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Trifunctional enzyme subunit alpha, mitochondrial (78 kDa gastrin-binding protein) (TP-alpha) [Includes: Long-chain enoyl-CoA hydratase (EC 4.2.1.17); Long chain 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.211)]

 ECHA_HUMAN              Reviewed;         763 AA.
P40939; B2R7L4; B4DYP2; Q16679; Q53T69; Q53TA2; Q96GT7; Q9UQC5;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
03-APR-2002, sequence version 2.
12-SEP-2018, entry version 211.
RecName: Full=Trifunctional enzyme subunit alpha, mitochondrial;
AltName: Full=78 kDa gastrin-binding protein;
AltName: Full=TP-alpha;
Includes:
RecName: Full=Long-chain enoyl-CoA hydratase;
EC=4.2.1.17;
Includes:
RecName: Full=Long chain 3-hydroxyacyl-CoA dehydrogenase;
EC=1.1.1.211;
Flags: Precursor;
Name=HADHA; Synonyms=HADH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8135828; DOI=10.1006/bbrc.1994.1302;
Kamijo T., Aoyama T., Komiyama A., Hashimoto T.;
"Structural analysis of cDNAs for subunits of human mitochondrial
fatty acid beta-oxidation trifunctional protein.";
Biochem. Biophys. Res. Commun. 199:818-825(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7918661; DOI=10.1016/0167-4781(94)90091-4;
Zhang Q.X., Baldwin G.S.;
"Structures of the human cDNA and gene encoding the 78 kDa gastrin-
binding protein and of a related pseudogene.";
Biochim. Biophys. Acta 1219:567-575(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Amygdala, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
PubMed=10075708; DOI=10.1074/jbc.274.12.8077;
Orii K.E., Orii K.O., Souri M., Orii T., Kondo N., Hashimoto T.,
Aoyama T.;
"Genes for the human mitochondrial trifunctional protein alpha- and
beta-subunits are divergently transcribed from a common promoter
region.";
J. Biol. Chem. 274:8077-8084(1999).
[8]
SUBUNIT.
PubMed=8163672; DOI=10.1172/JCI117158;
Kamijo T., Wanders R.J., Saudubray J.-M., Aoyama T., Komiyama A.,
Hashimoto T.;
"Mitochondrial trifunctional protein deficiency. Catalytic
heterogeneity of the mutant enzyme in two patients.";
J. Clin. Invest. 93:1740-1747(1994).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-295; LYS-303; LYS-406;
LYS-505; LYS-540 AND LYS-644, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-756, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-395, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[14]
VARIANT LCHAD DEFICIENCY GLN-510.
PubMed=7811722; DOI=10.1016/0005-2760(94)90064-7;
Ijlst L., Wanders R.J.A., Ushikubo S., Kamijo T., Hashimoto T.;
"Molecular basis of long-chain 3-hydroxyacyl-CoA dehydrogenase
deficiency: identification of the major disease-causing mutation in
the alpha-subunit of the mitochondrial trifunctional protein.";
Biochim. Biophys. Acta 1215:347-350(1994).
[15]
VARIANT AFLP GLN-510.
PubMed=7846063; DOI=10.1073/pnas.92.3.841;
Sims H.F., Brackett J.C., Powell C.K., Treem W.R., Hale D.E.,
Bennett M.J., Gibson B., Shapiro S., Strauss A.W.;
"The molecular basis of pediatric long chain 3-hydroxyacyl-CoA
dehydrogenase deficiency associated with maternal acute fatty liver of
pregnancy.";
Proc. Natl. Acad. Sci. U.S.A. 92:841-845(1995).
[16]
CHARACTERIZATION OF VARIANT LCHAD DEFICIENCY GLN-510.
