;
CC IsoId=P36776-3; Sequence=VSP_055310;
CC -!- TISSUE SPECIFICITY: Duodenum, heart, lung and liver, but not thymus.
CC -!- DOMAIN: The Lon N-terminal domains are crucial for the overall
CC structure of the protein, maintaining it in a conformation allowing its
CC proper functioning. {ECO:0000269|PubMed:27632940}.
CC -!- DOMAIN: The AP-domain (ATP-binding and proteolytic domains) has a
CC closed-ring conformation in the presence of AMP-PNP and its N-terminal
CC entry gate appears closed. Upon ADP binding, it switches to a lock-
CC washer conformation and its N-terminal gate opens.
CC {ECO:0000269|PubMed:27632940}.
CC -!- DOMAIN: The proteolytic site is connected to the ATP binding site
CC through the GG loop (Gly-893 and Gly-894) and the loop containing Trp-
CC 770. Binding of a protein substrate such as beta-casein appears to
CC trigger movement of both these loops as part of the conformational
CC changes which lead to enhanced ATPase and peptidase activities.
CC {ECO:0000305|PubMed:24520911}.
CC -!- DISEASE: CODAS syndrome (CODASS) [MIM:600373]: A rare syndrome
CC characterized by the combination of cerebral, ocular, dental,
CC auricular, and skeletal features. These include developmental delay,
CC craniofacial anomalies, cataracts, ptosis, median nasal groove, delayed
CC tooth eruption, hearing loss, short stature, delayed epiphyseal
CC ossification, metaphyseal hip dysplasia, and vertebral coronal clefts.
CC {ECO:0000269|PubMed:25574826, ECO:0000269|PubMed:25808063}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_03120}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA52291.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U02389; AAA61616.1; -; mRNA.
DR EMBL; HQ204946; ADP90374.1; -; Genomic_DNA.
DR EMBL; HQ204947; ADP90375.1; -; Genomic_DNA.
DR EMBL; HQ204948; ADP90376.1; -; Genomic_DNA.
DR EMBL; HQ204949; ADP90377.1; -; Genomic_DNA.
DR EMBL; HQ204950; ADP90378.1; -; Genomic_DNA.
DR EMBL; HQ204951; ADP90379.1; -; Genomic_DNA.
DR EMBL; HQ204952; ADP90380.1; -; Genomic_DNA.
DR EMBL; HQ204953; ADP90381.1; -; Genomic_DNA.
DR EMBL; HQ204954; ADP90382.1; -; Genomic_DNA.
DR EMBL; HQ204955; ADP90383.1; -; Genomic_DNA.
DR EMBL; HQ204956; ADP90384.1; -; Genomic_DNA.
DR EMBL; HQ204957; ADP90385.1; -; Genomic_DNA.
DR EMBL; HQ204958; ADP90386.1; -; Genomic_DNA.
DR EMBL; HQ204959; ADP90387.1; -; Genomic_DNA.
DR EMBL; HQ204960; ADP90388.1; -; Genomic_DNA.
DR EMBL; HQ204961; ADP90389.1; -; Genomic_DNA.
DR EMBL; HQ204962; ADP90390.1; -; Genomic_DNA.
DR EMBL; HQ204963; ADP90391.1; -; Genomic_DNA.
DR EMBL; HQ204964; ADP90392.1; -; Genomic_DNA.
DR EMBL; HQ204965; ADP90393.1; -; Genomic_DNA.
DR EMBL; HQ204966; ADP90394.1; -; Genomic_DNA.
DR EMBL; HQ204968; ADP90396.1; -; Genomic_DNA.
DR EMBL; HQ204969; ADP90397.1; -; Genomic_DNA.
DR EMBL; HQ204970; ADP90398.1; -; Genomic_DNA.
DR EMBL; HQ204971; ADP90399.1; -; Genomic_DNA.
DR EMBL; HQ204972; ADP90400.1; -; Genomic_DNA.
DR EMBL; HQ204973; ADP90401.1; -; Genomic_DNA.
DR EMBL; HQ204974; ADP90402.1; -; Genomic_DNA.
DR EMBL; HQ204975; ADP90403.1; -; Genomic_DNA.
DR EMBL; HQ204976; ADP90404.1; -; Genomic_DNA.
