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UniProtKB/Swiss-Prot entry P51659


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DHB4_HUMAN
Primary accession number P51659
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    December 16, 2008 (Entry version 92)
Name and origin of the protein
Protein name Peroxisomal multifunctional enzyme type 2
Synonyms MFE-2
D-bifunctional protein
DBP
17-beta-hydroxysteroid dehydrogenase 4
17-beta-HSD 4
Includes 3-hydroxyacyl-CoA dehydrogenase
     (EC 1.1.1.35)
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase
     (EC 4.2.1.107)
Gene name
Name: HSD17B4
Synonyms: EDH17B4
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=7487879 [NCBI, ExPASy, EBI, Israel, Japan]
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], AND FUNCTION.
PubMed=9089413 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1007/s003359900921; PubMed=9880674 [NCBI, ExPASy, EBI, Israel, Japan]
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].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
CHARACTERIZATION.
PubMed=8902629 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-265, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[7]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 618-736 IN COMPLEX WITH LIGAND.
DOI=10.1006/jmbi.2001.5084; PubMed=11700068 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 320-614.
DOI=10.1016/j.jmb.2004.11.009; PubMed=15644212 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
VARIANT DBPD SER-16.
DOI=10.1073/pnas.95.5.2128; PubMed=9482850 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X87176; CAA60643.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057740; AAD08652.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057720; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057721; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057722; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057723; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057724; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057725; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057726; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057727; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057728; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057729; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057730; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057731; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057732; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057733; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057734; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057735; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057736; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057737; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057738; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057739; AAD08652.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003098; AAH03098.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S59136; S59136.
RefSeq NP_000405.1; -.
UniGene Hs.406861
3D structure databases
PDB
1IKT; X-ray; 1.75 A; A=618-736.[ExPASy / RCSB / EBI]
1S9C; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=320-614.[ExPASy / RCSB / EBI]
1ZBQ; X-ray; 2.71 A; A/B/C/D/E/F=1-304.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1IKT; -.
1S9C; -.
1ZBQ; -.
ModBase P51659.
Protein-protein interaction databases
IntAct P51659; 3.
PTM databases
PhosphoSite P51659; -.
Enzyme and pathway databases
Reactome REACT_602; Lipid and lipoprotein metabolism.
Organism-specific databases
GeneCards GC05P118816; -.
H-InvDB HIX0005116; -.
HGNC HGNC:5213; HSD17B4.
GenAtlas HSD17B4.
MIM 261515; phenotype. [NCBI / EBI]
601860; gene. [NCBI / EBI]
Orphanet 300; Bifunctional enzyme deficiency.
2981; Pseudo-Zellweger syndrome.
PharmGKB PA29481; -.
GeneCards P51659.
Gene expression databases
ArrayExpress P51659; -.
CleanEx HS_HSD17B4; -.
GermOnline ENSG00000133835; Homo sapiens.
Ontologies
GO
GO:0005782; Cellular component: peroxisomal matrix (inferred from experiment from Reactome).
GO:0003857; Molecular function: 3-hydroxyacyl-CoA dehydrogenase activity (inferred from electronic annotation from EC).
GO:0033989; Molecular function: 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity (inferred from electronic annotation from EC).
GO:0004303; Molecular function: estradiol 17-beta-dehydrogenase activity (traceable author statement from ProtInc).
GO:0016853; Molecular function: isomerase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0005498; Molecular function: sterol carrier activity (traceable author statement from ProtInc).
GO:0015248; Molecular function: sterol transporter activity (traceable author statement from ProtInc).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR002539; MaoC_deHydtase.
IPR016040; NAD(P)-bd.
IPR003033; SCP2_sterol_bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR19410; ADH_short_C2; 1.
Pfam PF00106; adh_short; 1.
PF01575; MaoC_dehydratas; 1.
PF02036; SCP2; 1.
Pfam graphical view of domain structure.
PRINTS PR00081; GDHRDH.
PR00080; SDRFAMILY.
PROSITE PS00061; ADH_SHORT; 1.
Proteomic databases
PeptideAtlas P51659; -.
Proteomics databases
PRIDE P51659; -.
Genome annotation databases
Ensembl ENSG00000133835; Homo sapiens. [Contig view]
GeneID 3295; -.
KEGG hsa:3295; -.
Phylogenomic databases
HOGENOM P51659; -.
HOVERGEN P51659; -.
