ID   SDHA_MOUSE              Reviewed;         664 AA.
AC   Q8K2B3; Q0QF19; Q3UH25; Q3UKP7; Q3V4B1; Q921P5; Q9Z1Z4;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 170.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;
DE            EC=1.3.5.1 {ECO:0000250|UniProtKB:P31040};
DE   AltName: Full=Flavoprotein subunit of complex II;
DE            Short=Fp;
DE   Flags: Precursor;
GN   Name=Sdha;
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; TISSUE=Bone marrow, Egg, Heart, Pancreas, and Testis;
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=Czech II, and FVB/N; TISSUE=Mammary gland, and Mammary tumor;
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 1-14; 47-92; 121-128; 196-207; 233-246; 251-282;
RP   313-325; 362-418; 452-480; 486-498; 528-547; 601-615; 624-633 AND 637-647.
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 59-609.
RC   TISSUE=Liver;
RX   PubMed=16751257; DOI=10.1093/molbev/msl027;
RA   Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.;
RT   "Housekeeping genes for phylogenetic analysis of eutherian relationships.";
RL   Mol. Biol. Evol. 23:1493-1503(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 74-605.
RC   TISSUE=Heart;
RA   Weinreich D.M.;
RT   "OXPHOS genes in mammals and the molecular clock.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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   [7]
RP   ACETYLATION AT LYS-179; LYS-182; LYS-250; LYS-335; LYS-480; LYS-485;
RP   LYS-498; LYS-547; LYS-550; LYS-598; LYS-608; LYS-624 AND LYS-633, AND
RP   DEACETYLATION BY SIRT3.
RX   PubMed=21858060; DOI=10.1371/journal.pone.0023295;
RA   Finley L.W., Haas W., Desquiret-Dumas V., Wallace D.C., Procaccio V.,
RA   Gygi S.P., Haigis M.C.;
RT   "Succinate dehydrogenase is a direct target of sirtuin 3 deacetylase
RT   activity.";
RL   PLoS ONE 6:E23295-E23295(2011).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179 AND LYS-547, SUCCINYLATION
RP   [LARGE SCALE ANALYSIS] AT LYS-179; LYS-250; LYS-335; LYS-485; LYS-498;
RP   LYS-538; LYS-547 AND LYS-615, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast, and 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   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-167; LYS-179; LYS-182; LYS-335;
RP   LYS-423; LYS-498; LYS-517; LYS-538; LYS-547; LYS-608; LYS-636 AND LYS-647,
RP   AND 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).
CC   -!- FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH)
CC       that is involved in complex II of the mitochondrial electron transport
CC       chain and is responsible for transferring electrons from succinate to
CC       ubiquinone (coenzyme Q). Can act as a tumor suppressor.
CC       {ECO:0000250|UniProtKB:P31040}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + succinate = a quinol + fumarate;
CC         Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
CC         Evidence={ECO:0000250|UniProtKB:P31040};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q0QF01};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC       from succinate (eukaryal route): step 1/1.
CC       {ECO:0000250|UniProtKB:P31040}.
CC   -!- SUBUNIT: Component of complex II composed of four subunits: the
CC       flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome
CC       b560 composed of SDHC and SDHD (By similarity). Interacts with
CC       SDHAF2/SDH5; interaction is required for FAD attachment (By
CC       similarity). Interacts with TRAP1 (By similarity). Interacts with LACC1
CC       (By similarity). {ECO:0000250|UniProtKB:P31040,
CC       ECO:0000250|UniProtKB:Q0QF01}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q0QF01}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q0QF01}; Matrix side
CC       {ECO:0000250|UniProtKB:Q0QF01}.
CC   -!- PTM: Acetylation of Lys-498 and Lys-538 is observed in liver
CC       mitochondria from fasted mice but not from fed mice. Deacetylated by
CC       SIRT3. {ECO:0000269|PubMed:21858060}.
CC   -!- PTM: Phosphorylation at Tyr-215 is important for efficient electron
CC       transfer in complex II and the prevention of ROS generation.
CC       {ECO:0000250|UniProtKB:P31040}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000305}.
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DR   EMBL; AK029520; BAC26491.1; -; mRNA.
DR   EMBL; AK034928; BAC28884.1; -; mRNA.
DR   EMBL; AK049590; BAC33831.1; -; mRNA.