PubMed=8770876; DOI=10.1172/JCI118863;
Ijlst L., Ruiter J.P.N., Hoovers J.M.N., Jakobs M.E., Wanders R.J.A.;
"Common missense mutation G1528C in long-chain 3-hydroxyacyl-CoA
dehydrogenase deficiency. Characterization and expression of the
mutant protein, mutation analysis on genomic DNA and chromosomal
localization of the mitochondrial trifunctional protein alpha subunit
gene.";
J. Clin. Invest. 98:1028-1033(1996).
[17]
VARIANTS LCHAD DEFICIENCY PRO-342 AND GLN-510.
PubMed=9266371; DOI=10.1023/A:1005310903004;
Ijlst L., Oostheim W., Ruiter J.P.N., Wanders R.J.A.;
"Molecular basis of long-chain 3-hydroxyacyl-CoA dehydrogenase
deficiency: identification of two new mutations.";
J. Inherit. Metab. Dis. 20:420-422(1997).
[18]
VARIANTS MTPD ASP-282 AND ASN-305.
PubMed=9739053; DOI=10.1172/JCI2091;
Ibdah J.A., Tein I., Dionisi-Vici C., Bennett M.J., Ijlst L.,
Gibson B., Wanders R.J.A., Strauss A.W.;
"Mild trifunctional protein deficiency is associated with progressive
neuropathy and myopathy and suggests a novel genotype-phenotype
correlation.";
J. Clin. Invest. 102:1193-1199(1998).
-!- FUNCTION: Bifunctional subunit.
-!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CoA + H(2)O.
-!- CATALYTIC ACTIVITY: A long-chain (S)-3-hydroxyacyl-CoA + NAD(+) =
a long-chain 3-oxoacyl-CoA + NADH.
-!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
-!- SUBUNIT: Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits.
{ECO:0000269|PubMed:8163672}.
-!- INTERACTION:
O95166:GABARAP; NbExp=5; IntAct=EBI-356720, EBI-712001;
Q9H0R8:GABARAPL1; NbExp=4; IntAct=EBI-356720, EBI-746969;
P60520:GABARAPL2; NbExp=4; IntAct=EBI-356720, EBI-720116;
Q9GZQ8:MAP1LC3B; NbExp=4; IntAct=EBI-356720, EBI-373144;
-!- SUBCELLULAR LOCATION: Mitochondrion.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P40939-1; Sequence=Displayed;
Name=2;
IsoId=P40939-2; Sequence=VSP_059010, VSP_059011;
Note=No experimental confirmation available. May be produced at
very low levels due to a premature stop codon in the mRNA,
leading to nonsense-mediated mRNA decay.;
-!- DISEASE: Mitochondrial trifunctional protein deficiency (MTPD)
[MIM:609015]: A disease biochemically characterized by loss of all
enzyme activities of the mitochondrial trifunctional protein
complex. Variable clinical manifestations include hypoglycemia,
cardiomyopathy, delayed psychomotor development, sensorimotor
axonopathy, generalized weakness, hepatic dysfunction, respiratory
failure. Sudden infant death may occur. Most patients die from
heart failure. {ECO:0000269|PubMed:9739053}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Long-chain 3-hydroxyl-CoA dehydrogenase deficiency (LCHAD
deficiency) [MIM:609016]: The clinical features are very similar
to TFP deficiency. Biochemically, LCHAD deficiency is
characterized by reduced long-chain 3-hydroxyl-CoA dehydrogenase
activity, while the other enzyme activities of the TFP complex are
normal or only slightly reduced. {ECO:0000269|PubMed:7811722,
ECO:0000269|PubMed:9266371}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Maternal acute fatty liver of pregnancy (AFLP)
[MIM:609016]: Severe maternal illness occurring during pregnancies
with affected fetuses. This disease is associated with LCHAD
deficiency and characterized by sudden unexplained infant death or
hypoglycemia and abnormal liver enzymes (Reye-like syndrome).
{ECO:0000269|PubMed:7846063}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
hydratase/isomerase family. {ECO:0000305}.
