ID   NDUV1_MOUSE             Reviewed;         464 AA.
AC   Q91YT0;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;
DE            Short=NDUFV1 {ECO:0000303|PubMed:29915388};
DE            EC=7.1.1.2 {ECO:0000269|PubMed:29915388};
DE   AltName: Full=Complex I-51kD;
DE            Short=CI-51kD;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 51 kDa subunit {ECO:0000250|UniProtKB:P49821};
DE   Flags: Precursor;
GN   Name=Ndufv1 {ECO:0000312|MGI:MGI:107851};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
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   [3]
RP   PROTEIN SEQUENCE OF 21-29.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=10870971;
RX   DOI=10.1002/(sici)1522-2683(20000501)21:9<1853::aid-elps1853>3.0.co;2-y;
RA   Tsugita A., Kawakami T., Uchida T., Sakai T., Kamo M., Matsui T.,
RA   Watanabe Y., Morimasa T., Hosokawa K., Toda T.;
RT   "Proteome analysis of mouse brain: two-dimensional electrophoresis profiles
RT   of tissue proteins during the course of aging.";
RL   Electrophoresis 21:1853-1871(2000).
RN   [4]
RP   PROTEIN SEQUENCE OF 29-48; 72-81; 89-126; 138-147; 153-219; 258-267;
RP   275-297; 303-329; 370-375; 387-394 AND 402-449, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-81, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81; LYS-104 AND LYS-375, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN   [8]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-257, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [9]
RP   INTERACTION WITH RAB5IF.
RX   PubMed=31536960; DOI=10.1016/j.isci.2019.08.057;
RA   Moutaoufik M.T., Malty R., Amin S., Zhang Q., Phanse S., Gagarinova A.,
RA   Zilocchi M., Hoell L., Minic Z., Gagarinova M., Aoki H., Stockwell J.,
RA   Jessulat M., Goebels F., Broderick K., Scott N.E., Vlasblom J., Musso G.,
RA   Prasad B., Lamantea E., Garavaglia B., Rajput A., Murayama K., Okazaki Y.,
RA   Foster L.J., Bader G.D., Cayabyab F.S., Babu M.;
RT   "Rewiring of the Human Mitochondrial Interactome during Neuronal
RT   Reprogramming Reveals Regulators of the Respirasome and Neurogenesis.";
RL   IScience 19:1114-1132(2019).
RN   [10] {ECO:0007744|PDB:6G2J, ECO:0007744|PDB:6G72}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 30-457, FUNCTION,
RP   CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RX   PubMed=29915388; DOI=10.1038/s41594-018-0073-1;
RA   Agip A.A., Blaza J.N., Bridges H.R., Viscomi C., Rawson S., Muench S.P.,
RA   Hirst J.;
RT   "Cryo-EM structures of complex I from mouse heart mitochondria in two
RT   biochemically defined states.";
RL   Nat. Struct. Mol. Biol. 25:548-556(2018).
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC       NADH dehydrogenase (Complex I) which catalyzes electron transfer from
CC       NADH through the respiratory chain, using ubiquinone as an electron
CC       acceptor. Part of the peripheral arm of the enzyme, where the electrons
CC       from NADH are accepted by flavin mononucleotide (FMN) and then passed
CC       along a chain of iron-sulfur clusters by electron tunnelling to the
CC       final acceptor ubiquinone. Contains FMN, which is the initial electron
CC       acceptor as well as one iron-sulfur cluster.
CC       {ECO:0000269|PubMed:29915388}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC         COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC         Evidence={ECO:0000305|PubMed:29915388};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29092;
CC         Evidence={ECO:0000305|PubMed:29915388};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:29915388};
CC       Note=Binds 1 FMN. {ECO:0000269|PubMed:29915388};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000269|PubMed:29915388};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:29915388};
CC   -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC       I) which is composed of 45 different subunits (PubMed:29915388). This
CC       is a component of the flavoprotein-sulfur (FP) fragment of the enzyme
CC       (PubMed:29915388). Interacts with RAB5IF (PubMed:31536960).
CC       {ECO:0000269|PubMed:29915388, ECO:0000269|PubMed:31536960}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P25708}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P25708}; Matrix side
CC       {ECO:0000250|UniProtKB:P25708}.
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AK075692; BAC35893.1; -; mRNA.
DR   EMBL; BC014818; AAH14818.1; -; mRNA.
DR   EMBL; BC041682; AAH41682.1; -; mRNA.
DR   CCDS; CCDS29410.1; -.
DR   PIR; PC7078; PC7078.
