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Peroxisomal multifunctional enzyme type 2 (MFE-2) (17-beta-hydroxysteroid dehydrogenase 4) (17-beta-HSD 4) (D-bifunctional protein) (DBP) (Multifunctional protein 2) (MPF-2) (Short chain dehydrogenase/reductase family 8C member 1) [Cleaved into: (3R)-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.n12); Enoyl-CoA hydratase 2 (EC 4.2.1.107) (EC 4.2.1.119) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase)]

 DHB4_HUMAN              Reviewed;         736 AA.
P51659; B4DNV1; B4DVS5; E9PB82; F5HE57;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 193.
RecName: Full=Peroxisomal multifunctional enzyme type 2;
Short=MFE-2;
AltName: Full=17-beta-hydroxysteroid dehydrogenase 4;
Short=17-beta-HSD 4;
AltName: Full=D-bifunctional protein;
Short=DBP;
AltName: Full=Multifunctional protein 2;
Short=MPF-2;
AltName: Full=Short chain dehydrogenase/reductase family 8C member 1;
Contains:
RecName: Full=(3R)-hydroxyacyl-CoA dehydrogenase;
EC=1.1.1.n12;
Contains:
RecName: Full=Enoyl-CoA hydratase 2;
EC=4.2.1.107;
EC=4.2.1.119;
AltName: Full=3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase;
Name=HSD17B4; Synonyms=EDH17B4, SDR8C1;
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).
TISSUE=Liver;
PubMed=7487879; DOI=10.1042/bj3110437;
Adamski J., Normand T., Leenders F., Monte D., Begue A., Stehelin D.,
Jungblut P.W., de Launoit Y.;
"Molecular cloning of a novel widely expressed human 80 kDa 17 beta-
hydroxysteroid dehydrogenase IV.";
Biochem. J. 311:437-443(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 69-77;
81-90; 261-270; 291-310; 312-339; 413-426; 451-459; 478-488 AND
590-631, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=9089413; DOI=10.1093/oxfordjournals.jbchem.a021596;
Jiang L.L., Miyazawa S., Souri M., Hashimoto T.;
"Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA
dehydrogenase bifunctional protein.";
J. Biochem. 121:364-369(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9880674; DOI=10.1007/s003359900921;
Leenders F., Dolez V., Begue A., Moller G., Gloeckner J.C.,
de Launoit Y., Adamski J.;
"Structure of the gene for the human 17beta-hydroxysteroid
dehydrogenase type IV.";
Mamm. Genome 9:1036-1041(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
VARIANTS HIS-106 AND VAL-559.
TISSUE=Lung, and Spleen;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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]
FUNCTION, AND SUBUNIT.
PubMed=8902629; DOI=10.1093/oxfordjournals.jbchem.a021458;
Jiang L.L., Kobayashi A., Matsuura H., Fukushima H., Hashimoto T.;
"Purification and properties of human D-3-hydroxyacyl-CoA dehydratase:
medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase.";
J. Biochem. 120:624-632(1996).
[8]
MUTAGENESIS OF TYR-347; GLU-366; ASP-370; HIS-406; GLU-408; TYR-410;
ASP-490; TYR-505; ASP-510; HIS-515; ASP-517 AND HIS-532, AND
CHARACTERIZATION OF VARIANT DBPD SER-16.
PubMed=10671535; DOI=10.1074/jbc.275.7.4965;
Qin Y.M., Haapalainen A.M., Kilpelainen S.H., Marttila M.S.,
Koski M.K., Glumoff T., Novikov D.K., Hiltunen J.K.;
"Human peroxisomal multifunctional enzyme type 2. Site-directed
mutagenesis studies show the importance of two protic residues for 2-
enoyl-CoA hydratase 2 activity.";
J. Biol. Chem. 275:4965-4972(2000).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-309, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-565; LYS-669 AND LYS-707,
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).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-265, 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, 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).
[15]
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).
[16]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 618-736 IN COMPLEX WITH
LIGAND.
