Reviewed, UniProtKB/Swiss-Prot P51660 (DHB4_MOUSE)

Names and origin

Protein names

Recommended name:
    Peroxisomal multifunctional enzyme type 2
      Short name=MFE-2
Alternative name(s):
    D-bifunctional protein
      Short name=DBP
    17-beta-hydroxysteroid dehydrogenase 4
      Short name=17-beta-HSD 4
Including the following 2 domains:
    1- Recommended name:
            3-hydroxyacyl-CoA dehydrogenase
              EC=1.1.1.35
    2- Recommended name:
            3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase
              EC=4.2.1.107

Gene names

Name:	Hsd17b4
Synonyms:	Edh17b4

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	735 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

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 By similarity.
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 + H2O. (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Subcellular location	Peroxisome By similarity.
Tissue specificity	Present in many tissues with highest concentrations in liver and kidney.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family. Contains 1 SCP2 domain.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Ligand	NAD
Molecular function	Isomerase Lyase Oxidoreductase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	Sertoli cell development Inferred from mutant phenotype. Source: MGI fatty acid beta-oxidation Inferred from mutant phenotype. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW very-long-chain fatty acid metabolic process Inferred from mutant phenotype. Source: MGI
Cellular component	mitochondrion Inferred from direct assay. Source: MGI peroxisome Inferred from direct assay. Source: MGI
Molecular function	3-hydroxyacyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: EC 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity Inferred from electronic annotation. Source: EC isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW sterol carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 735	734	Peroxisomal multifunctional enzyme type 2		PRO_0000054584
Regions
	Domain	623 – 735	113	SCP2
	Nucleotide binding	13 – 37	25	NAD By similarity
	Nucleotide binding	75 – 76	2	NAD By similarity
	Nucleotide binding	164 – 168	5	NAD By similarity
	Nucleotide binding	196 – 199	4	NAD By similarity
	Region	2 – 305	304	3-hydroxyacyl-CoA dehydrogenase
	Region	321 – 621	301	3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase
Sites
	Active site	164	1	Proton acceptor By similarity
	Binding site	21	1	NAD; via amide nitrogen By similarity
	Binding site	40	1	NAD By similarity
	Binding site	99	1	NAD; via carbonyl oxygen By similarity
	Binding site	151	1	Substrate By similarity
	Binding site	705	1	Substrate By similarity
	Binding site	723	1	Substrate By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.5
	Modified residue	3	1	Phosphoserine Ref.5
	Modified residue	265	1	Phosphothreonine By similarity
	Modified residue	308	1	Phosphoserine Ref.6
	Modified residue	662	1	N6-acetyllysine Ref.4
Experimental info
	Sequence conflict	17	1	A → P in CAA62015. Ref.1
	Sequence conflict	417	1	P → L in CAA62015. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P51660-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: AD7804FE93EB9BA8	FASTA	735	79,482
	10 20 30 40 50 60 MASPLRFDGR VVLVTGAGGG LGRAYALAFA ERGALVIVND LGGDFKGIGK GSSAADKVVA 70 80 90 100 110 120 EIRRKGGKAV ANYDSVEAGE KLVKTALDTF GRIDVVVNNA GILRDRSFSR ISDEDWDIIH 130 140 150 160 170 180 RVHLRGSFQV TRAAWDHMKK QNYGRILMTS SASGIYGNFG QANYSAAKLG ILGLCNTLAI 190 200 210 220 230 240 EGRKNNIHCN TIAPNAGSRM TETVLPEDLV EALKPEYVAP LVLWLCHESC EENGGLFEVG 250 260 270 280 290 300 AGWIGKLRWE RTLGAIVRKR NQPMTPEAVR DNWEKICDFS NASKPQTIQE STGGIVEVLH 310 320 330 340 350 360 KVDSEGISPN RTSHAAPAAT SGFVGAVGHK LPSFSSSYTE LQSIMYALGV GASVKNPKDL 370 380 390 400 410 420 KFVYEGSADF SCLPTFGVIV AQKSMMNGGL AEVPGLSFNF AKALHGEQYL ELYKPLPRSG 430 440 450 460 470 480 ELKCEAVIAD ILDKGSGVVI VMDVYSYSGK ELICYNQFSV FVVGSGGFGG KRTSEKLKAA 490 500 510 520 530 540 VAVPNRPPDA VLRDATSLNQ AALYRLSGDW NPLHIDPDFA SVAGFEKPIL HGLCTFGFSA 550 560 570 580 590 600 RHVLQQFADN DVSRFKAIKV RFAKPVYPGQ TLQTEMWKEG NRIHFQTKVH ETGDVVISNA 610 620 630 640 650 660 YVDLVPASGV STQTPSEGGE LQSALVFGEI GRRLKSVGRE VVKKANAVFE WHITKGGTVA 670 680 690 700 710 720 AKWTIDLKSG SGEVYQGPAK GSADVTIIIS DEDFMEVVFG KLDPQKAFFS GRLKARGNIM 730 LSQKLQMILK DYAKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of mouse 17 beta-hydroxysteroid dehydrogenase IV." Normand T., Husen B., Leenders F., Pelczar H., Baert J.-L., Begue A., Flourens A.C., Adamski J., de Launoit Y. J. Steroid Biochem. Mol. Biol. 55:541-548(1995) [PubMed: 8547180] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Amnion, Liver and Thymus.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Colon.
[4]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-662, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed: 16452087] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION AT SER-3, MASS SPECTROMETRY. Tissue: Brain.
[6]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X89998 mRNA. Translation: CAA62015.1. AK004866 mRNA. Translation: BAB23627.1. AK088381 mRNA. Translation: BAC40317.1. AK166801 mRNA. Translation: BAE39029.1. AK167060 mRNA. Translation: BAE39222.1. AK169077 mRNA. Translation: BAE40862.1. BC022175 mRNA. Translation: AAH22175.1.
IPI	IPI00331628.
RefSeq	NP_032318.2.
UniGene	Mm.277857
3D structure databases
HSSP	HSSP built from PDB template 1GZ6 based on UniProtKB P97852.
SMR	P51660. Positions 3-303, 322-604, 621-735.
ModBase	Search...
PTM databases
PhosphoSite	P51660.
Proteomic databases
PRIDE	P51660.
Genome annotation databases
Ensembl	ENSMUSG00000024507. Mus musculus. [Contig view]
GeneID	15488.
KEGG	mmu:15488.
Organism-specific databases
MGI	MGI:105089. Hsd17b4.
Phylogenomic databases
HOGENOM	P51660.
HOVERGEN	P51660.
OMA	P51660. NQPMTPE.
Enzyme and pathway databases
BRENDA	1.1.1.35. 244. 4.2.1.107. 244.
Gene expression databases
ArrayExpress	P51660.
Bgee	P51660.
CleanEx	MM_HSD17B4.
GermOnline	ENSMUSG00000024507. Mus musculus.
Family and domain databases
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR002539. MaoC_deHydtase. IPR016040. NAD(P)-bd_dom. IPR003033. SCP2_sterol_bd. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR19410. ADH_short_C2. 1 hit.
Pfam	PF00106. adh_short. 1 hit. PF01575. MaoC_dehydratas. 1 hit. PF02036. SCP2. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
PROSITE	PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	288358.
SOURCE	Search...

Entry information

Entry name

DHB4_MOUSE

Accession

Primary (citable) accession number: P51660
Secondary accession number(s): Q9DBM3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 78 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)