ID   ACSM1_HUMAN             Reviewed;         577 AA.
AC   Q08AH1; Q08AH2; Q96A20;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   22-FEB-2023, entry version 126.
DE   RecName: Full=Acyl-coenzyme A synthetase ACSM1, mitochondrial;
DE            EC=6.2.1.2 {ECO:0000269|PubMed:10434065};
DE   AltName: Full=Acyl-CoA synthetase medium-chain family member 1;
DE   AltName: Full=Benzoate--CoA ligase;
DE            EC=6.2.1.25 {ECO:0000269|PubMed:10434065};
DE   AltName: Full=Butyrate--CoA ligase 1;
DE   AltName: Full=Butyryl-coenzyme A synthetase 1;
DE   AltName: Full=Lipoate-activating enzyme {ECO:0000250|UniProtKB:Q9BEA2};
DE   AltName: Full=Middle-chain acyl-CoA synthetase 1;
DE   AltName: Full=Xenobiotic/medium-chain fatty acid-CoA ligase HXM-B {ECO:0000303|PubMed:10434065};
DE   Flags: Precursor;
GN   Name=ACSM1; Synonyms=BUCS1, LAE {ECO:0000250|UniProtKB:Q9BEA2}, MACS1;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
RX   PubMed=11470804; DOI=10.1074/jbc.m106651200;
RA   Fujino T., Takei Y.A., Sone H., Ioka R.X., Kamataki A., Magoori K.,
RA   Takahashi S., Sakai J., Yamamoto T.T.;
RT   "Molecular identification and characterization of two medium-chain acyl-CoA
RT   synthetases, MACS1 and the Sa gene product.";
RL   J. Biol. Chem. 276:35961-35966(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=10434065; DOI=10.1016/s0304-4165(99)00088-4;
RA   Vessey D.A., Kelley M., Warren R.S.;
RT   "Characterization of the CoA ligases of human liver mitochondria catalyzing
RT   the activation of short- and medium-chain fatty acids and xenobiotic
RT   carboxylic acids.";
RL   Biochim. Biophys. Acta 1428:455-462(1999).
RN   [4]
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   [5]
RP   REVIEW.
RX   PubMed=27351777; DOI=10.1080/17425255.2016.1206888;
RA   van der Sluis R., Erasmus E.;
RT   "Xenobiotic/medium chain fatty acid: CoA ligase - a critical review on its
RT   role in fatty acid metabolism and the detoxification of benzoic acid and
RT   aspirin.";
RL   Expert Opin. Drug Metab. Toxicol. 12:1169-1179(2016).
CC   -!- FUNCTION: Catalyzes the activation of fatty acids by CoA to produce an
CC       acyl-CoA, the first step in fatty acid metabolism (PubMed:10434065).
CC       Capable of activating medium-chain fatty acids (e.g. butyric (C4) to
CC       decanoic (C10) acids), and certain carboxylate-containing xenobiotics,
CC       e.g. benzoate (PubMed:10434065). Also catalyzes the activation of
CC       lipoate to lipoyl-nucleoside monophosphate (By similarity). Activates
CC       lipoate with GTP at a 1000-fold higher rate than with ATP and activates
CC       both (R)- and (S)-lipoate to the respective lipoyl-GMP, with a
CC       preference for (R)-lipoate (By similarity).