PubMed=11700068; DOI=10.1006/jmbi.2001.5084;
Haapalainen A.M., van Aalten D.M., Merilaeinen G., Jalonen J.E.,
Pirilae P., Wierenga R.K., Hiltunen J.K., Glumoff T.;
"Crystal structure of the liganded SCP-2-like domain of human
peroxisomal multifunctional enzyme type 2 at 1.75 A resolution.";
J. Mol. Biol. 313:1127-1138(2001).
[17]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 320-614.
PubMed=15644212; DOI=10.1016/j.jmb.2004.11.009;
Koski K.M., Haapalainen A.M., Hiltunen J.K., Glumoff T.;
"Crystal structure of 2-enoyl-CoA hydratase 2 from human peroxisomal
multifunctional enzyme type 2.";
J. Mol. Biol. 345:1157-1169(2005).
[18]
VARIANT DBPD SER-16.
PubMed=9482850; DOI=10.1073/pnas.95.5.2128;
van Grunsven E.G., van Berkel E., Ijlst L., Vreken P.,
de Klerk J.B.C., Adamski J., Lemonde H., Clayton P.T., Cuebas D.A.,
Wanders R.J.A.;
"Peroxisomal D-hydroxyacyl-CoA dehydrogenase deficiency: resolution of
the enzyme defect and its molecular basis in bifunctional protein
deficiency.";
Proc. Natl. Acad. Sci. U.S.A. 95:2128-2133(1998).
[19]
VARIANT DBPD TYR-457, AND VARIANT ARG-511.
PubMed=10400999; DOI=10.1093/hmg/8.8.1509;
van Grunsven E.G., Mooijer P.A., Aubourg P., Wanders R.J.;
"Enoyl-CoA hydratase deficiency: identification of a new type of D-
bifunctional protein deficiency.";
Hum. Mol. Genet. 8:1509-1516(1999).
[20]
VARIANT DBPD PRO-106.
PubMed=11743515; DOI=10.1067/mpd.2001.119170;
Nakano K., Zhang Z., Shimozawa N., Kondo N., Ishii N., Funatsuka M.,
Shirakawa S., Itoh M., Takashima S., Une M., Kana-aki R.R., Mukai K.,
Osawa M., Suzuki Y.;
"D-bifunctional protein deficiency with fetal ascites, polyhydramnios,
and contractures of hands and toes.";
J. Pediatr. 139:865-867(2001).
[21]
VARIANT PRLTS1 CYS-217.
PubMed=20673864; DOI=10.1016/j.ajhg.2010.07.007;
Pierce S.B., Walsh T., Chisholm K.M., Lee M.K., Thornton A.M.,
Fiumara A., Opitz J.M., Levy-Lahad E., Klevit R.E., King M.C.;
"Mutations in the DBP-deficiency protein HSD17B4 cause ovarian
dysgenesis, hearing loss, and ataxia of Perrault Syndrome.";
Am. J. Hum. Genet. 87:282-288(2010).
[22]
VARIANTS HIS-106 AND VAL-559.
PubMed=25956234; DOI=10.1016/j.jns.2015.04.038;
Ahmed S., Jelani M., Alrayes N., Mohamoud H.S., Almramhi M.M.,
Anshasi W., Ahmed N.A., Wang J., Nasir J., Al-Aama J.Y.;
"Exome analysis identified a novel missense mutation in the CLPP gene
in a consanguineous Saudi family expanding the clinical spectrum of
Perrault Syndrome type-3.";
J. Neurol. Sci. 353:149-154(2015).
-!- FUNCTION: Bifunctional enzyme acting on the peroxisomal beta-
oxidation pathway for fatty acids. Catalyzes the formation of 3-
ketoacyl-CoA intermediates from both straight-chain and 2-methyl-
branched-chain fatty acids. {ECO:0000269|PubMed:8902629,
ECO:0000269|PubMed:9089413}.
-!- CATALYTIC ACTIVITY: (R)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
+ NADH. {ECO:0000269|PubMed:9089413}.
-!- CATALYTIC ACTIVITY: (24R,25R)-3-alpha,7-alpha,12-alpha,24-
tetrahydroxy-5-beta-cholestanoyl-CoA = (24E)-3-alpha,7-alpha,12-
alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA + H(2)O.
{ECO:0000269|PubMed:9089413}.
