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Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial (HCDH) (EC 1 1 1 35) (Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase) (Short-chain 3-hydroxyacyl-CoA dehydrogenase)

 HCDH_HUMAN              Reviewed;         314 AA.
Q16836; J3KQ17; O00324; O00397; O00753; Q4W5B4;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 3.
20-JUN-2018, entry version 197.
RecName: Full=Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial;
Short=HCDH;
EC=1.1.1.35;
AltName: Full=Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase;
AltName: Full=Short-chain 3-hydroxyacyl-CoA dehydrogenase;
Flags: Precursor;
Name=HADH; Synonyms=HAD, HADHSC, SCHAD;
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), AND VARIANTS PRO-86 AND
HIS-152.
TISSUE=Liver;
PubMed=8687463; DOI=10.1006/bbrc.1996.0961;
Vredendaal P.J.C.M., van den Berg I.E.T., Malingre H.E.M.,
Stroobants A.K., Oldeweghuis D.E.M., Berger R.;
"Human short-chain L-3-hydroxyacyl-CoA dehydrogenase: cloning and
characterization of the coding sequence.";
Biochem. Biophys. Res. Commun. 223:718-723(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), NUCLEOTIDE
SEQUENCE [MRNA] OF 7-314 (ISOFORM 1), AND VARIANT PRO-86.
TISSUE=Skeletal muscle;
Shi Y., Samuel S.J., Lee W., Yu C.H., Zhang W., Lachaal M., Jung C.Y.;
"Cloning of a L-3-hydroxyacyl CoA dehydrogenase that binds to GLUT4
glucose transporter cytoplasmic C-terminus: possible crosstalk between
glucose transport and fatty acid metabolism.";
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-86.
O'Brien L.K., Sims H.F., Strauss A.W.;
"Human short chain L-3-hydroxyacyl-CoA dehydrogenase.";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[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 MRNA] (ISOFORM 1), AND VARIANT
PRO-86.
TISSUE=Lung;
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).
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-185; LYS-202; LYS-241 AND
LYS-312, 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).
[7]
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).
[8]
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).
[9]
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).
[10]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 13-314 IN COMPLEX WITH
SUBSTRATE AND NAD.
PubMed=10231530; DOI=10.1021/bi9829027;
Barycki J.J., O'Brien L.K., Bratt J.M., Zhang R., Sanishvili R.,
Strauss A.W., Banaszak L.J.;
"Biochemical characterization and crystal structure determination of
human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide
insights into catalytic mechanism.";
Biochemistry 38:5786-5798(1999).
[11]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 13-314 IN COMPLEX WITH
SUBSTRATE AND NAD.
PubMed=10840044; DOI=10.1074/jbc.M004669200;
Barycki J.J., O'Brien L.K., Strauss A.W., Banaszak L.J.;
"Sequestration of the active site by interdomain shifting.
Crystallographic and spectroscopic evidence for distinct conformations
of L-3-hydroxyacyl-CoA dehydrogenase.";
J. Biol. Chem. 275:27186-27196(2000).
[12]
REVIEW.
PubMed=16176262; DOI=10.1111/j.1742-4658.2005.04911.x;
Yang S.-Y., He X.-Y., Schulz H.;
"3-hydroxyacyl-CoA dehydrogenase and short chain 3-hydroxyacyl-CoA
dehydrogenase in human health and disease.";
FEBS J. 272:4874-4883(2005).
[13]
VARIANTS HADH DEFICIENCY THR-40 AND GLU-57.
O'Brien L.K., Rinaldo P., Sims H.F., Alonso E.M., Charrow J.,
Jones P.M., Bennett M.J., Barycki J.J., Banaszak L.J., Strauss A.W.;
"Fulminant hepatic failure associated with mutations in the medium and
short chain L-3-hydroxyacyl-CoA dehydrogenase gene.";
J. Inherit. Metab. Dis. 23 Suppl. 1:127-127(2000).
[14]
VARIANT HHF4 LEU-258, AND CHARACTERIZATION OF VARIANT HHF4 LEU-258.
PubMed=11489939; DOI=10.1172/JCI200111294;
Clayton P.T., Eaton S., Aynsley-Green A., Edginton M., Hussain K.,
Krywawych S., Datta V., Malingre H.E.M., Berger R.,
van den Berg I.E.T.;
"Hyperinsulinism in short-chain L-3-hydroxyacyl-CoA dehydrogenase
deficiency reveals the importance of beta-oxidation in insulin
secretion.";
J. Clin. Invest. 108:457-465(2001).
-!- FUNCTION: Plays an essential role in the mitochondrial beta-
oxidation of short chain fatty acids. Exerts it highest activity
toward 3-hydroxybutyryl-CoA.
-!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
+ NADH.
