ECHA_PIG
ID ECHA_PIG Reviewed; 763 AA.
AC Q29554;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Trifunctional enzyme subunit alpha, mitochondrial;
DE AltName: Full=78 kDa gastrin-binding protein;
DE AltName: Full=Monolysocardiolipin acyltransferase {ECO:0000250|UniProtKB:P40939};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:P40939};
DE AltName: Full=TP-alpha;
DE Includes:
DE RecName: Full=Long-chain enoyl-CoA hydratase;
DE EC=4.2.1.17 {ECO:0000250|UniProtKB:P40939};
DE Includes:
DE RecName: Full=Long chain 3-hydroxyacyl-CoA dehydrogenase;
DE EC=1.1.1.211 {ECO:0000250|UniProtKB:P40939};
DE Flags: Precursor;
GN Name=HADHA; Synonyms=LCHYD-HAD;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Stomach;
RX PubMed=8399347; DOI=10.1016/0005-2760(93)90073-i;
RA Mantamadiotis T., Sobieszczuk P., Weinstock J., Baldwin G.S.;
RT "Nucleotide sequence encoding a novel member of the hydratase/dehydrogenase
RT family.";
RL Biochim. Biophys. Acta 1170:211-215(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=8297352; DOI=10.1006/bbrc.1994.1063;
RA Yang S.-Y., He X.-Y., Styles J., Luo M.J., Schulz H., Elzinga M.;
RT "Primary structure of the large subunit of trifunctional beta-oxidation
RT complex from pig heart mitochondria.";
RL Biochem. Biophys. Res. Commun. 198:431-437(1994).
RN [3]
RP PARTIAL NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver;
RX PubMed=8512557; DOI=10.1006/bbrc.1993.1660;
RA Baldwin G.S., Casey A., Weinstock J.;
RT "Partial structure of the gene encoding the 78 kDa gastrin binding protein
RT excludes a close relationship with the peroxisomal trifunctional enzyme.";
RL Biochem. Biophys. Res. Commun. 193:560-564(1993).
RN [4]
RP IDENTIFICATION.
RC TISSUE=Heart;
RX PubMed=7881821; DOI=10.1016/0305-0491(94)90117-1;
RA Yang S.-Y.;
RT "The large subunit of the pig heart mitochondrial membrane-bound beta-
RT oxidation complex is a long-chain enoyl-CoA hydratase: 3-hydroxyacyl-CoA
RT dehydrogenase bifunctional enzyme.";
RL Comp. Biochem. Physiol. 109B:557-566(1994).
CC -!- FUNCTION: Mitochondrial trifunctional enzyme catalyzes the last three
CC of the four reactions of the mitochondrial beta-oxidation pathway. The
CC mitochondrial beta-oxidation pathway is the major energy-producing
CC process in tissues and is performed through four consecutive reactions
CC breaking down fatty acids into acetyl-CoA. Among the enzymes involved
CC in this pathway, the trifunctional enzyme exhibits specificity for
CC long-chain fatty acids. Mitochondrial trifunctional enzyme is a
CC heterotetrameric complex composed of two proteins, the trifunctional
CC enzyme subunit alpha/HADHA described here carries the 2,3-enoyl-CoA
CC hydratase and the 3-hydroxyacyl-CoA dehydrogenase activities while the
CC trifunctional enzyme subunit beta/HADHB bears the 3-ketoacyl-CoA
CC thiolase activity. Independently of the subunit beta, the trifunctional
CC enzyme subunit alpha/HADHA also has a monolysocardiolipin
CC acyltransferase activity. It acylates monolysocardiolipin into
CC cardiolipin, a major mitochondrial membrane phospholipid which plays a
CC key role in apoptosis and supports mitochondrial respiratory chain
CC complexes in the generation of ATP. Allows the acylation of
CC monolysocardiolipin with different acyl-CoA substrates including
CC oleoyl-CoA for which it displays the highest activity.