-!- CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-CoA = (2E)-2-enoyl-CoA +
H(2)O. {ECO:0000269|PubMed:9089413}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=10 uM for D-3-hydroxy-octanoyl-CoA
{ECO:0000269|PubMed:9089413};
KM=13 uM for NAD {ECO:0000269|PubMed:9089413};
KM=2.7 uM for 3-ketooctanoyl-CoA {ECO:0000269|PubMed:9089413};
KM=5.4 uM for NADH {ECO:0000269|PubMed:9089413};
Vmax=8.8 umol/min/mg enzyme {ECO:0000269|PubMed:9089413};
-!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11700068,
ECO:0000269|PubMed:8902629}.
-!- SUBCELLULAR LOCATION: Peroxisome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P51659-1; Sequence=Displayed;
Name=2;
IsoId=P51659-2; Sequence=VSP_046152;
Note=No experimental confirmation available.;
Name=3;
IsoId=P51659-3; Sequence=VSP_046153;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Present in many tissues with highest
concentrations in liver, heart, prostate and testis.
-!- DISEASE: D-bifunctional protein deficiency (DBPD) [MIM:261515]:
Disorder of peroxisomal fatty acid beta-oxidation.
{ECO:0000269|PubMed:10400999, ECO:0000269|PubMed:10671535,
ECO:0000269|PubMed:11743515, ECO:0000269|PubMed:9482850}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Perrault syndrome 1 (PRLTS1) [MIM:233400]: A sex-
influenced disorder characterized by sensorineural deafness in
both males and females and ovarian dysgenesis in females. Some
patients also have neurologic manifestations, including mild
mental retardation and cerebellar and peripheral nervous system
involvement. {ECO:0000269|PubMed:20673864}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: The protein is found both as a full-length peptide
and in a cleaved version.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
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EMBL; X87176; CAA60643.1; -; mRNA.
EMBL; AF057740; AAD08652.1; -; Genomic_DNA.
EMBL; AF057720; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AF057721; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AF057722; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AF057723; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AF057724; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AF057725; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AF057726; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AF057727; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AF057728; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AF057729; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AF057730; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AF057731; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AF057732; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AF057733; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AF057734; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AF057735; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AF057736; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AF057737; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AF057738; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AF057739; AAD08652.1; JOINED; Genomic_DNA.
EMBL; AK298075; BAG60363.1; -; mRNA.
EMBL; AK301212; BAG62787.1; -; mRNA.
EMBL; AC024564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC003098; AAH03098.1; -; mRNA.
CCDS; CCDS4126.1; -. [P51659-1]
CCDS; CCDS56378.1; -. [P51659-3]
CCDS; CCDS56379.1; -. [P51659-2]
PIR; S59136; S59136.
RefSeq; NP_000405.1; NM_000414.3. [P51659-1]
RefSeq; NP_001186220.1; NM_001199291.2. [P51659-2]
RefSeq; NP_001186221.1; NM_001199292.1. [P51659-3]
RefSeq; NP_001278956.1; NM_001292027.1.
RefSeq; NP_001278957.1; NM_001292028.1.
UniGene; Hs.406861; -.
PDB; 1IKT; X-ray; 1.75 A; A=618-736.
PDB; 1S9C; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=318-615.
PDB; 1ZBQ; X-ray; 2.71 A; A/B/C/D/E/F=1-304.
PDBsum; 1IKT; -.
PDBsum; 1S9C; -.
PDBsum; 1ZBQ; -.
ProteinModelPortal; P51659; -.
SMR; P51659; -.
BioGrid; 109528; 49.
IntAct; P51659; 36.
MINT; P51659; -.
STRING; 9606.ENSP00000420914; -.
ChEMBL; CHEMBL5814; -.
DrugBank; DB03192; 3r-Hydroxydecanoyl-Coa.
DrugBank; DB00157; NADH.
SwissLipids; SLP:000000540; -.
iPTMnet; P51659; -.
PhosphoSitePlus; P51659; -.
SwissPalm; P51659; -.
BioMuta; HSD17B4; -.
DMDM; 1706396; -.
EPD; P51659; -.
MaxQB; P51659; -.
PaxDb; P51659; -.
PeptideAtlas; P51659; -.
PRIDE; P51659; -.