CC       {ECO:0000250|UniProtKB:Q9BEA2, ECO:0000269|PubMed:10434065}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC         acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC         Evidence={ECO:0000269|PubMed:10434065};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC         Evidence={ECO:0000305|PubMed:10434065};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + benzoate + CoA = AMP + benzoyl-CoA + diphosphate;
CC         Xref=Rhea:RHEA:10132, ChEBI:CHEBI:16150, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57369,
CC         ChEBI:CHEBI:456215; EC=6.2.1.25;
CC         Evidence={ECO:0000269|PubMed:10434065};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10133;
CC         Evidence={ECO:0000269|PubMed:10434065};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-lipoate + GTP + H(+) = (R)-lipoyl-GMP + diphosphate;
CC         Xref=Rhea:RHEA:46700, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:83088, ChEBI:CHEBI:86460;
CC         Evidence={ECO:0000250|UniProtKB:Q9BEA2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46701;
CC         Evidence={ECO:0000250|UniProtKB:Q9BEA2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA;
CC         Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q91VA0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33632;
CC         Evidence={ECO:0000250|UniProtKB:Q91VA0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + decanoate = AMP + decanoyl-CoA + diphosphate;
CC         Xref=Rhea:RHEA:33627, ChEBI:CHEBI:27689, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:10434065};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33628;
CC         Evidence={ECO:0000305|PubMed:10434065};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + dodecanoate = AMP + diphosphate + dodecanoyl-CoA;
CC         Xref=Rhea:RHEA:33623, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q91VA0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33624;
CC         Evidence={ECO:0000250|UniProtKB:Q91VA0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + tetradecanoate = AMP + diphosphate +
CC         tetradecanoyl-CoA; Xref=Rhea:RHEA:33619, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:30807, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57385, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:Q91VA0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33620;
CC         Evidence={ECO:0000250|UniProtKB:Q91VA0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA;
CC         Xref=Rhea:RHEA:43740, ChEBI:CHEBI:17120, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000305|PubMed:10434065};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741;
CC         Evidence={ECO:0000305|PubMed:10434065};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + butanoate + CoA = AMP + butanoyl-CoA + diphosphate;
CC         Xref=Rhea:RHEA:46172, ChEBI:CHEBI:17968, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000305|PubMed:10434065};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173;
CC         Evidence={ECO:0000305|PubMed:10434065};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC         CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q91VA0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC         Evidence={ECO:0000250|UniProtKB:Q91VA0};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:10434065};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:10434065};
CC   -!- ACTIVITY REGULATION: Activated by monovalent cations, such as
CC       potassium, rubidium or ammonium. {ECO:0000269|PubMed:10434065}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=21 uM for benzoate {ECO:0000269|PubMed:10434065};
CC         KM=570 uM for butyrate {ECO:0000269|PubMed:10434065};
CC         KM=20 uM for decanoate {ECO:0000269|PubMed:10434065};
CC         KM=34 uM for hexanoate {ECO:0000269|PubMed:10434065};
CC         KM=24 uM for laurate {ECO:0000269|PubMed:10434065};
CC         KM=143 uM for phenylacetate {ECO:0000269|PubMed:10434065};
CC         KM=25 uM for salicylate {ECO:0000269|PubMed:10434065};
CC         Vmax=9 nmol/min/mg enzyme for benzoate {ECO:0000269|PubMed:10434065};
CC         Vmax=24 nmol/min/mg enzyme for butyrate
CC         {ECO:0000269|PubMed:10434065};
CC         Vmax=8 nmol/min/mg enzyme for decanoate
CC         {ECO:0000269|PubMed:10434065};
CC         Vmax=118 nmol/min/mg enzyme for hexanoate
CC         {ECO:0000269|PubMed:10434065};
CC         Vmax=0.15 nmol/min/mg enzyme for laurate
CC         {ECO:0000269|PubMed:10434065};
CC         Vmax=2 nmol/min/mg enzyme for phenylacetate
CC         {ECO:0000269|PubMed:10434065};
CC       pH dependence:
CC         Optimum pH is 8.8. {ECO:0000269|PubMed:10434065};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9BEA2}.
CC   -!- INTERACTION:
CC       Q08AH1; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-2818055, EBI-11522780;
CC       Q08AH1; P43356: MAGEA2B; NbExp=3; IntAct=EBI-2818055, EBI-5650739;
CC       Q08AH1; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2818055, EBI-11522433;
CC       Q08AH1; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-2818055, EBI-1051317;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q91VA0}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q91VA0}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q08AH1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q08AH1-2; Sequence=VSP_028391;
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AB059429; BAB64535.1; -; mRNA.
DR   EMBL; AB062503; BAB68363.1; -; Genomic_DNA.