CC {ECO:0000250|UniProtKB:P40939}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:58856; EC=4.2.1.17;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16107;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC ChEBI:CHEBI:137480; EC=4.2.1.17;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20726;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxyoctanoyl-CoA = (2E)-octenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:31199, ChEBI:CHEBI:15377, ChEBI:CHEBI:62242,
CC ChEBI:CHEBI:62617; Evidence={ECO:0000250|UniProtKB:P40939};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31201;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxydodecanoyl-CoA = (2E)-dodecenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:31075, ChEBI:CHEBI:15377, ChEBI:CHEBI:57330,
CC ChEBI:CHEBI:62558; Evidence={ECO:0000250|UniProtKB:P40939};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31077;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxyhexadecanoyl-CoA = (2E)-hexadecenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:31163, ChEBI:CHEBI:15377, ChEBI:CHEBI:61526,
CC ChEBI:CHEBI:62613; Evidence={ECO:0000250|UniProtKB:P40939};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31165;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain (3S)-3-hydroxy fatty acyl-CoA + NAD(+) = a long-
CC chain 3-oxo-fatty acyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:52656,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:136757, ChEBI:CHEBI:136758; EC=1.1.1.211;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52657;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxyoctanoyl-CoA + NAD(+) = 3-oxooctanoyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:31195, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:62617, ChEBI:CHEBI:62619;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31196;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxydecanoyl-CoA + NAD(+) = 3-oxodecanoyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:31187, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:62548, ChEBI:CHEBI:62616;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31188;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxydodecanoyl-CoA + NAD(+) = 3-oxododecanoyl-CoA +
CC H(+) + NADH; Xref=Rhea:RHEA:31179, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62558,
CC ChEBI:CHEBI:62615; Evidence={ECO:0000250|UniProtKB:P40939};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31180;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxytetradecanoyl-CoA + NAD(+) = 3-oxotetradecanoyl-
CC CoA + H(+) + NADH; Xref=Rhea:RHEA:31167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62543,
CC ChEBI:CHEBI:62614; Evidence={ECO:0000250|UniProtKB:P40939};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31168;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxyhexadecanoyl-CoA + NAD(+) = 3-oxohexadecanoyl-CoA
CC + H(+) + NADH; Xref=Rhea:RHEA:31159, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57349, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:62613; Evidence={ECO:0000250|UniProtKB:P40939};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31160;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-3'-
CC [1-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-glycerol +
CC hexadecanoyl-CoA = 1'-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phospho]-3'-[1-(9Z,12Z-octadecadienoyl)-2-hexadecanoyl-sn-glycero-3-
CC phospho]-glycerol + CoA; Xref=Rhea:RHEA:43680, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:83580, ChEBI:CHEBI:83583;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43681;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1'-[1,2-di-(9Z,12Z-octadecadienoyl)-
CC sn-glycero-3-phospho]-3'-[1-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phospho]-glycerol = 1'-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phospho]-3'-[1-(9Z,12Z-octadecadienoyl)-2-(9Z-octadecenoyl)-sn-
CC glycero-3-phospho]-glycerol + CoA; Xref=Rhea:RHEA:43676,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:83580,
CC ChEBI:CHEBI:83582; Evidence={ECO:0000250|UniProtKB:P40939};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43677;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1'-[1,2-di-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phospho]-3'-[1-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phospho]-glycerol = 1',3'-bis-[1,2-di-
CC (9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-glycerol + CoA;
CC Xref=Rhea:RHEA:43672, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:83580, ChEBI:CHEBI:83581;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43673;
CC Evidence={ECO:0000250|UniProtKB:P40939};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:P40939}.
CC -!- SUBUNIT: Heterotetramer of 2 alpha/HADHA and 2 beta/HADHB subunits;
CC forms the mitochondrial trifunctional enzyme (By similarity). Also
CC purified as higher order heterooligomers including a 4 alpha/HADHA and
CC 4 beta/HADHB heterooligomer which physiological significance remains
CC unclear (By similarity). The mitochondrial trifunctional enzyme
CC interacts with MTLN (By similarity). {ECO:0000250|UniProtKB:P40939,
CC ECO:0000250|UniProtKB:Q8BMS1}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P40939}.
CC Mitochondrion inner membrane {ECO:0000250|UniProtKB:P40939}.
CC Note=Protein stability and association with mitochondrion inner
CC membrane do not require HADHB. {ECO:0000250|UniProtKB:P40939}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; L12581; AAA03733.1; -; mRNA.
DR EMBL; AF028609; AAB84118.1; -; mRNA.
DR PIR; PN0511; PN0511.
DR RefSeq; NP_999127.1; NM_213962.2.
DR AlphaFoldDB; Q29554; -.
DR SMR; Q29554; -.
DR IntAct; Q29554; 1.
DR STRING; 9823.ENSSSCP00000009137; -.
DR PaxDb; Q29554; -.
DR PeptideAtlas; Q29554; -.
DR PRIDE; Q29554; -.
DR Ensembl; ENSSSCT00000009377; ENSSSCP00000009137; ENSSSCG00000008571.
DR Ensembl; ENSSSCT00055017005; ENSSSCP00055013425; ENSSSCG00055008692.
DR Ensembl; ENSSSCT00070023491; ENSSSCP00070019432; ENSSSCG00070012038.
DR GeneID; 397012; -.
DR KEGG; ssc:397012; -.
DR CTD; 3030; -.
DR VGNC; VGNC:88772; HADHA.
DR eggNOG; KOG1683; Eukaryota.
DR GeneTree; ENSGT00940000154677; -.
DR HOGENOM; CLU_009834_16_1_1; -.
DR InParanoid; Q29554; -.
DR OMA; PFRYMDT; -.
DR OrthoDB; 219667at2759; -.