TopDownProteomics; P51659-1; -. [P51659-1]
DNASU; 3295; -.
Ensembl; ENST00000256216; ENSP00000256216; ENSG00000133835. [P51659-1]
Ensembl; ENST00000504811; ENSP00000420914; ENSG00000133835. [P51659-2]
Ensembl; ENST00000515320; ENSP00000424613; ENSG00000133835. [P51659-3]
GeneID; 3295; -.
KEGG; hsa:3295; -.
UCSC; uc003ksj.4; human. [P51659-1]
CTD; 3295; -.
DisGeNET; 3295; -.
EuPathDB; HostDB:ENSG00000133835.14; -.
GeneCards; HSD17B4; -.
H-InvDB; HIX0078166; -.
HGNC; HGNC:5213; HSD17B4.
HPA; HPA021302; -.
HPA; HPA021311; -.
HPA; HPA021479; -.
MalaCards; HSD17B4; -.
MIM; 233400; phenotype.
MIM; 261515; phenotype.
MIM; 601860; gene.
neXtProt; NX_P51659; -.
OpenTargets; ENSG00000133835; -.
Orphanet; 300; Bifunctional enzyme deficiency.
Orphanet; 2855; Perrault syndrome.
PharmGKB; PA29481; -.
eggNOG; KOG1206; Eukaryota.
eggNOG; COG2030; LUCA.
GeneTree; ENSGT00530000062928; -.
HOGENOM; HOG000170895; -.
HOVERGEN; HBG002174; -.
InParanoid; P51659; -.
KO; K12405; -.
OMA; SRMTQTV; -.
OrthoDB; EOG091G02S9; -.
PhylomeDB; P51659; -.
TreeFam; TF105656; -.
BioCyc; MetaCyc:HS05792-MONOMER; -.
BRENDA; 4.2.1.119; 2681.
Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-HSA-2046106; alpha-linolenic acid (ALA) metabolism.
Reactome; R-HSA-389887; Beta-oxidation of pristanoyl-CoA.
Reactome; R-HSA-390247; Beta-oxidation of very long chain fatty acids.
Reactome; R-HSA-9033241; Peroxisomal protein import.
Reactome; R-HSA-9033500; TYSND1 cleaves peroxisomal proteins.
SABIO-RK; P51659; -.
UniPathway; UPA00659; -.
ChiTaRS; HSD17B4; human.
EvolutionaryTrace; P51659; -.
GeneWiki; HSD17B4; -.
GenomeRNAi; 3295; -.
PRO; PR:P51659; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000133835; -.
CleanEx; HS_HSD17B4; -.
ExpressionAtlas; P51659; baseline and differential.
Genevisible; P51659; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
GO; GO:0005778; C:peroxisomal membrane; HDA:UniProtKB.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IDA:UniProtKB.
GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IDA:UniProtKB.
GO; GO:0033989; F:3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity; TAS:Reactome.
GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
GO; GO:0016508; F:long-chain-enoyl-CoA hydratase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
GO; GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
GO; GO:0008209; P:androgen metabolic process; IDA:UniProtKB.
GO; GO:0006699; P:bile acid biosynthetic process; TAS:Reactome.
GO; GO:0008210; P:estrogen metabolic process; IDA:UniProtKB.
GO; GO:0006635; P:fatty acid beta-oxidation; IDA:UniProtKB.
GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome.
GO; GO:0036112; P:medium-chain fatty-acyl-CoA metabolic process; IDA:UniProtKB.
GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
GO; GO:0006625; P:protein targeting to peroxisome; TAS:Reactome.
GO; GO:0036111; P:very long-chain fatty-acyl-CoA metabolic process; IDA:UniProtKB.
Gene3D; 3.30.1050.10; -; 1.
InterPro; IPR029069; HotDog_dom_sf.
InterPro; IPR002539; MaoC_dom.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR003033; SCP2_sterol-bd_dom.
InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
InterPro; IPR002347; SDR_fam.
Pfam; PF00106; adh_short; 1.
Pfam; PF01575; MaoC_dehydratas; 1.
Pfam; PF02036; SCP2; 1.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF54637; SSF54637; 2.