DR EMBL; HQ204977; ADP90405.1; -; Genomic_DNA.
DR EMBL; HQ204978; ADP90406.1; -; Genomic_DNA.
DR EMBL; HQ204979; ADP90407.1; -; Genomic_DNA.
DR EMBL; HQ204980; ADP90408.1; -; Genomic_DNA.
DR EMBL; HQ204981; ADP90409.1; -; Genomic_DNA.
DR EMBL; HQ204982; ADP90410.1; -; Genomic_DNA.
DR EMBL; HQ204983; ADP90411.1; -; Genomic_DNA.
DR EMBL; HQ204984; ADP90412.1; -; Genomic_DNA.
DR EMBL; HQ204985; ADP90413.1; -; Genomic_DNA.
DR EMBL; AF059309; AAD24414.1; -; Genomic_DNA.
DR EMBL; AF059296; AAD24414.1; JOINED; Genomic_DNA.
DR EMBL; AF059297; AAD24414.1; JOINED; Genomic_DNA.
DR EMBL; AF059298; AAD24414.1; JOINED; Genomic_DNA.
DR EMBL; AF059299; AAD24414.1; JOINED; Genomic_DNA.
DR EMBL; AF059300; AAD24414.1; JOINED; Genomic_DNA.
DR EMBL; AF059301; AAD24414.1; JOINED; Genomic_DNA.
DR EMBL; AF059302; AAD24414.1; JOINED; Genomic_DNA.
DR EMBL; AF059303; AAD24414.1; JOINED; Genomic_DNA.
DR EMBL; AF059304; AAD24414.1; JOINED; Genomic_DNA.
DR EMBL; AF059305; AAD24414.1; JOINED; Genomic_DNA.
DR EMBL; AF059306; AAD24414.1; JOINED; Genomic_DNA.
DR EMBL; AF059307; AAD24414.1; JOINED; Genomic_DNA.
DR EMBL; AF059308; AAD24414.1; JOINED; Genomic_DNA.
DR EMBL; AK056366; BAG51690.1; -; mRNA.
DR EMBL; AK096626; BAC04829.1; -; mRNA.
DR EMBL; AC011499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471139; EAW69151.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69154.1; -; Genomic_DNA.
DR EMBL; BC000235; AAH00235.1; -; mRNA.
DR EMBL; X74215; CAA52291.1; ALT_INIT; mRNA.
DR EMBL; X76040; CAA53625.1; -; mRNA.
DR CCDS; CCDS12148.1; -. [P36776-1]
DR CCDS; CCDS62507.1; -. [P36776-3]
DR CCDS; CCDS62508.1; -. [P36776-2]
DR PIR; S42366; S42366.
DR PIR; S57342; S57342.
DR RefSeq; NP_001263408.1; NM_001276479.1. [P36776-2]
DR RefSeq; NP_001263409.1; NM_001276480.1. [P36776-3]
DR RefSeq; NP_004784.2; NM_004793.3. [P36776-1]
DR PDB; 2X36; X-ray; 2.00 A; A/B/C/D/E/F=753-959.
DR PDB; 6WYS; X-ray; 2.23 A; A/B/C=754-959.
DR PDB; 6WZV; X-ray; 2.51 A; A/B/C=754-959.
DR PDB; 6X1M; X-ray; 3.51 A; A/B/C=754-959.
DR PDB; 6X27; X-ray; 2.12 A; A/B/C/D/E/F/G/H/I/J/K/L=754-959.
DR PDB; 7KRZ; EM; 3.20 A; A/B/C/D/E/F=414-947.
DR PDB; 7KSL; EM; 3.40 A; A/B/C/E/F=421-947.
DR PDB; 7KSM; EM; 3.20 A; A/B/C/D/E/F=416-947.
DR PDB; 7NFY; EM; 3.90 A; A/B/C/D/E/F=115-959.
DR PDB; 7NG4; EM; 4.40 A; A/B/C/D/E/F=115-959.
DR PDB; 7NG5; EM; 3.80 A; A/B/C/D/E/F=115-959.
DR PDB; 7NGC; EM; 7.50 A; A/B/C/D/E/F=123-948.
DR PDB; 7NGF; EM; 5.60 A; A/B/C/D/E/F=123-948.