-!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10231530,
ECO:0000269|PubMed:10840044}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q16836-1; Sequence=Displayed;
Name=2;
IsoId=Q16836-2; Sequence=VSP_016551, VSP_016552;
Note=Ref.2 (AAB58153) sequence is in conflict in position:
41:L->P. Ref.2 (AAB58153) sequence is in conflict in position:
56:R->H. {ECO:0000305};
Name=3;
IsoId=Q16836-3; Sequence=VSP_016552;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in liver, kidney, pancreas, heart
and skeletal muscle.
-!- PTM: Succinylation at Lys-81, adjacent to a coenzyme A binding
site. Desuccinylated by SIRT5 (By similarity). {ECO:0000250}.
-!- DISEASE: 3-alpha-hydroxyacyl-CoA dehydrogenase deficiency (HADH
deficiency) [MIM:231530]: An autosomal recessive, metabolic
disorder with various clinical presentations including
hypoglycemia, hepatoencephalopathy, myopathy or cardiomyopathy,
and in some cases sudden death. {ECO:0000269|Ref.13}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Familial hyperinsulinemic hypoglycemia 4 (HHF4)
[MIM:609975]: Most common cause of persistent hypoglycemia in
infancy. Unless early and aggressive intervention is undertaken,
brain damage from recurrent episodes of hypoglycemia may occur.
HHF4 should be easily recognizable by analysis of acylcarnitine
species and that this disorder responds well to treatment with
diazoxide. It provides the first 'experiment of nature' that links
impaired fatty acid oxidation to hyperinsulinism and that provides
support for the concept that a lipid signaling pathway is
implicated in the control of insulin secretion.
{ECO:0000269|PubMed:11489939}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
{ECO:0000305}.
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EMBL; X96752; CAA65528.1; -; mRNA.
EMBL; AF001902; AAB54008.1; -; mRNA.
EMBL; AF001903; AAB54009.1; -; mRNA.
EMBL; AF001904; AAB58153.1; -; Genomic_DNA.
EMBL; AF095703; AAD13581.1; -; Genomic_DNA.
EMBL; AC114733; AAY41050.1; -; Genomic_DNA.
EMBL; AC118062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000306; AAH00306.1; -; mRNA.
CCDS; CCDS3678.1; -. [Q16836-1]
CCDS; CCDS54790.1; -. [Q16836-3]
PIR; JC4879; JC4879.
RefSeq; NP_001171634.2; NM_001184705.2.
RefSeq; NP_005318.3; NM_005327.4.
UniGene; Hs.438289; -.
PDB; 1F0Y; X-ray; 1.80 A; A/B=13-314.
PDB; 1F12; X-ray; 2.40 A; A/B=13-314.
PDB; 1F14; X-ray; 2.30 A; A/B=13-314.
PDB; 1F17; X-ray; 2.30 A; A/B=13-314.
PDB; 1IL0; X-ray; 2.20 A; A/B=13-314.
PDB; 1LSJ; X-ray; 2.50 A; A/B=13-314.
PDB; 1LSO; X-ray; 2.60 A; A/B=13-314.
PDB; 1M75; X-ray; 2.30 A; A/B=13-314.
PDB; 1M76; X-ray; 2.15 A; A/B=13-314.
PDB; 2HDH; X-ray; 2.20 A; A/B=24-314.
PDB; 3HAD; X-ray; 2.00 A; A/B=13-314.
PDB; 3RQS; X-ray; 2.00 A; A/B=1-314.
PDBsum; 1F0Y; -.
PDBsum; 1F12; -.
PDBsum; 1F14; -.
PDBsum; 1F17; -.
PDBsum; 1IL0; -.
PDBsum; 1LSJ; -.
PDBsum; 1LSO; -.
PDBsum; 1M75; -.
PDBsum; 1M76; -.
PDBsum; 2HDH; -.
PDBsum; 3HAD; -.
PDBsum; 3RQS; -.
ProteinModelPortal; Q16836; -.
SMR; Q16836; -.
BioGrid; 109283; 23.
IntAct; Q16836; 5.
DrugBank; DB03612; 3-Hydroxybutyryl-Coenzyme A.
DrugBank; DB03059; Acetoacetyl-Coenzyme A.
DrugBank; DB00157; NADH.
SwissLipids; SLP:000001250; -.
iPTMnet; Q16836; -.
PhosphoSitePlus; Q16836; -.
BioMuta; HADH; -.
DMDM; 311033442; -.
REPRODUCTION-2DPAGE; IPI00298406; -.
UCD-2DPAGE; Q16836; -.
EPD; Q16836; -.
MaxQB; Q16836; -.
PeptideAtlas; Q16836; -.
PRIDE; Q16836; -.
ProteomicsDB; 61096; -.
ProteomicsDB; 61097; -. [Q16836-2]
TopDownProteomics; Q16836-1; -. [Q16836-1]
DNASU; 3033; -.
