AL7A1_MOUSE
ID AL7A1_MOUSE Reviewed; 539 AA.
AC Q9DBF1; Q3TFC7; Q3TVH7; Q3UKT6;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 4.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Alpha-aminoadipic semialdehyde dehydrogenase;
DE Short=Alpha-AASA dehydrogenase;
DE EC=1.2.1.31 {ECO:0000250|UniProtKB:P49419};
DE AltName: Full=Aldehyde dehydrogenase family 7 member A1;
DE EC=1.2.1.3 {ECO:0000250|UniProtKB:P49419};
DE AltName: Full=Antiquitin-1;
DE AltName: Full=Betaine aldehyde dehydrogenase;
DE EC=1.2.1.8 {ECO:0000250|UniProtKB:P49419};
DE AltName: Full=Delta1-piperideine-6-carboxylate dehydrogenase;
DE Short=P6c dehydrogenase;
DE Flags: Precursor;
GN Name=Aldh7a1 {ECO:0000312|MGI:MGI:108186}; Synonyms=Ald7a1;
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 {ECO:0000312|EMBL:BAB23726.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Liver;
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] (ISOFORM 1).
RC TISSUE=Salivary gland;
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 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 [4]
RP TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX PubMed=20207735; DOI=10.1074/jbc.m109.077925;
RA Brocker C., Lassen N., Estey T., Pappa A., Cantore M., Orlova V.V.,
RA Chavakis T., Kavanagh K.L., Oppermann U., Vasiliou V.;
RT "Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in
RT cellular defense against hyperosmotic stress.";
RL J. Biol. Chem. 285:18452-18463(2010).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-86; LYS-94; LYS-97 AND LYS-537,
RP AND IDENTIFICATION BY MASS 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-86; LYS-94; LYS-97; LYS-462 AND
RP LYS-500, 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: Multifunctional enzyme mediating important protective
CC effects. Metabolizes betaine aldehyde to betaine, an important cellular
CC osmolyte and methyl donor. Protects cells from oxidative stress by
CC metabolizing a number of lipid peroxidation-derived aldehydes. Involved
CC in lysine catabolism. {ECO:0000250|UniProtKB:P49419}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + nonanal = 2 H(+) + NADH + nonanoate;
CC Xref=Rhea:RHEA:69759, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32361, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:84268; Evidence={ECO:0000250|UniProtKB:P49419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69760;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2-amino-6-oxohexanoate + H2O + NAD(+) = 2 H(+) + L-2-
CC aminoadipate + NADH; Xref=Rhea:RHEA:12308, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58321, ChEBI:CHEBI:58672; EC=1.2.1.31;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12309;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.8;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16186;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH;
CC Xref=Rhea:RHEA:67276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:88528; Evidence={ECO:0000250|UniProtKB:P49419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67277;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + octanal = 2 H(+) + NADH + octanoate;
CC Xref=Rhea:RHEA:44100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P49419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44101;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-non-2-enal + H2O + NAD(+) = (E)-non-2-enoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:69767, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:142592,
CC ChEBI:CHEBI:143908; Evidence={ECO:0000250|UniProtKB:P49419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69768;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-hydroxynon-2-enal + H2O + NAD(+) = (E)-4-hydroxynon-2-
CC enoate + 2 H(+) + NADH; Xref=Rhea:RHEA:67248, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58968, ChEBI:CHEBI:142920;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67249;
CC Evidence={ECO:0000250|UniProtKB:P49419};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine from betaine aldehyde: step 1/1.
CC {ECO:0000250|UniProtKB:P49419}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P49419}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P49419}. Nucleus {ECO:0000250|UniProtKB:P49419}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion
CC {ECO:0000250|UniProtKB:P49419}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=mALDH7A1_v2 {ECO:0000269|PubMed:20207735};
CC IsoId=Q9DBF1-1; Sequence=Displayed;
CC Name=2; Synonyms=mALDH7A1_v1 {ECO:0000269|PubMed:20207735};
CC IsoId=Q9DBF1-2; Sequence=VSP_038989;
CC -!- TISSUE SPECIFICITY: Present in liver, kidney, brain and pancreas, and
CC at lower levels in jejunum, duodenum, stomach and testes (at protein
CC level). {ECO:0000269|PubMed:20207735}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH12407.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE26715.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK004991; BAB23726.1; -; mRNA.
DR EMBL; AK145873; BAE26715.1; ALT_INIT; mRNA.
DR EMBL; AK160117; BAE35641.1; -; mRNA.
DR EMBL; AK169195; BAE40971.1; -; mRNA.
DR EMBL; BC012407; AAH12407.1; ALT_INIT; mRNA.
DR CCDS; CCDS29258.2; -. [Q9DBF1-1]
DR CCDS; CCDS50291.1; -. [Q9DBF1-2]
DR RefSeq; NP_001120810.1; NM_001127338.1. [Q9DBF1-2]
DR RefSeq; NP_613066.2; NM_138600.4. [Q9DBF1-1]
DR AlphaFoldDB; Q9DBF1; -.
DR SMR; Q9DBF1; -.
DR BioGRID; 225826; 15.
DR STRING; 10090.ENSMUSP00000133372; -.
DR iPTMnet; Q9DBF1; -.