Other
DrugBank DB00157; NADH.
LinkHub P51659; -.
NextBio 13071; -.
SOURCE HSD17B4; Homo sapiens.
ProtoNet P51659.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Disease mutation; Fatty acid metabolism; Isomerase; Lipid metabolism; Lyase; NAD; Oxidoreductase; Peroxisome; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   736  735     Peroxisomal multifunctional enzyme type 2. PRO_0000054583
DOMAIN   624   736  113     SCP2. 
NP_BIND   13    37  25     NAD (By similarity). 
NP_BIND   75    76  2     NAD. 
NP_BIND   164   168  5     NAD. 
NP_BIND   196   199  4     NAD. 
REGION   2   305  304     3-hydroxyacyl-CoA dehydrogenase. 
REGION   322   622  301     3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase. 
ACT_SITE   164   164        Proton acceptor (By similarity). 
BINDING   21    21        NAD; via amide nitrogen. 
BINDING   40    40        NAD. 
BINDING   99    99        NAD; via carbonyl oxygen. 
BINDING   151   151        Substrate (By similarity). 
BINDING   706   706        Substrate. 
BINDING   724   724        Substrate. 
MOD_RES   3     3        Phosphoserine (By similarity). 
MOD_RES   265   265        Phosphothreonine. 
MOD_RES   309   309        Phosphoserine (By similarity). 
MOD_RES   663   663        N6-acetyllysine (By similarity). 
VARIANT   16    16  1     G -> S (in DBPD). VAR_037576 
VARIANT   90    90  1     F -> L (in dbSNP:rs28943588 [NCBI]). VAR_052309 
VARIANT   106   106  1     R -> H (in dbSNP:rs25640 [NCBI]). VAR_014872 
VARIANT   140   140  1     K -> N (in dbSNP:rs28943589 [NCBI]). VAR_052310 
VARIANT   292   292  1     T -> S (in dbSNP:rs1143650 [NCBI]). VAR_024625 
VARIANT   427   427  1     A -> V (in dbSNP:rs28943590 [NCBI]). VAR_052311 
VARIANT   491   491  1     A -> T (in dbSNP:rs28943591 [NCBI]). VAR_052312 
VARIANT   511   511  1     W -> R (in dbSNP:rs11539471 [NCBI]). VAR_014873 
VARIANT   559   559  1     I -> V (in dbSNP:rs11205 [NCBI]). VAR_014874 
VARIANT   606   606  1     A -> S (in dbSNP:rs15228 [NCBI]). VAR_052313 
VARIANT   687   687  1     T -> I (in dbSNP:rs28943592 [NCBI]). VAR_052314 [3D]
VARIANT   728   728  1     M -> V (in dbSNP:rs28943594 [NCBI]). VAR_052315 [3D]
STRAND   11    14  4      
TURN   15    18  4      
HELIX   20    31  12      
STRAND   35    39  5      
HELIX   53    64  12      
STRAND   68    72  5      
HELIX   76    78  3      
HELIX   79    90  12      
STRAND   95    98  4      
HELIX   108   110  3      
HELIX   113   141  29      
STRAND   144   149  6      
HELIX   152   156  5      
HELIX   162   182  21      
HELIX   183   185  3      
STRAND   187   194  8      
TURN   199   204  6      
HELIX   207   212  6      
HELIX   215   217  3      
HELIX   219   225  7      
STRAND   236   240  5      
STRAND   243   251  9      
HELIX   266   271  6      
HELIX   273   277  5      
HELIX   288   303  16      
STRAND   335   339  5      
HELIX   341   350  10      
HELIX   358   360  3      
HELIX   361   364  4      
HELIX   375   377  3      
HELIX   378   381  4      
HELIX   383   385  3      
STRAND   405   415  11      
STRAND   419   432  14      
STRAND   440   462  23      
STRAND   490   496  7      
HELIX   501   505  5      
HELIX   506   508  3      
HELIX   513   515  3      
HELIX   518   522  5      
TURN   523   525  3      
HELIX   533   548  16      
HELIX   553   555  3      
STRAND   556   563  8      
STRAND   572   580  9      
STRAND   583   590  8      
TURN   591   593  3      
STRAND   596   605  10      
HELIX   624   646  23      
STRAND   648   670  23      
STRAND   674   679  6      
STRAND   685   691  7      
HELIX   692   699  8      
HELIX   705   710  6      
STRAND   713   719  7