DR PDB; 7NGL; EM; 3.80 A; A/B/C/D/E/F=123-948.
DR PDB; 7NGP; EM; 15.00 A; A/B/C/D/E/F=123-948.
DR PDB; 7NGQ; EM; 12.00 A; A/B/C/D/E/F=123-948.
DR PDB; 7OXO; EM; 3.90 A; A/B/C/D/E/F=1-959.
DR PDB; 7P09; EM; 2.70 A; A/B/C/D/E/F=67-949.
DR PDB; 7P0B; EM; 4.00 A; A/B/C/D/E/F=67-949.
DR PDB; 7P0M; EM; 2.75 A; A/B/C/D/E/F=67-959.
DR PDBsum; 2X36; -.
DR PDBsum; 6WYS; -.
DR PDBsum; 6WZV; -.
DR PDBsum; 6X1M; -.
DR PDBsum; 6X27; -.
DR PDBsum; 7KRZ; -.
DR PDBsum; 7KSL; -.
DR PDBsum; 7KSM; -.
DR PDBsum; 7NFY; -.
DR PDBsum; 7NG4; -.
DR PDBsum; 7NG5; -.
DR PDBsum; 7NGC; -.
DR PDBsum; 7NGF; -.
DR PDBsum; 7NGL; -.
DR PDBsum; 7NGP; -.
DR PDBsum; 7NGQ; -.
DR PDBsum; 7OXO; -.
DR PDBsum; 7P09; -.
DR PDBsum; 7P0B; -.
DR PDBsum; 7P0M; -.
DR AlphaFoldDB; P36776; -.
DR SMR; P36776; -.
DR BioGRID; 114762; 426.
DR IntAct; P36776; 102.
DR MINT; P36776; -.
DR STRING; 9606.ENSP00000353826; -.
DR GuidetoPHARMACOLOGY; 3180; -.
DR MEROPS; S16.002; -.
DR MoonDB; P36776; Curated.
DR GlyGen; P36776; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P36776; -.
DR MetOSite; P36776; -.
DR PhosphoSitePlus; P36776; -.
DR SwissPalm; P36776; -.
DR BioMuta; LONP1; -.
DR DMDM; 12644239; -.
DR EPD; P36776; -.
DR jPOST; P36776; -.
DR MassIVE; P36776; -.
DR MaxQB; P36776; -.
DR PaxDb; P36776; -.
DR PeptideAtlas; P36776; -.
DR PRIDE; P36776; -.
DR ProteomicsDB; 24918; -.
DR ProteomicsDB; 55221; -. [P36776-1]
DR Antibodypedia; 811; 305 antibodies from 29 providers.
DR DNASU; 9361; -.
DR Ensembl; ENST00000360614.8; ENSP00000353826.2; ENSG00000196365.12. [P36776-1]
DR Ensembl; ENST00000540670.6; ENSP00000441523.1; ENSG00000196365.12. [P36776-3]
DR Ensembl; ENST00000593119.5; ENSP00000468541.1; ENSG00000196365.12. [P36776-2]
DR GeneID; 9361; -.
DR KEGG; hsa:9361; -.
DR MANE-Select; ENST00000360614.8; ENSP00000353826.2; NM_004793.4; NP_004784.2.
DR UCSC; uc002mcx.5; human. [P36776-1]
DR CTD; 9361; -.
DR DisGeNET; 9361; -.
DR GeneCards; LONP1; -.
DR HGNC; HGNC:9479; LONP1.
DR HPA; ENSG00000196365; Tissue enhanced (adrenal).
DR MalaCards; LONP1; -.
DR MIM; 600373; phenotype.
DR MIM; 605490; gene.
DR neXtProt; NX_P36776; -.
DR OpenTargets; ENSG00000196365; -.
DR Orphanet; 1458; CODAS syndrome.
DR Orphanet; 2140; Congenital diaphragmatic hernia.
DR Orphanet; 79243; Pyruvate dehydrogenase E1-alpha deficiency.
DR PharmGKB; PA162394145; -.
DR VEuPathDB; HostDB:ENSG00000196365; -.
DR eggNOG; KOG2004; Eukaryota.
DR GeneTree; ENSGT00530000063553; -.
DR HOGENOM; CLU_004109_1_1_1; -.
DR InParanoid; P36776; -.
