SDHA_MOUSE
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 03-AUG-2022, entry version 162.
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, Pancreas,
RC 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; 72.
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 iPTMnet; Q8K2B3; -.
DR PhosphoSitePlus; Q8K2B3; -.
DR SwissPalm; Q8K2B3; -.
DR REPRODUCTION-2DPAGE; Q8K2B3; -.
DR EPD; Q8K2B3; -.
DR jPOST; Q8K2B3; -.
DR MaxQB; Q8K2B3; -.
DR PaxDb; Q8K2B3; -.
DR PeptideAtlas; Q8K2B3; -.
DR PRIDE; Q8K2B3; -.
DR ProteomicsDB; 255377; -.
DR DNASU; 66945; -.
DR Ensembl; ENSMUST00000022062; ENSMUSP00000022062; ENSMUSG00000021577.
DR GeneID; 66945; -.
DR KEGG; mmu:66945; -.
DR UCSC; uc007rfa.1; mouse.
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; DPIPIQP; -.
DR OrthoDB; 606981at2759; -.
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 75 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 270 other tissues.
DR ExpressionAtlas; Q8K2B3; baseline and differential.
DR Genevisible; Q8K2B3; MM.
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:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
DR GO; GO:0000104; F:succinate dehydrogenase activity; ISO:MGI.
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; IC: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; IC:ComplexPortal.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 3.90.700.10; -; 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 PANTHER; PTHR11632; PTHR11632; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR SUPFAM; SSF46977; SSF46977; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF56425; SSF56425; 1.
DR TIGRFAMs; TIGR01816; sdhA_forward; 1.
DR TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
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