Ensembl; ENST00000309522; ENSP00000312288; ENSG00000138796. [Q16836-1]
Ensembl; ENST00000603302; ENSP00000474560; ENSG00000138796. [Q16836-3]
GeneID; 3033; -.
KEGG; hsa:3033; -.
UCSC; uc003hyq.4; human. [Q16836-1]
CTD; 3033; -.
DisGeNET; 3033; -.
EuPathDB; HostDB:ENSG00000138796.15; -.
GeneCards; HADH; -.
GeneReviews; HADH; -.
HGNC; HGNC:4799; HADH.
HPA; HPA039588; -.
HPA; HPA043888; -.
MalaCards; HADH; -.
MIM; 231530; phenotype.
MIM; 601609; gene.
MIM; 609975; phenotype.
neXtProt; NX_Q16836; -.
OpenTargets; ENSG00000138796; -.
Orphanet; 71212; Hyperinsulinism due to short chain 3-hydroxylacyl-CoA dehydrogenase deficiency.
PharmGKB; PA29173; -.
GeneTree; ENSGT00880000137923; -.
HOGENOM; HOG000141498; -.
HOVERGEN; HBG000832; -.
InParanoid; Q16836; -.
KO; K00022; -.
PhylomeDB; Q16836; -.
TreeFam; TF300886; -.
BioCyc; MetaCyc:HS06563-MONOMER; -.
BRENDA; 1.1.1.35; 2681.
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.
Reactome; R-HSA-77352; Beta oxidation of butanoyl-CoA to acetyl-CoA.
SABIO-RK; Q16836; -.
UniPathway; UPA00659; -.
ChiTaRS; HADH; human.
EvolutionaryTrace; Q16836; -.
GeneWiki; Hydroxyacyl-Coenzyme_A_dehydrogenase; -.
GenomeRNAi; 3033; -.
PRO; PR:Q16836; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000138796; -.
CleanEx; HS_HADH; -.
ExpressionAtlas; Q16836; baseline and differential.
Genevisible; Q16836; HS.
GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; TAS:Reactome.
GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
GO; GO:0006635; P:fatty acid beta-oxidation; TAS:Reactome.
GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
Gene3D; 1.10.1040.10; -; 1.
InterPro; IPR022694; 3-OHacyl-CoA_DH.
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; IPR013328; 6PGD_dom2.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF00725; 3HCDH; 1.
Pfam; PF02737; 3HCDH_N; 1.
PIRSF; PIRSF000105; HCDH; 1.
SUPFAM; SSF48179; SSF48179; 1.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00067; 3HCDH; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Disease mutation; Fatty acid metabolism; Lipid metabolism;
Mitochondrion; NAD; Oxidoreductase; Polymorphism; Reference proteome;
Transit peptide.
TRANSIT 1 12 Mitochondrion.
CHAIN 13 314 Hydroxyacyl-coenzyme A dehydrogenase,
mitochondrial.
/FTId=PRO_0000007406.
NP_BIND 34 39 NAD. {ECO:0000269|PubMed:10231530,
ECO:0000269|PubMed:10840044}.
BINDING 57 57 NAD. {ECO:0000269|PubMed:10231530,
ECO:0000269|PubMed:10840044}.
BINDING 73 73 Coenzyme A.
BINDING 80 80 Coenzyme A.
BINDING 122 122 NAD. {ECO:0000269|PubMed:10231530,
ECO:0000269|PubMed:10840044}.
BINDING 127 127 NAD. {ECO:0000269|PubMed:10231530,
ECO:0000269|PubMed:10840044}.
BINDING 149 149 Coenzyme A.
BINDING 149 149 NAD. {ECO:0000269|PubMed:10231530,
ECO:0000269|PubMed:10840044}.
BINDING 173 173 NAD. {ECO:0000269|PubMed:10231530,
ECO:0000269|PubMed:10840044}.
BINDING 305 305 NAD. {ECO:0000269|PubMed:10231530,
ECO:0000269|PubMed:10840044}.
SITE 170 170 Important for catalytic activity.
{ECO:0000305}.
MOD_RES 80 80 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q61425}.
MOD_RES 81 81 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q61425}.
MOD_RES 81 81 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q61425}.
MOD_RES 87 87 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q61425}.
MOD_RES 87 87 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q61425}.
MOD_RES 125 125 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q61425}.
MOD_RES 136 136 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q61425}.
MOD_RES 136 136 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q61425}.
MOD_RES 179 179 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q61425}.
MOD_RES 185 185 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 185 185 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q61425}.
MOD_RES 192 192 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q61425}.
MOD_RES 192 192 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q61425}.
MOD_RES 202 202 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 202 202 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q61425}.
MOD_RES 206 206 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q61425}.
