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P51660

- DHB4_MOUSE

UniProt

P51660 - DHB4_MOUSE

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Protein

Peroxisomal multifunctional enzyme type 2

Gene
Hsd17b4, Edh17b4
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

(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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211NAD; via amide nitrogen By similarity
Binding sitei40 – 401NAD By similarity
Binding sitei99 – 991NAD; via carbonyl oxygen By similarity
Binding sitei151 – 1511Substrate By similarity
Active sitei164 – 1641Proton acceptor By similarity
Binding sitei434 – 4341(3R)-3-hydroxydecanoyl-CoA By similarity
Binding sitei532 – 5321(3R)-3-hydroxydecanoyl-CoA; via amide nitrogen By similarity
Binding sitei562 – 5621(3R)-3-hydroxydecanoyl-CoA; via carbonyl oxygen By similarity
Binding sitei705 – 7051Substrate By similarity
Binding sitei723 – 7231Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 3725NAD By similarityAdd
BLAST
Nucleotide bindingi75 – 762NAD By similarity
Nucleotide bindingi164 – 1685NAD By similarity
Nucleotide bindingi196 – 1994NAD By similarity

GO - Molecular functioni

  1. 17-beta-hydroxysteroid dehydrogenase (NAD+) activity Source: Ensembl
  2. 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity Source: UniProtKB-EC
  3. 3-hydroxyacyl-CoA dehydrogenase activity Source: Ensembl
  4. isomerase activity Source: UniProtKB-KW
  5. long-chain-enoyl-CoA hydratase activity Source: Ensembl

GO - Biological processi

  1. androgen metabolic process Source: Ensembl
  2. estrogen metabolic process Source: Ensembl
  3. fatty acid beta-oxidation Source: MGI
  4. medium-chain fatty-acyl-CoA metabolic process Source: Ensembl
  5. Sertoli cell development Source: MGI
  6. very long-chain fatty acid metabolic process Source: MGI
  7. very long-chain fatty-acyl-CoA metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiREACT_196541. alpha-linolenic acid (ALA) metabolism.
REACT_203193. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended 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:
Alternative name(s):
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase
Gene namesi
Name:Hsd17b4
Synonyms:Edh17b4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:105089. Hsd17b4.

Subcellular locationi

Peroxisome By similarity

GO - Cellular componenti

  1. mitochondrion Source: MGI
  2. peroxisomal membrane Source: Ensembl
  3. peroxisome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 735735Peroxisomal multifunctional enzyme type 2PRO_0000054584Add
BLAST
Chaini1 – 311311(3R)-hydroxyacyl-CoA dehydrogenasePRO_0000400084Add
BLAST
Chaini312 – 735424Enoyl-CoA hydratase 2PRO_0000400085Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461N6-acetyllysine; alternate1 Publication
Modified residuei46 – 461N6-succinyllysine; alternate1 Publication
Modified residuei57 – 571N6-succinyllysine1 Publication
Modified residuei68 – 681N6-succinyllysine1 Publication
Modified residuei84 – 841N6-succinyllysine1 Publication
Modified residuei275 – 2751N6-succinyllysine1 Publication
Modified residuei304 – 3041Phosphoserine By similarity
Modified residuei308 – 3081Phosphoserine1 Publication
Modified residuei355 – 3551N6-succinyllysine1 Publication
Modified residuei423 – 4231N6-succinyllysine1 Publication
Modified residuei564 – 5641N6-acetyllysine1 Publication
Modified residuei578 – 5781N6-succinyllysine1 Publication
Modified residuei662 – 6621N6-succinyllysine1 Publication
Modified residuei668 – 6681N6-acetyllysine By similarity
Modified residuei706 – 7061N6-acetyllysine1 Publication
Modified residuei724 – 7241N6-succinyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP51660.
PaxDbiP51660.
PRIDEiP51660.

PTM databases

PhosphoSiteiP51660.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP51660.
CleanExiMM_HSD17B4.
GenevestigatoriP51660.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

BioGridi200435. 1 interaction.
IntActiP51660. 5 interactions.
MINTiMINT-2512164.

Structurei

3D structure databases

ProteinModelPortaliP51660.
SMRiP51660. Positions 3-303, 322-604, 621-735.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini483 – 599117MaoC-likeAdd
BLAST
Domaini623 – 735113SCP2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 305305(3R)-hydroxyacyl-CoA dehydrogenaseAdd
BLAST
Regioni321 – 621301Enoyl-CoA hydratase 2Add
BLAST
Regioni405 – 4062(3R)-3-hydroxydecanoyl-CoA binding By similarity
Regioni509 – 5146(3R)-3-hydroxydecanoyl-CoA binding By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi733 – 7353Microbody targeting signal Reviewed prediction

Sequence similaritiesi

Contains 1 MaoC-like domain.
Contains 1 SCP2 domain.