DR OMA; YVGPPIY; -.
DR OrthoDB; 528132at2759; -.
DR PhylomeDB; P36776; -.
DR TreeFam; TF105001; -.
DR BRENDA; 3.4.21.53; 2681.
DR PathwayCommons; P36776; -.
DR SignaLink; P36776; -.
DR SIGNOR; P36776; -.
DR BioGRID-ORCS; 9361; 779 hits in 1077 CRISPR screens.
DR ChiTaRS; LONP1; human.
DR EvolutionaryTrace; P36776; -.
DR GeneWiki; LONP1; -.
DR GenomeRNAi; 9361; -.
DR Pharos; P36776; Tbio.
DR PRO; PR:P36776; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P36776; protein.
DR Bgee; ENSG00000196365; Expressed in right adrenal gland and 191 other tissues.
DR ExpressionAtlas; P36776; baseline and differential.
DR Genevisible; P36776; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IMP:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0043531; F:ADP binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:UniProtKB.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IDA:UniProtKB.
DR GO; GO:0070182; F:DNA polymerase binding; IPI:UniProtKB.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0001018; F:mitochondrial promoter sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
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:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:UniProtKB.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR GO; GO:0032042; P:mitochondrial DNA metabolic process; NAS:UniProtKB.
DR GO; GO:0000002; P:mitochondrial genome maintenance; NAS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR GO; GO:0070407; P:oxidation-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IDA:UniProtKB.
DR GO; GO:0010044; P:response to aluminum ion; IEA:Ensembl.
DR GO; GO:0009725; P:response to hormone; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEP:UniProtKB.
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 3D-structure; Alternative splicing; ATP-binding; Cataract; Deafness;
KW Disease variant; DNA-binding; Dwarfism; Hydrolase; Mitochondrion;
KW Nucleotide-binding; Protease; Reference proteome; Serine protease;
KW Transit peptide.
FT TRANSIT 1..67
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 68..959
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000026734"
FT DOMAIN 124..368
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 759..949
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 77..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 855
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 898
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 523..530
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT VAR_SEQ 1..196
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055310"
FT VAR_SEQ 42..105
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054617"
FT VARIANT 87
FT /note="E -> D (in dbSNP:rs34413649)"
FT /id="VAR_051564"
FT VARIANT 241
FT /note="R -> Q (in dbSNP:rs11085147)"
FT /id="VAR_051565"
FT VARIANT 476
FT /note="E -> A (in CODASS)"
FT /evidence="ECO:0000269|PubMed:25808063"
FT /id="VAR_073338"
FT VARIANT 631
FT /note="S -> Y (in CODASS; dbSNP:rs879255248)"
FT /evidence="ECO:0000269|PubMed:25574826"
FT /id="VAR_073339"
FT VARIANT 670
FT /note="A -> V (in CODASS; dbSNP:rs770036526)"
FT /evidence="ECO:0000269|PubMed:25808063"
FT /id="VAR_073340"
FT VARIANT 672
FT /note="R -> C (in CODASS; dbSNP:rs777009012)"
FT /evidence="ECO:0000269|PubMed:25808063"
FT /id="VAR_073341"
FT VARIANT 676
FT /note="P -> S (in CODASS; dbSNP:rs879255247)"
FT /evidence="ECO:0000269|PubMed:25574826"
FT /id="VAR_073342"
FT VARIANT 679
FT /note="R -> H (in CODASS; dbSNP:rs549574673)"
FT /evidence="ECO:0000269|PubMed:25808063"
FT /id="VAR_073343"
FT VARIANT 721
FT /note="R -> G (in CODASS; dbSNP:rs147588238)"
FT /evidence="ECO:0000269|PubMed:25574826"
FT /id="VAR_073344"
FT VARIANT 724
FT /note="A -> V (in CODASS; dbSNP:rs879255249)"
FT /evidence="ECO:0000269|PubMed:25574826"
FT /id="VAR_073345"
FT VARIANT 749
FT /note="P -> S (in CODASS)"
FT /evidence="ECO:0000269|PubMed:25808063"
FT /id="VAR_073346"
FT VARIANT 767
FT /note="G -> E (in CODASS; dbSNP:rs562553348)"
FT /evidence="ECO:0000269|PubMed:25808063"
FT /id="VAR_073347"
FT VARIANT 829
FT /note="A -> T (in dbSNP:rs35804229)"
FT /id="VAR_067708"
FT VARIANT 911
FT /note="V -> I (in dbSNP:rs1062373)"
FT /evidence="ECO:0000269|PubMed:20843780,
FT ECO:0000269|PubMed:8119403"
FT /id="VAR_067709"
FT VARIANT 927
FT /note="Missing (in CODASS)"
FT /evidence="ECO:0000269|PubMed:25808063"
FT /id="VAR_073348"
FT MUTAGEN 529
FT /note="K->R: Abolishes ATPase activity, and presumably ATP-
FT driven protein unfolding, but does not block access to the
FT proteolytic active site or prevent a substrate from binding
FT to it."