SUPFAM; SSF55718; SSF55718; 1.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Deafness; Direct protein sequencing; Disease mutation;
Fatty acid metabolism; Isomerase; Lipid metabolism; Lyase; NAD;
Oxidoreductase; Peroxisome; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 736 Peroxisomal multifunctional enzyme type
2.
/FTId=PRO_0000054583.
CHAIN 1 311 (3R)-hydroxyacyl-CoA dehydrogenase.
/FTId=PRO_0000400082.
CHAIN 312 736 Enoyl-CoA hydratase 2.
/FTId=PRO_0000400083.
DOMAIN 484 600 MaoC-like.
DOMAIN 624 736 SCP2.
NP_BIND 13 37 NAD. {ECO:0000250}.
NP_BIND 75 76 NAD.
NP_BIND 164 168 NAD.
NP_BIND 196 199 NAD.
REGION 1 305 (3R)-hydroxyacyl-CoA dehydrogenase.
REGION 322 622 Enoyl-CoA hydratase 2.
REGION 406 407 (3R)-3-hydroxydecanoyl-CoA binding.
{ECO:0000250}.
REGION 510 515 (3R)-3-hydroxydecanoyl-CoA binding.
{ECO:0000250}.
MOTIF 734 736 Microbody targeting signal.
{ECO:0000255}.
ACT_SITE 164 164 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10001}.
BINDING 21 21 NAD; via amide nitrogen.
BINDING 40 40 NAD.
BINDING 99 99 NAD; via carbonyl oxygen.
BINDING 151 151 Substrate. {ECO:0000250}.
BINDING 435 435 (3R)-3-hydroxydecanoyl-CoA.
{ECO:0000250}.
BINDING 533 533 (3R)-3-hydroxydecanoyl-CoA; via amide
nitrogen. {ECO:0000250}.
BINDING 563 563 (3R)-3-hydroxydecanoyl-CoA; via carbonyl
oxygen. {ECO:0000250}.
BINDING 706 706 Substrate.
BINDING 724 724 Substrate.
MOD_RES 46 46 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 46 46 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 52 52 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 57 57 N6-succinyllysine.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 68 68 N6-succinyllysine.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 84 84 N6-succinyllysine.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 265 265 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 275 275 N6-succinyllysine.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 309 309 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 356 356 N6-succinyllysine.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 424 424 N6-succinyllysine.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 565 565 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 579 579 N6-succinyllysine.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 663 663 N6-succinyllysine.
{ECO:0000250|UniProtKB:P51660}.
MOD_RES 669 669 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 707 707 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 725 725 N6-succinyllysine.
{ECO:0000250|UniProtKB:P51660}.
VAR_SEQ 1 38 MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVV ->
MVILEAPHLLRRKEPETPGLSSRIGPSLCPGFCRKRSVSCC
FQNLCNNPMEKIISQCRFFVSM (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046152.
VAR_SEQ 20 37 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046153.
VARIANT 16 16 G -> S (in DBPD; no dehydrogenase
activity; dbSNP:rs137853096).
{ECO:0000269|PubMed:10671535,
ECO:0000269|PubMed:9482850}.
/FTId=VAR_037576.
VARIANT 90 90 F -> L (in dbSNP:rs28943588).
/FTId=VAR_052309.
VARIANT 106 106 R -> H (in dbSNP:rs25640).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:25956234}.
/FTId=VAR_014872.
VARIANT 106 106 R -> P (in DBPD; dbSNP:rs25640).
{ECO:0000269|PubMed:11743515}.
/FTId=VAR_065906.
VARIANT 140 140 K -> N (in dbSNP:rs28943589).
/FTId=VAR_052310.
VARIANT 217 217 Y -> C (in PRLTS1; dbSNP:rs387906825).
{ECO:0000269|PubMed:20673864}.
/FTId=VAR_065907.
VARIANT 292 292 T -> S (in dbSNP:rs1143650).
/FTId=VAR_024625.
VARIANT 427 427 A -> V (in dbSNP:rs28943590).
/FTId=VAR_052311.
VARIANT 457 457 N -> Y (in DBPD; the mutation leads to an
unstable protein; dbSNP:rs137853097).
{ECO:0000269|PubMed:10400999}.