DR   EMBL; BC125177; AAI25178.1; -; mRNA.
DR   EMBL; BC125178; AAI25179.1; -; mRNA.
DR   CCDS; CCDS10587.1; -. [Q08AH1-1]
DR   RefSeq; NP_001305819.1; NM_001318890.1. [Q08AH1-1]
DR   RefSeq; NP_443188.2; NM_052956.2. [Q08AH1-1]
DR   AlphaFoldDB; Q08AH1; -.
DR   SMR; Q08AH1; -.
DR   BioGRID; 125496; 10.
DR   IntAct; Q08AH1; 9.
DR   STRING; 9606.ENSP00000301956; -.
DR   SwissLipids; SLP:000000449; -.
DR   iPTMnet; Q08AH1; -.
DR   PhosphoSitePlus; Q08AH1; -.
DR   BioMuta; ACSM1; -.
DR   DMDM; 121940002; -.
DR   MassIVE; Q08AH1; -.
DR   PaxDb; Q08AH1; -.
DR   PeptideAtlas; Q08AH1; -.
DR   ProteomicsDB; 58670; -. [Q08AH1-1]
DR   ProteomicsDB; 58671; -. [Q08AH1-2]
DR   TopDownProteomics; Q08AH1-1; -. [Q08AH1-1]
DR   Antibodypedia; 49877; 70 antibodies from 18 providers.
DR   DNASU; 116285; -.
DR   Ensembl; ENST00000307493.8; ENSP00000301956.3; ENSG00000166743.10. [Q08AH1-1]
DR   Ensembl; ENST00000519745.5; ENSP00000428650.1; ENSG00000166743.10. [Q08AH1-2]
DR   Ensembl; ENST00000520010.6; ENSP00000428047.1; ENSG00000166743.10. [Q08AH1-1]
DR   GeneID; 116285; -.
DR   KEGG; hsa:116285; -.
DR   MANE-Select; ENST00000520010.6; ENSP00000428047.1; NM_001318890.3; NP_001305819.1.
DR   UCSC; uc002dhm.1; human. [Q08AH1-1]
DR   AGR; HGNC:18049; -.
DR   CTD; 116285; -.
DR   DisGeNET; 116285; -.
DR   GeneCards; ACSM1; -.
DR   HGNC; HGNC:18049; ACSM1.
DR   HPA; ENSG00000166743; Tissue enriched (breast).
DR   MIM; 614357; gene.
DR   neXtProt; NX_Q08AH1; -.
DR   OpenTargets; ENSG00000166743; -.
DR   PharmGKB; PA25468; -.
DR   VEuPathDB; HostDB:ENSG00000166743; -.
DR   eggNOG; KOG1175; Eukaryota.
DR   GeneTree; ENSGT00940000161138; -.
DR   HOGENOM; CLU_000022_59_10_1; -.
DR   InParanoid; Q08AH1; -.
DR   OMA; ECTAPCA; -.
DR   OrthoDB; 5474118at2759; -.
DR   PhylomeDB; Q08AH1; -.
DR   TreeFam; TF354287; -.
DR   BioCyc; MetaCyc:HS09445-MON; -.
DR   PathwayCommons; Q08AH1; -.
DR   Reactome; R-HSA-177135; Conjugation of benzoate with glycine.
DR   Reactome; R-HSA-177162; Conjugation of phenylacetate with glutamine.
DR   SignaLink; Q08AH1; -.
DR   BioGRID-ORCS; 116285; 15 hits in 1149 CRISPR screens.
DR   ChiTaRS; ACSM1; human.
DR   GenomeRNAi; 116285; -.
DR   Pharos; Q08AH1; Tbio.
DR   PRO; PR:Q08AH1; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q08AH1; protein.
DR   Bgee; ENSG00000166743; Expressed in left ovary and 93 other tissues.
DR   ExpressionAtlas; Q08AH1; baseline and differential.
DR   Genevisible; Q08AH1; HS.
DR   GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0018858; F:benzoate-CoA ligase activity; IDA:UniProtKB.