FT /evidence="ECO:0000269|PubMed:24520911"
FT MUTAGEN 770
FT /note="W->A: Has low basal, but normal stimulated ATPase
FT activity, and retains peptidase activity."
FT /evidence="ECO:0000269|PubMed:24520911"
FT MUTAGEN 770
FT /note="W->P: Has normal basal, but low stimulated ATPase
FT activity, and abolishes peptidase activity."
FT /evidence="ECO:0000269|PubMed:24520911"
FT MUTAGEN 855
FT /note="S->A: Lacks both ATPase and protease activity, but
FT retains DNA binding activity."
FT /evidence="ECO:0000269|PubMed:14739292,
FT ECO:0000269|PubMed:24520911"
FT MUTAGEN 880
FT /note="T->V: Enhances the basal, but not the stimulated
FT ATPase activity."
FT /evidence="ECO:0000269|PubMed:24520911"
FT MUTAGEN 893
FT /note="G->A: Has low basal, but normal stimulated ATPase
FT activity, and retains peptidase activity."
FT /evidence="ECO:0000269|PubMed:24520911"
FT MUTAGEN 893
FT /note="G->P: Has normal basal, but low stimulated ATPase
FT activity, and abolishes peptidase activity."
FT /evidence="ECO:0000269|PubMed:24520911"
FT MUTAGEN 894
FT /note="G->A,S: Enhances the basal, but not the stimulated
FT ATPase activity, and retains peptidase activity."
FT /evidence="ECO:0000269|PubMed:24520911"
FT MUTAGEN 894
FT /note="G->P: Enhances the basal, but not the stimulated
FT ATPase activity, and abolishes peptidase activity."
FT /evidence="ECO:0000269|PubMed:24520911"
FT CONFLICT 1..55
FT /note="MAASTGYVRLWGAARCWVLRRPMLAAAGGRVPTAAGAWLLRGQRTCDASPPW
FT ALW -> MAGLWRRALATCDCGERRGAGCCGGRCWPRRGAGSHCSRSVVAPRPADLRRL
FT SSLGTV (in Ref. 1; AAA61616)"
FT /evidence="ECO:0000305"
FT CONFLICT 65..66
FT /note="WR -> CG (in Ref. 1; AAA61616)"
FT /evidence="ECO:0000305"
FT CONFLICT 257..258
FT /note="EL -> DV (in Ref. 1; AAA61616)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="E -> G (in Ref. 4; BAG51690)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="N -> D (in Ref. 1; AAA61616)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="I -> V (in Ref. 4; BAG51690)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="A -> T (in Ref. 1; AAA61616)"
FT /evidence="ECO:0000305"
FT CONFLICT 842
FT /note="L -> P (in Ref. 1; AAA61616)"
FT /evidence="ECO:0000305"
FT CONFLICT 859
FT /note="T -> A (in Ref. 1; AAA61616)"
FT /evidence="ECO:0000305"
FT HELIX 413..427
FT /evidence="ECO:0007829|PDB:7P09"
FT HELIX 432..447
FT /evidence="ECO:0007829|PDB:7P09"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:7KSL"
FT HELIX 453..467
FT /evidence="ECO:0007829|PDB:7P09"
FT HELIX 480..490
FT /evidence="ECO:0007829|PDB:7P09"
FT HELIX 495..511
FT /evidence="ECO:0007829|PDB:7P09"
FT STRAND 518..522
FT /evidence="ECO:0007829|PDB:7P09"
FT STRAND 524..528
FT /evidence="ECO:0007829|PDB:7KSL"