DR   EMBL; AK050475; BAC34276.1; -; mRNA.
DR   EMBL; AK075990; BAC36101.1; -; mRNA.
DR   EMBL; AK145923; BAE26754.1; -; mRNA.
DR   EMBL; AK147286; BAE27822.1; -; mRNA.
DR   EMBL; AK147624; BAE28032.1; -; mRNA.
DR   EMBL; AK153085; BAE31710.1; -; mRNA.
DR   EMBL; AK162148; BAE36754.1; -; mRNA.
DR   EMBL; AK169254; BAE41018.1; -; mRNA.
DR   EMBL; AK004362; BAE43173.1; -; mRNA.
DR   EMBL; BC011301; AAH11301.1; -; mRNA.
DR   EMBL; BC031849; AAH31849.1; -; mRNA.
DR   EMBL; DQ402975; ABD77308.1; -; mRNA.
DR   EMBL; AF095938; AAC72373.1; -; mRNA.
DR   CCDS; CCDS26643.1; -.
DR   RefSeq; NP_075770.1; NM_023281.1.
DR   AlphaFoldDB; Q8K2B3; -.
DR   SMR; Q8K2B3; -.
DR   BioGRID; 211828; 76.
DR   ComplexPortal; CPX-562; Mitochondrial respiratory chain complex II.
DR   CORUM; Q8K2B3; -.
DR   IntAct; Q8K2B3; 22.
DR   MINT; Q8K2B3; -.
DR   STRING; 10090.ENSMUSP00000022062; -.
DR   CarbonylDB; Q8K2B3; -.
DR   GlyGen; Q8K2B3; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8K2B3; -.
DR   MetOSite; Q8K2B3; -.
DR   PhosphoSitePlus; Q8K2B3; -.
DR   SwissPalm; Q8K2B3; -.
DR   REPRODUCTION-2DPAGE; Q8K2B3; -.
DR   EPD; Q8K2B3; -.
DR   jPOST; Q8K2B3; -.
DR   MaxQB; Q8K2B3; -.
DR   PaxDb; 10090-ENSMUSP00000022062; -.
DR   PeptideAtlas; Q8K2B3; -.
DR   ProteomicsDB; 255377; -.
DR   Pumba; Q8K2B3; -.
DR   DNASU; 66945; -.
DR   Ensembl; ENSMUST00000022062.8; ENSMUSP00000022062.8; ENSMUSG00000021577.15.
DR   GeneID; 66945; -.
DR   KEGG; mmu:66945; -.
DR   UCSC; uc007rfa.1; mouse.
DR   AGR; MGI:1914195; -.
DR   CTD; 6389; -.
DR   MGI; MGI:1914195; Sdha.
DR   VEuPathDB; HostDB:ENSMUSG00000021577; -.
DR   eggNOG; KOG2403; Eukaryota.
DR   GeneTree; ENSGT00910000144277; -.
DR   HOGENOM; CLU_014312_6_1_1; -.
DR   InParanoid; Q8K2B3; -.
DR   OMA; FHPTGIW; -.
DR   OrthoDB; 551958at2759; -.
DR   PhylomeDB; Q8K2B3; -.
DR   TreeFam; TF300763; -.
DR   Reactome; R-MMU-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; UER01006.
DR   BioGRID-ORCS; 66945; 18 hits in 80 CRISPR screens.
DR   ChiTaRS; Sdha; mouse.
DR   PRO; PR:Q8K2B3; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q8K2B3; Protein.
DR   Bgee; ENSMUSG00000021577; Expressed in heart right ventricle and 273 other cell types or tissues.
DR   ExpressionAtlas; Q8K2B3; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0045257; C:succinate dehydrogenase complex (ubiquinone); IDA:MGI.
DR   GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
DR   GO; GO:0007399; P:nervous system development; ISO:MGI.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; NAS:ComplexPortal.
DR   GO; GO:0022904; P:respiratory electron transport chain; ISS:UniProtKB.
DR   GO; GO:0006105; P:succinate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; NAS:ComplexPortal.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain; 1.
DR   Gene3D; 4.10.80.40; succinate dehydrogenase protein domain; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR003952; FRD_SDH_FAD_BS.
DR   InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR   InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR   InterPro; IPR030664; SdhA/FrdA/AprA.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   InterPro; IPR011281; Succ_DH_flav_su_fwd.