MOD_RES 212 212 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q61425}.
MOD_RES 212 212 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q61425}.
MOD_RES 241 241 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 241 241 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q61425}.
MOD_RES 312 312 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 312 312 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q61425}.
VAR_SEQ 1 1 M -> MGRAGLEAPPPPCGVTGTPGARGLQGRVGPRPQSLA
FRGCLPRASSLPGSPRCRRRCHTM (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_016551.
VAR_SEQ 236 236 R -> RDFQTCGDSNSGLGFSLK (in isoform 2 and
isoform 3). {ECO:0000303|Ref.2}.
/FTId=VSP_016552.
VARIANT 40 40 A -> T (in HADH deficiency;
dbSNP:rs137853101). {ECO:0000269|Ref.13}.
/FTId=VAR_024079.
VARIANT 57 57 D -> E (in HADH deficiency;
dbSNP:rs137853102). {ECO:0000269|Ref.13}.
/FTId=VAR_024080.
VARIANT 86 86 L -> P (in dbSNP:rs4956145).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8687463,
ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
/FTId=VAR_026764.
VARIANT 152 152 Q -> H (in dbSNP:rs1051519).
{ECO:0000269|PubMed:8687463}.
/FTId=VAR_055701.
VARIANT 258 258 P -> L (in HHF4; loss of activity;
dbSNP:rs137853103).
{ECO:0000269|PubMed:11489939}.
/FTId=VAR_024081.
HELIX 1 11 {ECO:0000244|PDB:3RQS}.
HELIX 14 22 {ECO:0000244|PDB:3RQS}.
STRAND 29 33 {ECO:0000244|PDB:1F0Y}.
HELIX 37 48 {ECO:0000244|PDB:1F0Y}.
STRAND 52 56 {ECO:0000244|PDB:1F0Y}.
HELIX 60 79 {ECO:0000244|PDB:1F0Y}.
STRAND 82 84 {ECO:0000244|PDB:1F0Y}.
HELIX 86 98 {ECO:0000244|PDB:1F0Y}.
STRAND 100 104 {ECO:0000244|PDB:1F0Y}.
HELIX 106 109 {ECO:0000244|PDB:1F0Y}.
HELIX 110 112 {ECO:0000244|PDB:3HAD}.
STRAND 114 118 {ECO:0000244|PDB:1F0Y}.
HELIX 124 134 {ECO:0000244|PDB:1F0Y}.
TURN 135 137 {ECO:0000244|PDB:1F0Y}.
STRAND 143 146 {ECO:0000244|PDB:1F0Y}.
STRAND 149 151 {ECO:0000244|PDB:1F0Y}.
HELIX 153 157 {ECO:0000244|PDB:1F0Y}.
HELIX 163 165 {ECO:0000244|PDB:1F0Y}.
STRAND 166 171 {ECO:0000244|PDB:1F0Y}.
TURN 175 177 {ECO:0000244|PDB:1F0Y}.
STRAND 180 184 {ECO:0000244|PDB:1F0Y}.
HELIX 191 203 {ECO:0000244|PDB:1F0Y}.
STRAND 207 211 {ECO:0000244|PDB:1F0Y}.
TURN 215 218 {ECO:0000244|PDB:1F0Y}.
HELIX 219 235 {ECO:0000244|PDB:1F0Y}.
HELIX 241 252 {ECO:0000244|PDB:1F0Y}.
HELIX 258 265 {ECO:0000244|PDB:1F0Y}.
HELIX 267 279 {ECO:0000244|PDB:1F0Y}.
TURN 280 283 {ECO:0000244|PDB:1F0Y}.
HELIX 285 287 {ECO:0000244|PDB:1F0Y}.
HELIX 291 298 {ECO:0000244|PDB:1F0Y}.
TURN 304 307 {ECO:0000244|PDB:1F0Y}.
STRAND 308 312 {ECO:0000244|PDB:1F0Y}.
SEQUENCE 314 AA; 34294 MW; 0C6F7C01BBCE646A CRC64;
MAFVTRQFMR SVSSSSTASA SAKKIIVKHV TVIGGGLMGA GIAQVAAATG HTVVLVDQTE
DILAKSKKGI EESLRKVAKK KFAENLKAGD EFVEKTLSTI ATSTDAASVV HSTDLVVEAI
VENLKVKNEL FKRLDKFAAE HTIFASNTSS LQITSIANAT TRQDRFAGLH FFNPVPVMKL
VEVIKTPMTS QKTFESLVDF SKALGKHPVS CKDTPGFIVN RLLVPYLMEA IRLYERGDAS
KEDIDTAMKL GAGYPMGPFE LLDYVGLDTT KFIVDGWHEM DAENPLHQPS PSLNKLVAEN
KFGKKTGEGF YKYK


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