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P51660 (DHB4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisomal multifunctional enzyme type 2

Short name=MFE-2
Alternative name(s):
17-beta-hydroxysteroid dehydrogenase 4
Short name=17-beta-HSD 4
D-bifunctional protein
Short name=DBP
Multifunctional protein 2
Short name=MPF-2

Cleaved into the following 2 chains:

  1. (3R)-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.n12
  2. Enoyl-CoA hydratase 2
    EC=4.2.1.107
    EC=4.2.1.119
    Alternative name(s):
    3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase
Gene names
Name:Hsd17b4
Synonyms:Edh17b4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length735 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

(R)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.

(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.

(3R)-3-hydroxyacyl-CoA = (2E)-2-enoyl-CoA + H2O.

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Homodimer By similarity.

Subcellular location

Peroxisome By similarity.

Tissue specificity

Present in many tissues with highest concentrations in liver and kidney.

Miscellaneous

The protein is found both as a full length peptide and in a cleaved version By similarity.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Contains 1 MaoC-like domain.

Contains 1 SCP2 domain.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentPeroxisome
   LigandNAD
   Molecular functionIsomerase
Lyase
Oxidoreductase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSertoli cell development

Inferred from mutant phenotype PubMed 16484321. Source: MGI

androgen metabolic process

Inferred from electronic annotation. Source: Ensembl

estrogen metabolic process

Inferred from electronic annotation. Source: Ensembl

fatty acid beta-oxidation

Inferred from mutant phenotype PubMed 17442273. Source: MGI

medium-chain fatty-acyl-CoA metabolic process

Inferred from electronic annotation. Source: Ensembl

very long-chain fatty acid metabolic process

Inferred from mutant phenotype PubMed 16484321. Source: MGI

very long-chain fatty-acyl-CoA metabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentmitochondrion

Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI

peroxisomal membrane

Inferred from electronic annotation. Source: Ensembl

peroxisome

Inferred from direct assay PubMed 12897163. Source: MGI

   Molecular_function17-beta-hydroxysteroid dehydrogenase (NAD+) activity

Inferred from electronic annotation. Source: Ensembl

3-hydroxyacyl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: Ensembl

3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity

Inferred from electronic annotation. Source: UniProtKB-EC

isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

long-chain-enoyl-CoA hydratase activity

Inferred from electronic annotation. Source: Ensembl

sterol binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 735735Peroxisomal multifunctional enzyme type 2
PRO_0000054584
Chain1 – 311311(3R)-hydroxyacyl-CoA dehydrogenase
PRO_0000400084
Chain312 – 735424Enoyl-CoA hydratase 2
PRO_0000400085

Regions

Domain483 – 599117MaoC-like
Domain623 – 735113SCP2
Nucleotide binding13 – 3725NAD By similarity
Nucleotide binding75 – 762NAD By similarity
Nucleotide binding164 – 1685NAD By similarity
Nucleotide binding196 – 1994NAD By similarity
Region1 – 305305(3R)-hydroxyacyl-CoA dehydrogenase
Region321 – 621301Enoyl-CoA hydratase 2
Region405 – 4062(3R)-3-hydroxydecanoyl-CoA binding By similarity
Region509 – 5146(3R)-3-hydroxydecanoyl-CoA binding By similarity
Motif733 – 7353Microbody targeting signal Potential

Sites

Active site1641Proton acceptor By similarity
Binding site211NAD; via amide nitrogen By similarity
Binding site401NAD By similarity
Binding site991NAD; via carbonyl oxygen By similarity
Binding site1511Substrate By similarity
Binding site4341(3R)-3-hydroxydecanoyl-CoA By similarity
Binding site5321(3R)-3-hydroxydecanoyl-CoA; via amide nitrogen By similarity
Binding site5621(3R)-3-hydroxydecanoyl-CoA; via carbonyl oxygen By similarity
Binding site7051Substrate By similarity
Binding site7231Substrate By similarity

Amino acid modifications

Modified residue461N6-acetyllysine; alternate Ref.6
Modified residue461N6-succinyllysine; alternate Ref.5
Modified residue571N6-succinyllysine Ref.5
Modified residue681N6-succinyllysine Ref.5
Modified residue841N6-succinyllysine Ref.5
Modified residue2751N6-succinyllysine Ref.5
Modified residue3041Phosphoserine By similarity
Modified residue3081Phosphoserine Ref.4
Modified residue3551N6-succinyllysine Ref.5
Modified residue4231N6-succinyllysine Ref.5
Modified residue5641N6-acetyllysine Ref.6
Modified residue5781N6-succinyllysine Ref.5
Modified residue6621N6-succinyllysine Ref.5
Modified residue6681N6-acetyllysine By similarity
Modified residue7061N6-acetyllysine Ref.6
Modified residue7241N6-succinyllysine Ref.5

Experimental info

Sequence conflict171A → P in CAA62015. Ref.1
Sequence conflict4171P → L in CAA62015. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P51660 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: AD7804FE93EB9BA8

FASTA73579,482
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Colon.
[4]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-46; LYS-57; LYS-68; LYS-84; LYS-275; LYS-355; LYS-423; LYS-578; LYS-662 AND LYS-724, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-46; LYS-564 AND LYS-706, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS29242.1.
RefSeqNP_032318.2. NM_008292.4.
UniGeneMm.277857.

3D structure databases

ProteinModelPortalP51660.
SMRP51660. Positions 3-303, 322-604, 621-735.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200435. 1 interaction.
IntActP51660. 5 interactions.
MINTMINT-2512164.

PTM databases

PhosphoSiteP51660.

Proteomic databases

MaxQBP51660.
PaxDbP51660.
PRIDEP51660.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025385; ENSMUSP00000025385; ENSMUSG00000024507.
GeneID15488.
KEGGmmu:15488.
UCSCuc008eww.2. mouse.

Organism-specific databases

CTD3295.
MGIMGI:105089. Hsd17b4.

Phylogenomic databases

eggNOGCOG1028.
GeneTreeENSGT00530000062928.
HOGENOMHOG000170895.
HOVERGENHBG002174.
InParanoidP51660.
KOK12405.
OMATETIMPP.
OrthoDBEOG7RBZ7V.
PhylomeDBP51660.
TreeFamTF105656.

Enzyme and pathway databases

UniPathwayUPA00659.

Gene expression databases

BgeeP51660.
CleanExMM_HSD17B4.
GenevestigatorP51660.

Family and domain databases

Gene3D3.10.129.10. 2 hits.
3.30.1050.10. 1 hit.
3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR029069. HotDog_dom.
IPR002539. MaoC_dom.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR003033. SCP2_sterol-bd_dom.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
PF02036. SCP2. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMSSF54637. SSF54637. 2 hits.
SSF55718. SSF55718. 1 hit.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHSD17B4. mouse.
NextBio288358.
PROP51660.
SOURCESearch...

Entry information

Entry nameDHB4_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot