ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P51660


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name DHB4_MOUSE
Primary accession number P51660
Secondary accession number Q9DBM3
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 74)
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
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0960-0760(95)00204-9; PubMed=8547180 [NCBI, ExPASy, EBI, Israel, Japan]
Normand T., Husen B., Leenders F., Pelczar H., Baert J.-L., Begue A., Flourens A.C., Adamski J., de Launoit Y.;
"Molecular characterization of mouse 17 beta-hydroxysteroid dehydrogenase IV.";
J. Steroid Biochem. Mol. Biol. 55:541-548(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Amnion, Liver, and Thymus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Colon;
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).
[4]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-662, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.";
Mol. Cell 23:607-618(2006).
[5]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION AT SER-3, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1074/mcp.T500041-MCP200; PubMed=16452087 [NCBI, ExPASy, EBI, Israel, Japan]
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1073/pnas.0609836104; PubMed=17242355 [NCBI, ExPASy, EBI, Israel, Japan]
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
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
X89998; CAA62015.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK004866; BAB23627.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK088381; BAC40317.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK166801; BAE39029.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK167060; BAE39222.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK169077; BAE40862.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC022175; AAH22175.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_032318.2; -.
UniGene Mm.277857
3D structure databases
HSSP P97852; 1GZ6. [HSSP ENTRY / PDB]
SMR P51660; 3-303, 322-604, 621-735.
ModBase P51660.
PTM databases
PhosphoSite P51660; -.
Organism-specific databases
MGI MGI:105089; Hsd17b4.
Gene expression databases
ArrayExpress P51660; -.
CleanEx MM_HSD17B4; -.
GermOnline ENSMUSG00000024507; Mus musculus.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from MGI).
GO:0005777; Cellular component: peroxisome (inferred from direct assay from MGI).
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:0016853; Molecular function: isomerase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005498; Molecular function: sterol carrier activity (inferred from electronic annotation from InterPro).
GO:0006635; Biological process: fatty acid beta-oxidation (inferred from mutant phenotype from MGI).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0060009; Biological process: Sertoli cell development (inferred from mutant phenotype from MGI).
GO:0000038; Biological process: very-long-chain fatty acid metabolic process (inferred from mutant phenotype from MGI).
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.
Proteomics databases
PRIDE P51660; -.
Genome annotation databases
Ensembl ENSMUSG00000024507; Mus musculus. [Contig view]
GeneID 15488; -.
KEGG mmu:15488; -.
Phylogenomic databases
HOGENOM P51660; -.
HOVERGEN P51660; -.
Other
NextBio 288358; -.
SOURCE Hsd17b4; Mus musculus.
ProtoNet P51660.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Fatty acid metabolism; Isomerase; Lipid metabolism; Lyase; NAD; Oxidoreductase; Peroxisome; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   735  734     Peroxisomal multifunctional enzyme type 2. PRO_0000054584
DOMAIN   623   735  113     SCP2. 
NP_BIND   13    37  25     NAD (By similarity). 
NP_BIND   75    76  2     NAD (By similarity). 
NP_BIND   164   168  5     NAD (By similarity). 
NP_BIND   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. 
ACT_SITE   164   164        Proton acceptor (By similarity). 
BINDING   21    21        NAD; via amide nitrogen (By similarity). 
BINDING   40    40        NAD (By similarity). 
BINDING   99    99        NAD; via carbonyl oxygen (By similarity). 
BINDING   151   151        Substrate (By similarity). 
BINDING   705   705        Substrate (By similarity). 
BINDING   723   723        Substrate (By similarity). 
MOD_RES   2     2        N-acetylalanine. 
MOD_RES   3     3        Phosphoserine. 
MOD_RES   265   265        Phosphothreonine (By similarity). 
MOD_RES   308   308        Phosphoserine. 
MOD_RES   662   662        N6-acetyllysine. 
CONFLICT   17    17        A -> P (in Ref. 1; CAA62015). 
CONFLICT   417   417        P -> L (in Ref. 1; CAA62015). 
Sequence information
Length: 735 AA [This is the length of the unprocessed precursor] Molecular weight: 79482 Da [This is the MW of the unprocessed precursor] CRC64: AD7804FE93EB9BA8 [This is a checksum on the sequence]
        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 

P51660 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!