DR PhosphoSitePlus; Q9DBF1; -.
DR SwissPalm; Q9DBF1; -.
DR REPRODUCTION-2DPAGE; Q9DBF1; -.
DR EPD; Q9DBF1; -.
DR jPOST; Q9DBF1; -.
DR MaxQB; Q9DBF1; -.
DR PaxDb; Q9DBF1; -.
DR PeptideAtlas; Q9DBF1; -.
DR PRIDE; Q9DBF1; -.
DR ProteomicsDB; 296167; -. [Q9DBF1-1]
DR ProteomicsDB; 296168; -. [Q9DBF1-2]
DR Antibodypedia; 13922; 272 antibodies from 28 providers.
DR DNASU; 110695; -.
DR Ensembl; ENSMUST00000066208; ENSMUSP00000065089; ENSMUSG00000053644. [Q9DBF1-1]
DR Ensembl; ENSMUST00000174518; ENSMUSP00000133372; ENSMUSG00000053644. [Q9DBF1-2]
DR GeneID; 110695; -.
DR KEGG; mmu:110695; -.
DR UCSC; uc008eyn.2; mouse. [Q9DBF1-1]
DR CTD; 501; -.
DR MGI; MGI:108186; Aldh7a1.
DR VEuPathDB; HostDB:ENSMUSG00000053644; -.
DR eggNOG; KOG2453; Eukaryota.
DR GeneTree; ENSGT00940000154938; -.
DR InParanoid; Q9DBF1; -.
DR OMA; DAWKVYM; -.
DR OrthoDB; 692580at2759; -.
DR PhylomeDB; Q9DBF1; -.
DR TreeFam; TF300388; -.
DR BRENDA; 1.2.1.3; 3474.
DR BRENDA; 1.2.1.31; 3474.
DR Reactome; R-MMU-6798163; Choline catabolism.
DR Reactome; R-MMU-71064; Lysine catabolism.
DR UniPathway; UPA00529; UER00386.
DR BioGRID-ORCS; 110695; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Aldh7a1; mouse.
DR PRO; PR:Q9DBF1; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9DBF1; protein.
DR Bgee; ENSMUSG00000053644; Expressed in left lobe of liver and 286 other tissues.
DR ExpressionAtlas; Q9DBF1; baseline and differential.
DR Genevisible; Q9DBF1; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0004043; F:L-aminoadipate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR044638; ALDH7A1-like.
DR PANTHER; PTHR43521; PTHR43521; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Mitochondrion; NAD; Nucleus;
KW Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..539
FT /note="Alpha-aminoadipic semialdehyde dehydrogenase"
FT /id="PRO_0000056491"
FT ACT_SITE 296
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT BINDING 192..194
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P49419"
FT BINDING 218
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P49419"
FT BINDING 258..259
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P49419"
FT BINDING 274..279
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 274..275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P49419"
FT BINDING 296..297
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P49419"
FT BINDING 331
FT /ligand="(S)-2-amino-6-oxohexanoate"
FT /ligand_id="ChEBI:CHEBI:58321"
FT /evidence="ECO:0000250|UniProtKB:P49419"
FT BINDING 427
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P49419"
FT BINDING 489
FT /ligand="(S)-2-amino-6-oxohexanoate"
FT /ligand_id="ChEBI:CHEBI:58321"
FT /evidence="ECO:0000250|UniProtKB:P49419"
FT BINDING 490
FT /ligand="(S)-2-amino-6-oxohexanoate"
FT /ligand_id="ChEBI:CHEBI:58321"
FT /evidence="ECO:0000250|UniProtKB:P49419"
FT SITE 195
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 86
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 86
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 94
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 94
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 97
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 97
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 462
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 500
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 537
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 1..28
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038989"
FT CONFLICT 164
FT /note="I -> M (in Ref. 1; BAE26715)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="I -> V (in Ref. 1; BAE35641)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="E -> G (in Ref. 1; BAE35641)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 58861 MW; 7591EE5652F2577E CRC64;
MWRVPRRLCV QSVKTSKLSG PWSRPAAHMS TLLIHHPQYA WLQDLGLRED NEGVYNGSWG
GRGEVITTYC PANNEPIARV RQASLKDYEE TIGKAKKAWN IWADIPAPKR GEIVRKIGDA
FREKIQLLGR LVSLEMGKIL VEGIGEVQEY VDVCDYAAGL SRMIGGPTLP SERPGHALIE
MWNPLGLVGI ITAFNFPVAV FGWNNAIALI TGNVCLWKGA PTTSLVSVAV TKIIAQVLED
NLLPGAICSL VCGGADIGTT MARDERVNLL SFTGSTQVGK EVALMVQERF GKSLLELGGN
NAIIAFEDAD LSLVVPSVLF AAVGTAGQRC TTVRRLFLHE SIHNEVVDRL RSAYSQIRVG
NPWDPNILYG PLHTKQAVSM FVRAVEEAKK QGGTVVYGGK VMDHPGNYVE PTIVTGLAHD
APIVHQETFA PILYVFKFQD EEEVFEWNNE VKQGLSSSIF TKDLGRIFRW LGPKGSDCGI
VNVNIPTSGA EIGGAFGGEK HTGGGRESGS DAWKQYMRRS TCTINYSTSL PLAQGIKFQ
