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P51660

- DHB4_MOUSE

UniProt

P51660 - DHB4_MOUSE

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Protein

Peroxisomal multifunctional enzyme type 2

Gene

Hsd17b4

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).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 nitrogenBy similarity
Binding sitei40 – 401NADBy similarity
Binding sitei99 – 991NAD; via carbonyl oxygenBy similarity
Binding sitei151 – 1511SubstrateBy similarity
Active sitei164 – 1641Proton acceptorPROSITE-ProRule annotation
Binding sitei434 – 4341(3R)-3-hydroxydecanoyl-CoABy similarity
Binding sitei532 – 5321(3R)-3-hydroxydecanoyl-CoA; via amide nitrogenBy similarity
Binding sitei562 – 5621(3R)-3-hydroxydecanoyl-CoA; via carbonyl oxygenBy similarity
Binding sitei705 – 7051SubstrateBy similarity
Binding sitei723 – 7231SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 3725NADBy similarityAdd
BLAST
Nucleotide bindingi75 – 762NADBy similarity
Nucleotide bindingi164 – 1685NADBy similarity
Nucleotide bindingi196 – 1994NADBy 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. osteoblast differentiation Source: Ensembl
  6. Sertoli cell development Source: MGI
  7. very long-chain fatty acid metabolic process Source: MGI
  8. 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 – 3041PhosphoserineBy 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-acetyllysineBy 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.
ModBaseiSearch...
MobiDBiSearch...

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 bindingBy similarity
Regioni509 – 5146(3R)-3-hydroxydecanoyl-CoA bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi733 – 7353Microbody targeting signalSequence Analysis

Sequence similaritiesi

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

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

        10         20         30         40         50
MASPLRFDGR VVLVTGAGGG LGRAYALAFA ERGALVIVND LGGDFKGIGK
60 70 80 90 100
GSSAADKVVA EIRRKGGKAV ANYDSVEAGE KLVKTALDTF GRIDVVVNNA
110 120 130 140 150
GILRDRSFSR ISDEDWDIIH RVHLRGSFQV TRAAWDHMKK QNYGRILMTS
160 170 180 190 200
SASGIYGNFG QANYSAAKLG ILGLCNTLAI EGRKNNIHCN TIAPNAGSRM
210 220 230 240 250
TETVLPEDLV EALKPEYVAP LVLWLCHESC EENGGLFEVG AGWIGKLRWE
260 270 280 290 300
RTLGAIVRKR NQPMTPEAVR DNWEKICDFS NASKPQTIQE STGGIVEVLH
310 320 330 340 350
KVDSEGISPN RTSHAAPAAT SGFVGAVGHK LPSFSSSYTE LQSIMYALGV
360 370 380 390 400
GASVKNPKDL KFVYEGSADF SCLPTFGVIV AQKSMMNGGL AEVPGLSFNF
410 420 430 440 450
AKALHGEQYL ELYKPLPRSG ELKCEAVIAD ILDKGSGVVI VMDVYSYSGK
460 470 480 490 500
ELICYNQFSV FVVGSGGFGG KRTSEKLKAA VAVPNRPPDA VLRDATSLNQ
510 520 530 540 550
AALYRLSGDW NPLHIDPDFA SVAGFEKPIL HGLCTFGFSA RHVLQQFADN
560 570 580 590 600
DVSRFKAIKV RFAKPVYPGQ TLQTEMWKEG NRIHFQTKVH ETGDVVISNA
610 620 630 640 650
YVDLVPASGV STQTPSEGGE LQSALVFGEI GRRLKSVGRE VVKKANAVFE
660 670 680 690 700
WHITKGGTVA AKWTIDLKSG SGEVYQGPAK GSADVTIIIS DEDFMEVVFG
710 720 730
KLDPQKAFFS GRLKARGNIM LSQKLQMILK DYAKL
Length:735
Mass (Da):79,482
Last modified:January 23, 2007 - v3
Checksum:iAD7804FE93EB9BA8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171A → P in CAA62015. (PubMed:8547180)Curated
Sequence conflicti417 – 4171P → L in CAA62015. (PubMed:8547180)Curated

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: October 29, 2014
This is version 129 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