DR   RefSeq; NP_598427.1; NM_133666.3.
DR   PDB; 6G2J; EM; 3.30 A; F=30-457.
DR   PDB; 6G72; EM; 3.90 A; F=1-464.
DR   PDB; 6ZR2; EM; 3.10 A; F=1-464.
DR   PDB; 6ZTQ; EM; 3.00 A; F=1-464.
DR   PDB; 7AK5; EM; 3.17 A; F=1-464.
DR   PDB; 7AK6; EM; 3.82 A; F=1-464.
DR   PDB; 7B93; EM; 3.04 A; F=1-464.
DR   PDB; 7PSA; EM; 3.40 A; F=1-464.
DR   PDB; 8OLT; EM; 2.84 A; F=1-464.
DR   PDB; 8OM1; EM; 2.39 A; F=1-464.
DR   PDBsum; 6G2J; -.
DR   PDBsum; 6G72; -.
DR   PDBsum; 6ZR2; -.
DR   PDBsum; 6ZTQ; -.
DR   PDBsum; 7AK5; -.
DR   PDBsum; 7AK6; -.
DR   PDBsum; 7B93; -.
DR   PDBsum; 7PSA; -.
DR   PDBsum; 8OLT; -.
DR   PDBsum; 8OM1; -.
DR   AlphaFoldDB; Q91YT0; -.
DR   EMDB; EMD-11377; -.
DR   EMDB; EMD-11424; -.
DR   EMDB; EMD-11810; -.
DR   EMDB; EMD-11811; -.
DR   EMDB; EMD-12095; -.
DR   EMDB; EMD-13611; -.
DR   EMDB; EMD-16962; -.
DR   EMDB; EMD-16965; -.
DR   EMDB; EMD-4345; -.
DR   EMDB; EMD-4356; -.
DR   SMR; Q91YT0; -.
DR   BioGRID; 201719; 71.
DR   ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR   CORUM; Q91YT0; -.
DR   IntAct; Q91YT0; 7.
DR   MINT; Q91YT0; -.
DR   STRING; 10090.ENSMUSP00000042967; -.
DR   GlyGen; Q91YT0; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q91YT0; -.
DR   PhosphoSitePlus; Q91YT0; -.
DR   SwissPalm; Q91YT0; -.
DR   EPD; Q91YT0; -.
DR   jPOST; Q91YT0; -.
DR   MaxQB; Q91YT0; -.
DR   PaxDb; 10090-ENSMUSP00000042967; -.
DR   PeptideAtlas; Q91YT0; -.
DR   ProteomicsDB; 287471; -.
DR   Pumba; Q91YT0; -.
DR   Antibodypedia; 30465; 295 antibodies from 30 providers.
DR   DNASU; 17995; -.
DR   Ensembl; ENSMUST00000042497.14; ENSMUSP00000042967.8; ENSMUSG00000037916.15.
DR   GeneID; 17995; -.
DR   KEGG; mmu:17995; -.
DR   UCSC; uc008fye.2; mouse.
DR   AGR; MGI:107851; -.
DR   CTD; 4723; -.
DR   MGI; MGI:107851; Ndufv1.
DR   VEuPathDB; HostDB:ENSMUSG00000037916; -.
DR   eggNOG; KOG2658; Eukaryota.
DR   GeneTree; ENSGT00390000010641; -.
DR   HOGENOM; CLU_014881_1_0_1; -.
DR   InParanoid; Q91YT0; -.
DR   OMA; KWQFIPQ; -.
DR   OrthoDB; 5483539at2759; -.
DR   PhylomeDB; Q91YT0; -.
DR   TreeFam; TF300381; -.
DR   Reactome; R-MMU-611105; Respiratory electron transport.
DR   Reactome; R-MMU-6799198; Complex I biogenesis.
DR   BioGRID-ORCS; 17995; 23 hits in 64 CRISPR screens.
DR   ChiTaRS; Ndufv1; mouse.
DR   PRO; PR:Q91YT0; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q91YT0; Protein.
DR   Bgee; ENSMUSG00000037916; Expressed in soleus muscle and 271 other cell types or tissues.
DR   ExpressionAtlas; Q91YT0; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IDA:UniProtKB.
DR   GO; GO:0009060; P:aerobic respiration; NAS:ComplexPortal.
DR   GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; ISO:MGI.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IDA:UniProtKB.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; NAS:ComplexPortal.
DR   Gene3D; 3.10.20.600; -; 1.
DR   Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 1.
DR   Gene3D; 1.20.1440.230; NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain; 1.