/FTId=VAR_065908.
VARIANT 491 491 A -> T (in dbSNP:rs28943591).
/FTId=VAR_052312.
VARIANT 511 511 W -> R (in dbSNP:rs11539471).
{ECO:0000269|PubMed:10400999}.
/FTId=VAR_014873.
VARIANT 559 559 I -> V (in dbSNP:rs11205).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:25956234}.
/FTId=VAR_014874.
VARIANT 606 606 A -> S (in dbSNP:rs15228).
/FTId=VAR_052313.
VARIANT 687 687 T -> I (in dbSNP:rs28943592).
/FTId=VAR_052314.
VARIANT 728 728 M -> V (in dbSNP:rs28943594).
/FTId=VAR_052315.
MUTAGEN 347 347 Y->A: No hydratase activity.
{ECO:0000269|PubMed:10671535}.
MUTAGEN 366 366 E->A: No hydratase activity.
{ECO:0000269|PubMed:10671535}.
MUTAGEN 370 370 D->A: No effect.
{ECO:0000269|PubMed:10671535}.
MUTAGEN 406 406 H->A: No effect.
{ECO:0000269|PubMed:10671535}.
MUTAGEN 408 408 E->A: No effect.
{ECO:0000269|PubMed:10671535}.
MUTAGEN 410 410 Y->A: No effect.
{ECO:0000269|PubMed:10671535}.
MUTAGEN 490 490 D->A: No effect.
{ECO:0000269|PubMed:10671535}.
MUTAGEN 505 505 Y->A: Completely inactive.
{ECO:0000269|PubMed:10671535}.
MUTAGEN 510 510 D->A: No hydratase activity.
{ECO:0000269|PubMed:10671535}.
MUTAGEN 515 515 H->A: Completely inactive.
{ECO:0000269|PubMed:10671535}.
MUTAGEN 517 517 D->A: No effect.
{ECO:0000269|PubMed:10671535}.
MUTAGEN 532 532 H->A: No effect.
{ECO:0000269|PubMed:10671535}.
CONFLICT 587 587 Q -> R (in Ref. 4; BAG60363).
{ECO:0000305}.
STRAND 11 14 {ECO:0000244|PDB:1ZBQ}.
TURN 15 18 {ECO:0000244|PDB:1ZBQ}.
HELIX 20 31 {ECO:0000244|PDB:1ZBQ}.
STRAND 35 39 {ECO:0000244|PDB:1ZBQ}.
HELIX 53 64 {ECO:0000244|PDB:1ZBQ}.
STRAND 68 72 {ECO:0000244|PDB:1ZBQ}.
HELIX 76 78 {ECO:0000244|PDB:1ZBQ}.
HELIX 79 90 {ECO:0000244|PDB:1ZBQ}.
STRAND 95 98 {ECO:0000244|PDB:1ZBQ}.
HELIX 108 110 {ECO:0000244|PDB:1ZBQ}.
HELIX 113 141 {ECO:0000244|PDB:1ZBQ}.
STRAND 144 149 {ECO:0000244|PDB:1ZBQ}.
HELIX 152 156 {ECO:0000244|PDB:1ZBQ}.
HELIX 162 182 {ECO:0000244|PDB:1ZBQ}.
HELIX 183 185 {ECO:0000244|PDB:1ZBQ}.
STRAND 187 194 {ECO:0000244|PDB:1ZBQ}.
TURN 199 204 {ECO:0000244|PDB:1ZBQ}.
HELIX 207 212 {ECO:0000244|PDB:1ZBQ}.
HELIX 215 217 {ECO:0000244|PDB:1ZBQ}.
HELIX 219 225 {ECO:0000244|PDB:1ZBQ}.
STRAND 236 240 {ECO:0000244|PDB:1ZBQ}.
STRAND 243 251 {ECO:0000244|PDB:1ZBQ}.
HELIX 266 271 {ECO:0000244|PDB:1ZBQ}.
HELIX 273 277 {ECO:0000244|PDB:1ZBQ}.
HELIX 288 303 {ECO:0000244|PDB:1ZBQ}.
STRAND 335 339 {ECO:0000244|PDB:1S9C}.