DR   InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR   NCBIfam; TIGR01816; sdhA_forward; 1.
DR   NCBIfam; TIGR01812; sdhA_frdA_Gneg; 1.
DR   PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR   PANTHER; PTHR11632:SF51; SUCCINATE DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN SUBUNIT, MITOCHONDRIAL; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
DR   Genevisible; Q8K2B3; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; FAD;
KW   Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide;
KW   Transport; Tricarboxylic acid cycle; Tumor suppressor.
FT   TRANSIT         1..42
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   CHAIN           43..664
FT                   /note="Succinate dehydrogenase [ubiquinone] flavoprotein
FT                   subunit, mitochondrial"
FT                   /id="PRO_0000010337"
FT   ACT_SITE        340
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         68..73
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         91..106
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         275
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         308
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         407
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         440
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         451
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   BINDING         456..457
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   MOD_RES         99
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT   MOD_RES         167
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         179
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21858060,
FT                   ECO:0007744|PubMed:23576753, ECO:0007744|PubMed:23806337"
FT   MOD_RES         179
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         182
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21858060,
FT                   ECO:0007744|PubMed:23576753"
FT   MOD_RES         215
FT                   /note="Phosphotyrosine; by SRC"
FT                   /evidence="ECO:0000250|UniProtKB:P31040"
FT   MOD_RES         250
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21858060"
FT   MOD_RES         250
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         335
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21858060,
FT                   ECO:0007744|PubMed:23576753"
FT   MOD_RES         335
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         423
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         480
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21858060"
FT   MOD_RES         485
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21858060"
FT   MOD_RES         485
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         498
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21858060,
FT                   ECO:0007744|PubMed:23576753"
FT   MOD_RES         498
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         517
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         538
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         538
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         547
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21858060,
FT                   ECO:0007744|PubMed:23576753, ECO:0007744|PubMed:23806337"
FT   MOD_RES         547
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         550
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21858060"
FT   MOD_RES         598
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21858060"
FT   MOD_RES         608
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21858060,
FT                   ECO:0007744|PubMed:23576753"
FT   MOD_RES         615
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         624
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21858060"
FT   MOD_RES         633
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21858060"
FT   MOD_RES         636
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         647
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   CONFLICT        69
FT                   /note="A -> V (in Ref. 1; BAE26754)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        246
FT                   /note="R -> Q (in Ref. 1; BAE26754)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        428
FT                   /note="Q -> R (in Ref. 1; BAE26754)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        501
FT                   /note="F -> L (in Ref. 4; ABD77308)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        517
FT                   /note="K -> M (in Ref. 4; ABD77308)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        571
FT                   /note="L -> M (in Ref. 4; ABD77308)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   664 AA;  72585 MW;  DDCE1535163C9449 CRC64;
     MAGVGAVSRL LRGRRLALTG AWPGTLQKQT CGFHFSVGEN KKASAKVSDA ISTQYPVVDH
     EFDAVVVGAG GAGLRAAFGL SEAGFNTACL TKLFPTRSHT VAAQGGINAA LGNMEEDNWR
     WHFYDTVKGS DWLGDQDAIH YMTEQAPASV VELENYGMPF SRTEDGKIYQ RAFGGQSLKF
     GKGGQAHRCC CVADRTGHSL LHTLYGRSLR YDTSYFVEYF ALDLLMENGE CRGVIALCIE
     DGSIHRIRAK NTVIATGGYG RTYFSCTSAH TSTGDGTAMV TRAGLPCQDL EFVQFHPTGI
     YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE IREGRGCGPE
     KDHVYLQLHH LPPEQLATRL PGISETAMIF AGVDVTKEPI PVLPTVHYNM GGIPTNYKGQ
     VLKHVNGQDQ IVPGLYACGE AACASVHGAN RLGANSLLDL VVFGRACALS IAESCRPGDK
     VPSIKANAGE ESVMNLDKLR FADGSIRTSE LRLNMQKSMQ NHAAVFRVGS VLQEGCEKIS
     QLYGDLKHLK TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDYKVR
     VDEYDYSKPI QGQQKKPFGE HWRKHTLSYV DIKTGKVTLE YRPVIDKTLN EADCATVPPA
     IRSY
//