DR   GO; GO:0047760; F:butyrate-CoA ligase activity; IDA:UniProtKB.
DR   GO; GO:0016405; F:CoA-ligase activity; TAS:Reactome.
DR   GO; GO:0102391; F:decanoate-CoA ligase activity; IDA:UniProtKB.
DR   GO; GO:0015645; F:fatty acid ligase activity; IBA:GO_Central.
DR   GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR   GO; GO:0018874; P:benzoate metabolic process; NAS:UniProtKB.
DR   GO; GO:0019605; P:butyrate metabolic process; NAS:UniProtKB.
DR   GO; GO:0042632; P:cholesterol homeostasis; NAS:BHF-UCL.
DR   GO; GO:0015980; P:energy derivation by oxidation of organic compounds; NAS:UniProtKB.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019395; P:fatty acid oxidation; NAS:UniProtKB.
DR   GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR   CDD; cd05928; MACS_euk; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 1.
DR   PANTHER; PTHR43605:SF5; ACYL-COENZYME A SYNTHETASE ACSM1, MITOCHONDRIAL; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Fatty acid metabolism;
KW   GTP-binding; Ligase; Lipid metabolism; Magnesium; Metal-binding;
KW   Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide.
FT   TRANSIT         1..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           32..577
FT                   /note="Acyl-coenzyme A synthetase ACSM1, mitochondrial"
FT                   /id="PRO_0000306091"
FT   BINDING         226..234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         452
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         467
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         563
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         85
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT   MOD_RES         146
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT   MOD_RES         146
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT   MOD_RES         183
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT   MOD_RES         204
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT   MOD_RES         204
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT   MOD_RES         214
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT   MOD_RES         237
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT   MOD_RES         356
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT   MOD_RES         356
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT   MOD_RES         391
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT   MOD_RES         391
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT   MOD_RES         531
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT   MOD_RES         538
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT   MOD_RES         538
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT   MOD_RES         549
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VA0"
FT   VAR_SEQ         205..577
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_028391"
FT   VARIANT         272
FT                   /note="I -> M (in dbSNP:rs16970511)"
FT                   /id="VAR_048238"
FT   VARIANT         479
FT                   /note="I -> V (in dbSNP:rs8056709)"
FT                   /id="VAR_035245"
FT   VARIANT         515
FT                   /note="I -> T (in dbSNP:rs16970453)"
FT                   /id="VAR_035246"
FT   CONFLICT        549
FT                   /note="K -> N (in Ref. 1; BAB64535/BAB68363)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   577 AA;  65273 MW;  380BF4B8944B0E34 CRC64;
     MQWLMRFRTL WGIHKSFHNI HPAPSQLRCR SLSEFGAPRW NDYEVPEEFN FASYVLDYWA
     QKEKEGKRGP NPAFWWVNGQ GDEVKWSFRE MGDLTRRVAN VFTQTCGLQQ GDHLALMLPR
     VPEWWLVAVG CMRTGIIFIP ATILLKAKDI LYRLQLSKAK GIVTIDALAS EVDSIASQCP
     SLKTKLLVSD HSREGWLDFR SLVKSASPEH TCVKSKTLDP MVIFFTSGTT GFPKMAKHSH
     GLALQPSFPG SRKLRSLKTS DVSWCLSDSG WIVATIWTLV EPWTAGCTVF IHHLPQFDTK
     VIIQTLLKYP INHFWGVSSI YRMILQQDFT SIRFPALEHC YTGGEVVLPK DQEEWKRRTG
     LLLYENYGQS ETGLICATYW GMKIKPGFMG KATPPYDVQV IDDKGSILPP NTEGNIGIRI
     KPVRPVSLFM CYEGDPEKTA KVECGDFYNT GDRGKMDEEG YICFLGRSDD IINASGYRIG
     PAEVESALVE HPAVAESAVV GSPDPIRGEV VKAFIVLTPQ FLSHDKDQLT KELQQHVKSV
     TAPYKYPRKV EFVSELPKTI TGKIERKELR KKETGQM
//