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 27-MAR-2024, entry version 218. 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), FUNCTION, AND TISSUE SPECIFICITY. 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, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-855, SUBUNIT, RP AND INTERACTION WITH TWNK AND 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, CATALYTIC ACTIVITY, 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 FUNCTION. 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; SER-855; THR-880; GLY-893 AND 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 FUNCTION. 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 FUNCTION. RX PubMed=37327776; DOI=10.1016/j.molcel.2023.05.031; RA Sekine Y., Houston R., Eckl E.M., Fessler E., Narendra D.P., Jae L.T., RA Sekine S.; RT "A mitochondrial iron-responsive pathway regulated by DELE1."; RL Mol. Cell 83:2059-2076(2023). RN [26] 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 [27] 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 (PubMed:12198491, PubMed:15870080, PubMed:8248235, CC PubMed:17579211, PubMed:37327776). Endogenous substrates include CC mitochondrial steroidogenic acute regulatory (StAR) protein, DELE1, CC helicase Twinkle (TWNK) and the large ribosomal subunit protein CC MRPL32/bL32m (PubMed:17579211, PubMed:28377575, PubMed:37327776). CC MRPL32/bL32m is protected from degradation by LONP1 when it is bound to CC a nucleic acid (RNA), but TWNK is not (PubMed:17579211, CC PubMed:28377575). May also have a chaperone function in the assembly of CC inner membrane protein complexes (By similarity). Participates in the CC regulation of mitochondrial gene expression and in the maintenance of CC the integrity of the mitochondrial genome (PubMed:17420247). Binds to CC mitochondrial promoters and RNA in a single-stranded, site-specific, CC and strand-specific manner (PubMed:17420247). May regulate CC mitochondrial DNA replication and/or gene expression using site- CC specific, single-stranded DNA binding to target the degradation of CC regulatory proteins binding to adjacent sites in mitochondrial CC promoters (PubMed:14739292, PubMed:17420247). {ECO:0000255|HAMAP- CC Rule:MF_03120, ECO:0000269|PubMed:12198491, CC ECO:0000269|PubMed:14739292, ECO:0000269|PubMed:15870080, CC ECO:0000269|PubMed:17420247, ECO:0000269|PubMed:17579211, CC ECO:0000269|PubMed:28377575, ECO:0000269|PubMed:37327776, 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 ECO:0000269|PubMed:14739292, ECO:0000269|PubMed:17420247}; 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 {ECO:0000269|PubMed:8248235}. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-12306; -. DR EMDB; EMD-12307; -. DR EMDB; EMD-12308; -. DR EMDB; EMD-12312; -. DR EMDB; EMD-12313; -. DR EMDB; EMD-12315; -. DR EMDB; EMD-12316; -. DR EMDB; EMD-12317; -. DR EMDB; EMD-13102; -. DR EMDB; EMD-13146; -. DR EMDB; EMD-13147; -. DR EMDB; EMD-13148; -. DR EMDB; EMD-23013; -. DR EMDB; EMD-23019; -. DR EMDB; EMD-23020; -. DR EMDB; EMD-23320; -. DR EMDB; EMD-3274; -. DR EMDB; EMD-3275; -. DR SMR; P36776; -. DR BioGRID; 114762; 495. DR IntAct; P36776; 110. DR MINT; P36776; -. DR STRING; 9606.ENSP00000353826; -. DR BindingDB; P36776; -. DR ChEMBL; CHEMBL4879436; -. 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; 9606-ENSP00000353826; -. DR PeptideAtlas; P36776; -. DR ProteomicsDB; 24918; -. DR ProteomicsDB; 55221; -. [P36776-1] DR Pumba; P36776; -. DR Antibodypedia; 811; 337 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 AGR; HGNC:9479; -. 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; 1103874at2759; -. 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; 817 hits in 1165 CRISPR screens. DR ChiTaRS; LONP1; human. DR EvolutionaryTrace; P36776; -. DR GeneWiki; LONP1; -. DR GenomeRNAi; 9361; -. DR Pharos; P36776; Tchem. DR PRO; PR:P36776; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P36776; Protein. DR Bgee; ENSG00000196365; Expressed in right adrenal gland and 193 other cell types or tissues. DR ExpressionAtlas; P36776; baseline and differential. 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:HPA. 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; IEA:UniProtKB-UniRule. 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:0043560; F:insulin receptor substrate binding; IEA:Ensembl. DR GO; GO:0042731; F:PH domain binding; IEA:Ensembl. 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: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:0046627; P:negative regulation of insulin receptor signaling pathway; IEA:Ensembl. DR GO; GO:0070407; P:oxidation-dependent protein catabolic process; IMP:UniProtKB. DR GO; GO:0030163; P:protein catabolic process; IDA: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:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl. 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 CDD; cd19500; RecA-like_Lon; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 1.20.5.5270; -; 1. DR Gene3D; 1.20.58.1480; -; 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_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_Su5_D2-typ_SF. DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr. DR NCBIfam; TIGR00763; lon; 1. DR PANTHER; PTHR43718; LON PROTEASE; 1. DR PANTHER; PTHR43718:SF2; LON PROTEASE HOMOLOG, MITOCHONDRIAL; 1. DR Pfam; PF00004; AAA; 1. DR Pfam; PF05362; Lon_C; 1. DR Pfam; PF02190; LON_substr_bdg; 1. 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. DR Genevisible; P36776; HS. 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..370 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 FT ATP-driven protein unfolding, but does not block access to FT the proteolytic active site or prevent a substrate from FT binding 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 //