DR   InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR   InterPro; IPR011537; NADH-UbQ_OxRdtase_suF.
DR   InterPro; IPR011538; Nuo51_FMN-bd.
DR   InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR   InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR   InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR   NCBIfam; TIGR01959; nuoF_fam; 1.
DR   PANTHER; PTHR11780:SF10; NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11780; NADH-UBIQUINONE OXIDOREDUCTASE FLAVOPROTEIN 1 NDUFV1; 1.
DR   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF10589; NADH_4Fe-4S; 1.
DR   SMART; SM00928; NADH_4Fe-4S; 1.
DR   SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1.
DR   SUPFAM; SSF142984; Nqo1 middle domain-like; 1.
DR   SUPFAM; SSF140490; Nqo1C-terminal domain-like; 1.
DR   PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR   PROSITE; PS00645; COMPLEX1_51K_2; 1.
DR   Genevisible; Q91YT0; MM.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Acetylation; Direct protein sequencing;
KW   Electron transport; Flavoprotein; FMN; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; Methylation; Mitochondrion; Mitochondrion inner membrane;
KW   NAD; Oxidoreductase; Reference proteome; Respiratory chain;
KW   Transit peptide; Translocase; Transport; Ubiquinone.
FT   TRANSIT         1..20
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:10870971"
FT   CHAIN           21..464
FT                   /note="NADH dehydrogenase [ubiquinone] flavoprotein 1,
FT                   mitochondrial"
FT                   /id="PRO_0000019978"
FT   BINDING         87..96
FT                   /ligand="NADH"
FT                   /ligand_id="ChEBI:CHEBI:57945"
FT                   /evidence="ECO:0000250"
FT   BINDING         199..247
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         379
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:29915388,
FT                   ECO:0007744|PDB:6G2J, ECO:0007744|PDB:6G72"
FT   BINDING         382
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:29915388,
FT                   ECO:0007744|PDB:6G2J, ECO:0007744|PDB:6G72"
FT   BINDING         385
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:29915388,
FT                   ECO:0007744|PDB:6G2J, ECO:0007744|PDB:6G72"
FT   BINDING         425
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:29915388,
FT                   ECO:0007744|PDB:6G2J, ECO:0007744|PDB:6G72"
FT   MOD_RES         81
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         81
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         104
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         257
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         375
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   TURN            37..39
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   TURN            43..46
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           53..58
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   TURN            59..62
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           65..70
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           72..83
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          88..91
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           95..99
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           100..102
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   STRAND          112..117
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           126..133
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           135..149
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          152..158
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           163..178
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          181..183
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           186..188
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          193..199
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           204..207
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           209..216
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          226..228
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   TURN            230..232
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           235..237
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          240..244
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           245..249
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           251..257
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           259..262
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          265..267
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          268..270
FT                   /evidence="ECO:0007829|PDB:6G2J"
FT   STRAND          272..284
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          286..291
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           296..303
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   TURN            308..310
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           311..313
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          314..321
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           329..332
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          336..338
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           339..344
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          353..358
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          359..361
FT                   /evidence="ECO:0007829|PDB:6ZTQ"
FT   HELIX           363..377
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           383..401
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           407..419
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   STRAND          422..425
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           426..441
FT                   /evidence="ECO:0007829|PDB:8OM1"
FT   HELIX           443..457
FT                   /evidence="ECO:0007829|PDB:8OM1"
SQ   SEQUENCE   464 AA;  50834 MW;  611EAB1546D2A630 CRC64;
     MLAARHFLGG LVPVRVSVRF SSGTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGALRRG
     DWYKTKEILL KGPDWILGEM KTSGLRGRGG AGFPTGLKWS FMNKPSDGRP KYLVVNADEG
     EPGTCKDREI MRHDPHKLVE GCLVGGRAMG ARAAYIYIRG EFYNEASNLQ VAIREAYEAG
     LIGKNACGSD YDFDVFVVRG AGAYICGEET ALIESIEGKQ GKPRLKPPFP ADVGVFGCPT
     TVANVETVAV SPTICRRGGT WFAGFGRERN SGTKLFNISG HVNHPCTVEE EMSVPLKELI
     EKHAGGVTGG WDNLLAVIPG GSSTPLIPKS VCETVLMDFD ALVQAQTGLG TAAVIVMDRS
     TDIVKAIARL IEFYKHESCG QCTPCREGVD WMNKVMARFV KGDARPAEID SLWEISKQIE
     GHTICALGDG AAWPVQGLIR HFRPELEDRM QRFAQQHRAW QAAS
//