FT HELIX 529..540
FT /evidence="ECO:0007829|PDB:7P09"
FT STRAND 544..548
FT /evidence="ECO:0007829|PDB:7P09"
FT HELIX 556..559
FT /evidence="ECO:0007829|PDB:7P09"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:7KSL"
FT HELIX 572..580
FT /evidence="ECO:0007829|PDB:7P09"
FT STRAND 582..584
FT /evidence="ECO:0007829|PDB:7KRZ"
FT STRAND 586..590
FT /evidence="ECO:0007829|PDB:7P09"
FT HELIX 592..594
FT /evidence="ECO:0007829|PDB:7P09"
FT STRAND 599..601
FT /evidence="ECO:0007829|PDB:7P09"
FT HELIX 603..611
FT /evidence="ECO:0007829|PDB:7P09"
FT HELIX 613..616
FT /evidence="ECO:0007829|PDB:7P09"
FT STRAND 617..619
FT /evidence="ECO:0007829|PDB:7P09"
FT TURN 622..624
FT /evidence="ECO:0007829|PDB:7P0M"
FT STRAND 626..628
FT /evidence="ECO:0007829|PDB:7P0M"
FT STRAND 634..640
FT /evidence="ECO:0007829|PDB:7P09"
FT HELIX 642..644
FT /evidence="ECO:0007829|PDB:7KRZ"
FT HELIX 647..651
FT /evidence="ECO:0007829|PDB:7P09"
FT STRAND 653..657
FT /evidence="ECO:0007829|PDB:7P09"
FT HELIX 663..672
FT /evidence="ECO:0007829|PDB:7P09"
FT HELIX 674..682
FT /evidence="ECO:0007829|PDB:7P09"
FT TURN 686..688
FT /evidence="ECO:0007829|PDB:7P09"
FT HELIX 693..702
FT /evidence="ECO:0007829|PDB:7P09"
FT STRAND 706..709
FT /evidence="ECO:0007829|PDB:7P09"
FT HELIX 712..728
FT /evidence="ECO:0007829|PDB:7P09"
FT STRAND 733..736
FT /evidence="ECO:0007829|PDB:7P09"
FT HELIX 739..741
FT /evidence="ECO:0007829|PDB:7P09"
FT HELIX 742..746
FT /evidence="ECO:0007829|PDB:7P09"
FT STRAND 750..753
FT /evidence="ECO:0007829|PDB:7KSL"
FT STRAND 756..759
FT /evidence="ECO:0007829|PDB:7KSL"
FT STRAND 764..786
FT /evidence="ECO:0007829|PDB:2X36"
FT STRAND 799..804
FT /evidence="ECO:0007829|PDB:2X36"
FT HELIX 808..828
FT /evidence="ECO:0007829|PDB:2X36"
FT HELIX 834..837
FT /evidence="ECO:0007829|PDB:2X36"
FT STRAND 839..843
FT /evidence="ECO:0007829|PDB:2X36"
FT TURN 850..852
FT /evidence="ECO:0007829|PDB:2X36"
FT HELIX 853..856
FT /evidence="ECO:0007829|PDB:2X36"
FT HELIX 857..869
FT /evidence="ECO:0007829|PDB:2X36"
FT STRAND 877..879
FT /evidence="ECO:0007829|PDB:2X36"
FT STRAND 887..890
FT /evidence="ECO:0007829|PDB:2X36"
FT HELIX 895..904
FT /evidence="ECO:0007829|PDB:2X36"
FT STRAND 909..913
FT /evidence="ECO:0007829|PDB:2X36"
FT HELIX 914..916
FT /evidence="ECO:0007829|PDB:2X36"
FT HELIX 917..921
FT /evidence="ECO:0007829|PDB:2X36"
FT HELIX 925..928
FT /evidence="ECO:0007829|PDB:2X36"
FT STRAND 932..938
FT /evidence="ECO:0007829|PDB:2X36"
FT HELIX 939..946
FT /evidence="ECO:0007829|PDB:2X36"
FT HELIX 948..951
FT /evidence="ECO:0007829|PDB:6WZV"
FT HELIX 952..956
FT /evidence="ECO:0007829|PDB:6X27"
SQ 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