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00530000062928.
HOGENOMiHOG000170895.
HOVERGENiHBG002174.
InParanoidiP51660.
KOiK12405.
OMAiTETIMPP.
OrthoDBiEOG7RBZ7V.
PhylomeDBiP51660.
TreeFamiTF105656.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
3.30.1050.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR002198. 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]
PfamiPF00106. adh_short. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
PF02036. SCP2. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF54637. SSF54637. 2 hits.
SSF55718. SSF55718. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P51660-1 [UniParc]FASTAAdd to Basket

« Hide

MASPLRFDGR VVLVTGAGGG LGRAYALAFA ERGALVIVND LGGDFKGIGK    50
GSSAADKVVA EIRRKGGKAV ANYDSVEAGE KLVKTALDTF GRIDVVVNNA 100
GILRDRSFSR ISDEDWDIIH RVHLRGSFQV TRAAWDHMKK QNYGRILMTS 150
SASGIYGNFG QANYSAAKLG ILGLCNTLAI EGRKNNIHCN TIAPNAGSRM 200
TETVLPEDLV EALKPEYVAP LVLWLCHESC EENGGLFEVG AGWIGKLRWE 250
RTLGAIVRKR NQPMTPEAVR DNWEKICDFS NASKPQTIQE STGGIVEVLH 300
KVDSEGISPN RTSHAAPAAT SGFVGAVGHK LPSFSSSYTE LQSIMYALGV 350
GASVKNPKDL KFVYEGSADF SCLPTFGVIV AQKSMMNGGL AEVPGLSFNF 400
AKALHGEQYL ELYKPLPRSG ELKCEAVIAD ILDKGSGVVI VMDVYSYSGK 450
ELICYNQFSV FVVGSGGFGG KRTSEKLKAA VAVPNRPPDA VLRDATSLNQ 500
AALYRLSGDW NPLHIDPDFA SVAGFEKPIL HGLCTFGFSA RHVLQQFADN 550
DVSRFKAIKV RFAKPVYPGQ TLQTEMWKEG NRIHFQTKVH ETGDVVISNA 600
YVDLVPASGV STQTPSEGGE LQSALVFGEI GRRLKSVGRE VVKKANAVFE 650
WHITKGGTVA AKWTIDLKSG SGEVYQGPAK GSADVTIIIS DEDFMEVVFG 700
KLDPQKAFFS GRLKARGNIM LSQKLQMILK DYAKL 735
Length:735
Mass (Da):79,482
Last modified:January 23, 2007 - v3
Checksum:iAD7804FE93EB9BA8
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171A → P in CAA62015. 1 Publication
Sequence conflicti417 – 4171P → L in CAA62015. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS29242.1.
RefSeqiNP_032318.2. NM_008292.4.
UniGeneiMm.277857.

Genome annotation databases

EnsembliENSMUST00000025385; ENSMUSP00000025385; ENSMUSG00000024507.
GeneIDi15488.
KEGGimmu:15488.
UCSCiuc008eww.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS29242.1.
RefSeqi NP_032318.2. NM_008292.4.
UniGenei Mm.277857.

3D structure databases

ProteinModelPortali P51660.
SMRi P51660. Positions 3-303, 322-604, 621-735.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200435. 1 interaction.
IntActi P51660. 5 interactions.
MINTi MINT-2512164.

PTM databases

PhosphoSitei P51660.

Proteomic databases

MaxQBi P51660.
PaxDbi P51660.
PRIDEi P51660.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025385 ; ENSMUSP00000025385 ; ENSMUSG00000024507 .
GeneIDi 15488.
KEGGi mmu:15488.
UCSCi uc008eww.2. mouse.

Organism-specific databases

CTDi 3295.
MGIi MGI:105089. Hsd17b4.

Phylogenomic databases

eggNOGi COG1028.
GeneTreei ENSGT00530000062928.
HOGENOMi HOG000170895.
HOVERGENi HBG002174.
InParanoidi P51660.
KOi K12405.
OMAi TETIMPP.
OrthoDBi EOG7RBZ7V.
PhylomeDBi P51660.
TreeFami TF105656.

Enzyme and pathway databases

UniPathwayi UPA00659 .
Reactomei REACT_196541. alpha-linolenic acid (ALA) metabolism.
REACT_203193. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.

Miscellaneous databases

ChiTaRSi HSD17B4. mouse.
NextBioi 288358.
PROi P51660.
SOURCEi Search...

Gene expression databases

Bgeei P51660.
CleanExi MM_HSD17B4.
Genevestigatori P51660.

Family and domain databases

Gene3Di 3.10.129.10. 2 hits.
3.30.1050.10. 1 hit.
3.40.50.720. 1 hit.
InterProi IPR002198. 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 ]
Pfami PF00106. adh_short. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
PF02036. SCP2. 1 hit.
[Graphical view ]
PRINTSi PR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMi SSF54637. SSF54637. 2 hits.
SSF55718. SSF55718. 1 hit.
PROSITEi PS00061. ADH_SHORT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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] [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. 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.

Entry informationi

Entry nameiDHB4_MOUSE
AccessioniPrimary (citable) accession number: P51660
Secondary accession number(s): Q9DBM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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