-!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-
CoA dehydrogenase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAG63804.1; Type=Miscellaneous discrepancy; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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EMBL; D16480; BAA03941.1; -; mRNA.
EMBL; U04627; AAA56664.1; -; mRNA.
EMBL; AK302532; BAG63804.1; ALT_SEQ; mRNA.
EMBL; AK313027; BAG35861.1; -; mRNA.
EMBL; AC010896; AAY14643.1; -; Genomic_DNA.
EMBL; AC011742; AAX93141.1; -; Genomic_DNA.
EMBL; CH471053; EAX00703.1; -; Genomic_DNA.
EMBL; BC009235; AAH09235.1; -; mRNA.
EMBL; AB020811; BAA76735.1; -; Genomic_DNA.
CCDS; CCDS1721.1; -. [P40939-1]
PIR; JC2108; JC2108.
RefSeq; NP_000173.2; NM_000182.4. [P40939-1]
UniGene; Hs.516032; -.
PDB; 5ZQZ; EM; 4.20 A; A/C=1-763.
PDB; 5ZRV; EM; 7.70 A; A/C/E/G=1-763.
PDBsum; 5ZQZ; -.
PDBsum; 5ZRV; -.
ProteinModelPortal; P40939; -.
SMR; P40939; -.
BioGrid; 109280; 114.
IntAct; P40939; 67.
MINT; P40939; -.
STRING; 9606.ENSP00000370023; -.
DrugBank; DB00157; NADH.
SwissLipids; SLP:000000247; -.
iPTMnet; P40939; -.
PhosphoSitePlus; P40939; -.
SwissPalm; P40939; -.
BioMuta; HADHA; -.
DMDM; 20141376; -.
REPRODUCTION-2DPAGE; IPI00031522; -.
UCD-2DPAGE; P40939; -.
EPD; P40939; -.
MaxQB; P40939; -.
PaxDb; P40939; -.
PeptideAtlas; P40939; -.
PRIDE; P40939; -.
ProteomicsDB; 55392; -.
DNASU; 3030; -.
Ensembl; ENST00000380649; ENSP00000370023; ENSG00000084754. [P40939-1]
Ensembl; ENST00000646483; ENSP00000496185; ENSG00000084754. [P40939-2]
GeneID; 3030; -.
KEGG; hsa:3030; -.
UCSC; uc002rgy.3; human. [P40939-1]
CTD; 3030; -.
DisGeNET; 3030; -.
EuPathDB; HostDB:ENSG00000084754.10; -.
GeneCards; HADHA; -.
HGNC; HGNC:4801; HADHA.
HPA; HPA015536; -.
HPA; HPA056070; -.
MalaCards; HADHA; -.
MIM; 600890; gene.
MIM; 609015; phenotype.
MIM; 609016; phenotype.
neXtProt; NX_P40939; -.
OpenTargets; ENSG00000084754; -.
Orphanet; 243367; Acute fatty liver of pregnancy.
Orphanet; 5; Long chain 3-hydroxyacyl-CoA dehydrogenase deficiency.
Orphanet; 746; Mitochondrial trifunctional protein deficiency.
PharmGKB; PA29175; -.
eggNOG; KOG1683; Eukaryota.
eggNOG; COG1024; LUCA.
eggNOG; COG1250; LUCA.
GeneTree; ENSGT00880000137923; -.
HOGENOM; HOG000261346; -.
HOVERGEN; HBG005557; -.
InParanoid; P40939; -.
KO; K07515; -.
OMA; PFRYMDT; -.
OrthoDB; EOG091G02LF; -.
PhylomeDB; P40939; -.
TreeFam; TF352288; -.
BioCyc; MetaCyc:HS01481-MONOMER; -.
Reactome; R-HSA-1482798; Acyl chain remodeling of CL.
Reactome; R-HSA-77285; Beta oxidation of myristoyl-CoA to lauroyl-CoA.