DR TreeFam; TF352288; -.
DR Reactome; R-SSC-1482798; Acyl chain remodeling of CL.
DR Reactome; R-SSC-77285; Beta oxidation of myristoyl-CoA to lauroyl-CoA.
DR Reactome; R-SSC-77305; Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
DR Reactome; R-SSC-77310; Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
DR Reactome; R-SSC-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
DR Reactome; R-SSC-77348; Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
DR Reactome; R-SSC-77350; Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000008227; Chromosome 3.
DR Proteomes; UP000314985; Chromosome 3.
DR Bgee; ENSSSCG00000008571; Expressed in psoas major muscle and 43 other tissues.
DR ExpressionAtlas; Q29554; baseline and differential.
DR Genevisible; Q29554; SS.
DR GO; GO:0016507; C:mitochondrial fatty acid beta-oxidation multienzyme complex; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IBA:GO_Central.
DR GO; GO:0016509; F:long-chain-3-hydroxyacyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0035965; P:cardiolipin acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR InterPro; IPR006108; 3HC_DH_C.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR012803; Fa_ox_alpha_mit.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF48179; SSF48179; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR02441; fa_ox_alpha_mit; 1.
DR PROSITE; PS00067; 3HCDH; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Fatty acid metabolism; Lipid metabolism; Lyase; Membrane;
KW Methylation; Mitochondrion; Mitochondrion inner membrane;
KW Multifunctional enzyme; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 37..763
FT /note="Trifunctional enzyme subunit alpha, mitochondrial"
FT /id="PRO_0000007404"
FT ACT_SITE 510
FT /note="For hydroxyacyl-coenzyme A dehydrogenase activity"
FT /evidence="ECO:0000250|UniProtKB:P40939"
FT SITE 151
FT /note="Important for long-chain enoyl-CoA hydratase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P40939"
FT SITE 173
FT /note="Important for long-chain enoyl-CoA hydratase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P40939"
FT SITE 498
FT /note="Important for hydroxyacyl-coenzyme A dehydrogenase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P40939"
FT MOD_RES 46
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 46
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 60
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 60
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 129
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 166
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 166
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 213
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 214
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 214
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 230
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 249
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 249
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 289
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 295
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40939"
FT MOD_RES 303
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40939"
FT MOD_RES 303
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 326
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 326
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 334
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 334
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 350
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 350
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 353
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 399
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 406
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40939"
FT MOD_RES 406
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 411
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 411
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 415
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64428"
FT MOD_RES 440
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 460
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 460
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 505
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40939"
FT MOD_RES 505
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 519
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 519
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 540
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40939"
FT MOD_RES 569
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 569
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 620
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 634
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 644
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40939"
FT MOD_RES 644
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64428"
FT MOD_RES 728
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 728
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 735
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40939"
FT MOD_RES 759
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
FT MOD_RES 759
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS1"
SQ SEQUENCE 763 AA; 83107 MW; DD0C6E7AE6B3D0F4 CRC64;
MVASRAIGSL RRFTASQTLR CPGYICRNFT RSSALLTRTH INYGVKGDVA VIRINSPNSK
VNTLGQELHS EFIEVMNEVW SSSQIRSAVL ISSKPGCFIA GADINMLSAC TTSQEVTQIS
QEAQRTFEKL EKSTKPIVAA INGTCLGGGL ELAISCQYRI ATKDKKTVLG APEVLLGILP
GAGGTQRLPK MVGVPAAFDM MLTGRGIRAD KAKKMGLVDQ LVEPLGPGLK PPEERTIEYL
EEVAVTFAKG LADKKISPKR DKGLVEKLTS YAMSIPFVRQ QIYKKVEEKV RKQTKGLYPA
PLKIIDVVKT GIEQGSDAGY LSESQKFGEL AMTKESKALM GLYRGQTLCK KNKFGAPQKE
VKHLAILGAG LMGAGIAQVS VDKHLKTILK DASLPALGRG QQQVFKGLND KVRKKALTSF
ERDSLFSNLT GQLDYQGFEK ADMVIEAVFE ELSLKHKVLK EVEAVIPDHC VFASNTSALP
ISEIAAVSKR PEKVIGMHYF SPVDKMQLLE IITTEKTSKD STASAVEVGL KQGKVIIVVK
DGPGFYTTRC LAPMMSEVLR ILQEGVGPKK LDSLTTSFGF PVGAATLMDE VGMDVAKHVA
ENLGKIFGER FAGGNLDVLK QMISKGFLGR KSGKGFYVYQ EGVKNRNVNS DTESILASLK
IPSRPDISSD EDIQYRLVTR FVNEAVLCLQ EGILATPAEG DIGAVFGLGF PPCLGGPFRF
VDLYGAQKVV DRLRKYEAIY GKQFTPCQLL IDHASSPNKK FFQ