HELIX 341 350 {ECO:0000244|PDB:1S9C}.
HELIX 358 360 {ECO:0000244|PDB:1S9C}.
HELIX 361 364 {ECO:0000244|PDB:1S9C}.
HELIX 375 377 {ECO:0000244|PDB:1S9C}.
HELIX 378 381 {ECO:0000244|PDB:1S9C}.
HELIX 383 385 {ECO:0000244|PDB:1S9C}.
HELIX 401 403 {ECO:0000244|PDB:1S9C}.
STRAND 405 415 {ECO:0000244|PDB:1S9C}.
STRAND 419 432 {ECO:0000244|PDB:1S9C}.
STRAND 440 462 {ECO:0000244|PDB:1S9C}.
STRAND 490 496 {ECO:0000244|PDB:1S9C}.
HELIX 501 505 {ECO:0000244|PDB:1S9C}.
HELIX 506 508 {ECO:0000244|PDB:1S9C}.
HELIX 513 515 {ECO:0000244|PDB:1S9C}.
HELIX 518 522 {ECO:0000244|PDB:1S9C}.
TURN 523 525 {ECO:0000244|PDB:1S9C}.
HELIX 533 548 {ECO:0000244|PDB:1S9C}.
HELIX 553 555 {ECO:0000244|PDB:1S9C}.
STRAND 556 563 {ECO:0000244|PDB:1S9C}.
STRAND 572 580 {ECO:0000244|PDB:1S9C}.
STRAND 583 590 {ECO:0000244|PDB:1S9C}.
TURN 591 593 {ECO:0000244|PDB:1S9C}.
STRAND 596 605 {ECO:0000244|PDB:1S9C}.
HELIX 624 646 {ECO:0000244|PDB:1IKT}.
STRAND 648 670 {ECO:0000244|PDB:1IKT}.
STRAND 674 679 {ECO:0000244|PDB:1IKT}.
STRAND 685 691 {ECO:0000244|PDB:1IKT}.
HELIX 692 699 {ECO:0000244|PDB:1IKT}.
HELIX 705 710 {ECO:0000244|PDB:1IKT}.
STRAND 713 719 {ECO:0000244|PDB:1IKT}.
HELIX 720 733 {ECO:0000244|PDB:1IKT}.
SEQUENCE 736 AA; 79686 MW; 7B11E02483328BCE CRC64;
MGSPLRFDGR VVLVTGAGAG LGRAYALAFA ERGALVVVND LGGDFKGVGK GSLAADKVVE
EIRRRGGKAV ANYDSVEEGE KVVKTALDAF GRIDVVVNNA GILRDRSFAR ISDEDWDIIH
RVHLRGSFQV TRAAWEHMKK QKYGRIIMTS SASGIYGNFG QANYSAAKLG LLGLANSLAI
EGRKSNIHCN TIAPNAGSRM TQTVMPEDLV EALKPEYVAP LVLWLCHESC EENGGLFEVG
AGWIGKLRWE RTLGAIVRQK NHPMTPEAVK ANWKKICDFE NASKPQSIQE STGSIIEVLS
KIDSEGGVSA NHTSRATSTA TSGFAGAIGQ KLPPFSYAYT ELEAIMYALG VGASIKDPKD
LKFIYEGSSD FSCLPTFGVI IGQKSMMGGG LAEIPGLSIN FAKVLHGEQY LELYKPLPRA
GKLKCEAVVA DVLDKGSGVV IIMDVYSYSE KELICHNQFS LFLVGSGGFG GKRTSDKVKV
AVAIPNRPPD AVLTDTTSLN QAALYRLSGD WNPLHIDPNF ASLAGFDKPI LHGLCTFGFS
ARRVLQQFAD NDVSRFKAIK ARFAKPVYPG QTLQTEMWKE GNRIHFQTKV QETGDIVISN
AYVDLAPTSG TSAKTPSEGG KLQSTFVFEE IGRRLKDIGP EVVKKVNAVF EWHITKGGNI
GAKWTIDLKS GSGKVYQGPA KGAADTTIIL SDEDFMEVVL GKLDPQKAFF SGRLKARGNI
MLSQKLQMIL KDYAKL


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