Reactome; R-HSA-77288; mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
Reactome; R-HSA-77305; Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
Reactome; R-HSA-77310; Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
Reactome; R-HSA-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
Reactome; R-HSA-77348; Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
Reactome; R-HSA-77350; Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
SABIO-RK; P40939; -.
UniPathway; UPA00659; -.
ChiTaRS; HADHA; human.
GenomeRNAi; 3030; -.
PRO; PR:P40939; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000084754; Expressed in 242 organ(s), highest expression level in gastrocnemius.
CleanEx; HS_HADH; -.
CleanEx; HS_HADHA; -.
ExpressionAtlas; P40939; baseline and differential.
Genevisible; P40939; HS.
GO; GO:0016507; C:mitochondrial fatty acid beta-oxidation multienzyme complex; IEA:Ensembl.
GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; TAS:ProtInc.
GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; TAS:ProtInc.
GO; GO:0004300; F:enoyl-CoA hydratase activity; TAS:ProtInc.
GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:Ensembl.
GO; GO:0016509; F:long-chain-3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0016508; F:long-chain-enoyl-CoA hydratase activity; IEA:Ensembl.
GO; GO:0051287; F:NAD binding; IEA:Ensembl.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
InterPro; IPR006108; 3HC_DH_C.
InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
InterPro; IPR001753; Enoyl-CoA_hydra/iso.
InterPro; IPR012803; Fa_ox_alpha_mit.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF00725; 3HCDH; 2.
Pfam; PF02737; 3HCDH_N; 1.
Pfam; PF00378; ECH_1; 1.
SUPFAM; SSF48179; SSF48179; 2.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF52096; SSF52096; 1.
TIGRFAMs; TIGR02441; fa_ox_alpha_mit; 1.
PROSITE; PS00067; 3HCDH; 1.
PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Disease mutation; Fatty acid metabolism; Lipid metabolism; Lyase;
Methylation; Mitochondrion; Multifunctional enzyme; NAD;
Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome;
Transit peptide.
TRANSIT 1 36 Mitochondrion. {ECO:0000255}.
CHAIN 37 763 Trifunctional enzyme subunit alpha,
mitochondrial.
/FTId=PRO_0000007403.
SITE 151 151 Important for catalytic activity.
{ECO:0000250}.
SITE 173 173 Important for catalytic activity.
{ECO:0000250}.
MOD_RES 46 46 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 46 46 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 60 60 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 60 60 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 129 129 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 166 166 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 166 166 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 213 213 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 214 214 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 214 214 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 230 230 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 249 249 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 249 249 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 289 289 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 295 295 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 303 303 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 303 303 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 316 316 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 326 326 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 326 326 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 334 334 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 334 334 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 350 350 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 350 350 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 353 353 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 395 395 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 399 399 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 406 406 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 406 406 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 411 411 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 411 411 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 415 415 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 419 419 Phosphoserine.
{ECO:0000250|UniProtKB:Q64428}.
MOD_RES 440 440 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 460 460 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 460 460 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 505 505 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 505 505 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 519 519 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 519 519 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 540 540 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 569 569 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 569 569 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 634 634 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 644 644 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 644 644 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 646 646 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 650 650 Phosphoserine.
{ECO:0000250|UniProtKB:Q64428}.
MOD_RES 664 664 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 664 664 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 728 728 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 728 728 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 735 735 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 756 756 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 759 759 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
MOD_RES 759 759 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q8BMS1}.
VAR_SEQ 61 82 VNTLSKELHSEFSEVMNEIWAS -> HVSRLQDPSRSNTAI
TRSTENS (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_059010.
VAR_SEQ 83 763 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_059011.
VARIANT 282 282 V -> D (in MTPD; mild phenotype with
slowly progressive myopathy and
sensorimotor polyneuropathy;
dbSNP:rs137852773).
{ECO:0000269|PubMed:9739053}.
/FTId=VAR_021125.
VARIANT 305 305 I -> N (in MTPD; mild phenotype with
slowly progressive myopathy and
sensorimotor polyneuropathy;
dbSNP:rs137852774).
{ECO:0000269|PubMed:9739053}.
/FTId=VAR_021126.
VARIANT 342 342 L -> P (in LCHAD deficiency;
dbSNP:rs137852772).
{ECO:0000269|PubMed:9266371}.
/FTId=VAR_021127.
VARIANT 358 358 Q -> K (in dbSNP:rs2229420).
/FTId=VAR_048908.
VARIANT 510 510 E -> Q (in AFLP and LCHAD deficiency;
loss of activity; dbSNP:rs137852769).
{ECO:0000269|PubMed:7811722,
ECO:0000269|PubMed:7846063,
ECO:0000269|PubMed:8770876,
ECO:0000269|PubMed:9266371}.
/FTId=VAR_002273.
CONFLICT 146 146 L -> V (in Ref. 1; BAA03941).
{ECO:0000305}.
CONFLICT 152 152 V -> L (in Ref. 2; AAA56664).
{ECO:0000305}.
CONFLICT 171 171 T -> A (in Ref. 2; AAA56664).
{ECO:0000305}.
CONFLICT 178 178 A -> I (in Ref. 2; AAA56664).
{ECO:0000305}.
CONFLICT 197 198 AL -> VF (in Ref. 2; AAA56664).
{ECO:0000305}.
CONFLICT 206 206 S -> N (in Ref. 2; AAA56664).
{ECO:0000305}.
CONFLICT 211 211 R -> S (in Ref. 2; AAA56664).
{ECO:0000305}.
CONFLICT 576 576 T -> P (in Ref. 2; AAA56664).
{ECO:0000305}.
CONFLICT 694 694 L -> S (in Ref. 1; BAA03941).
{ECO:0000305}.
SEQUENCE 763 AA; 83000 MW; 247FF7B4E48FB484 CRC64;
MVACRAIGIL SRFSAFRILR SRGYICRNFT GSSALLTRTH INYGVKGDVA VVRINSPNSK
VNTLSKELHS EFSEVMNEIW ASDQIRSAVL ISSKPGCFIA GADINMLAAC KTLQEVTQLS
QEAQRIVEKL EKSTKPIVAA INGSCLGGGL EVAISCQYRI ATKDRKTVLG TPEVLLGALP
GAGGTQRLPK MVGVPAALDM MLTGRSIRAD RAKKMGLVDQ LVEPLGPGLK PPEERTIEYL
EEVAITFAKG LADKKISPKR DKGLVEKLTA YAMTIPFVRQ QVYKKVEEKV RKQTKGLYPA
PLKIIDVVKT GIEQGSDAGY LCESQKFGEL VMTKESKALM GLYHGQVLCK KNKFGAPQKD
VKHLAILGAG LMGAGIAQVS VDKGLKTILK DATLTALDRG QQQVFKGLND KVKKKALTSF
ERDSIFSNLT GQLDYQGFEK ADMVIEAVFE DLSLKHRVLK EVEAVIPDHC IFASNTSALP
ISEIAAVSKR PEKVIGMHYF SPVDKMQLLE IITTEKTSKD TSASAVAVGL KQGKVIIVVK
DGPGFYTTRC LAPMMSEVIR ILQEGVDPKK LDSLTTSFGF PVGAATLVDE VGVDVAKHVA
EDLGKVFGER FGGGNPELLT QMVSKGFLGR KSGKGFYIYQ EGVKRKDLNS DMDSILASLK
LPPKSEVSSD EDIQFRLVTR FVNEAVMCLQ EGILATPAEG DIGAVFGLGF PPCLGGPFRF
VDLYGAQKIV DRLKKYEAAY GKQFTPCQLL ADHANSPNKK FYQ


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