Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P97852

- DHB4_RAT

UniProt

P97852 - DHB4_RAT

Protein

Peroxisomal multifunctional enzyme type 2

Gene

Hsd17b4

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.

    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 – 1511Substrate
    Active sitei164 – 1641Proton acceptor
    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 bindingi16 – 4025NAD1 PublicationAdd
    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
    6. testosterone dehydrogenase [NAD(P)] activity Source: RGD

    GO - Biological processi

    1. androgen metabolic process Source: Ensembl
    2. cholesterol metabolic process Source: RGD
    3. estrogen metabolic process Source: Ensembl
    4. fatty acid beta-oxidation Source: UniProtKB-UniPathway
    5. medium-chain fatty-acyl-CoA metabolic process Source: Ensembl
    6. Sertoli cell development Source: Ensembl
    7. very long-chain fatty acid metabolic process Source: Ensembl
    8. very long-chain fatty-acyl-CoA metabolic process Source: Ensembl

    Keywords - Molecular functioni

    Isomerase, Lyase, Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14329.
    ReactomeiREACT_198818. alpha-linolenic acid (ALA) metabolism.
    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 18

    Organism-specific databases

    RGDi621806. Hsd17b4.

    Subcellular locationi

    Peroxisome 1 Publication

    GO - Cellular componenti

    1. mitochondrion Source: Ensembl
    2. peroxisomal membrane Source: Ensembl
    3. peroxisome Source: HGNC

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 735735Peroxisomal multifunctional enzyme type 2PRO_0000054585Add
    BLAST
    Chaini1 – 311311(3R)-hydroxyacyl-CoA dehydrogenasePRO_0000400086Add
    BLAST
    Chaini312 – 735424Enoyl-CoA hydratase 2PRO_0000400087Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei46 – 461N6-acetyllysine; alternateBy similarity
    Modified residuei46 – 461N6-succinyllysine; alternateBy similarity
    Modified residuei57 – 571N6-succinyllysineBy similarity
    Modified residuei68 – 681N6-succinyllysineBy similarity
    Modified residuei84 – 841N6-succinyllysineBy similarity
    Modified residuei275 – 2751N6-succinyllysineBy similarity
    Modified residuei304 – 3041PhosphoserineBy similarity
    Modified residuei308 – 3081PhosphoserineBy similarity
    Modified residuei355 – 3551N6-succinyllysineBy similarity
    Modified residuei423 – 4231N6-succinyllysineBy similarity
    Modified residuei564 – 5641N6-acetyllysineBy similarity
    Modified residuei578 – 5781N6-succinyllysineBy similarity
    Modified residuei662 – 6621N6-succinyllysineBy similarity
    Modified residuei668 – 6681N6-acetyllysineBy similarity
    Modified residuei724 – 7241N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP97852.
    PRIDEiP97852.

    PTM databases

    PhosphoSiteiP97852.

    Expressioni

    Gene expression databases

    GenevestigatoriP97852.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    IntActiP97852. 1 interaction.
    STRINGi10116.ENSRNOP00000043755.

    Structurei

    Secondary structure

    1
    735
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 144
    Turni15 – 184
    Helixi20 – 3112
    Beta strandi35 – 395
    Helixi53 – 6412
    Beta strandi68 – 725
    Helixi76 – 783
    Helixi79 – 8911
    Beta strandi95 – 984
    Helixi108 – 1103
    Helixi113 – 14129
    Beta strandi144 – 1496
    Helixi152 – 1565
    Helixi162 – 18120
    Helixi183 – 1853
    Beta strandi187 – 1959
    Turni199 – 2013
    Helixi202 – 2043
    Helixi207 – 2126
    Helixi215 – 2173
    Helixi219 – 2257
    Beta strandi236 – 2405
    Beta strandi243 – 2519
    Helixi266 – 2716
    Helixi273 – 2764
    Helixi288 – 30215

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GZ6X-ray2.38A/B/C/D1-319[»]
    ProteinModelPortaliP97852.
    SMRiP97852. Positions 3-303, 322-604, 621-735.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP97852.

    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.
    KOiK12405.
    OMAiTETIMPP.
    OrthoDBiEOG7RBZ7V.

    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.
    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.

    Sequencei

    Sequence statusi: Complete.

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

    P97852-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASPLRFDGR VVLVTGAGGG LGRAYALAFA ERGALVVVND LGGDFKGVGK    50
    GSSAADKVVE EIRRRGGKAV ANYDSVEAGE KLVKTALDTF GRIDVVVNNA 100
    GILRDRSFSR ISDEDWDIIQ RVHLRGSFQV TRAAWDHMKK QNYGRIIMTA 150
    SASGIYGNFG QANYSAAKLG LLGLANTLVI EGRKNNIHCN TIAPNAGSRM 200
    TETVMPEDLV EALKPEYVAP LVLWLCHESC EENGGLFEVG AGWIGKLRWE 250
    RTLGAIVRKR NQPMTPEAVR DNWVKICDFS NASKPKSIQE STGGIIEVLH 300
    KIDSEGISQN HTGQVASADA SGFAGVVGHK LPSFSSSYTE LQCIMYALGV 350
    GASVKNPKDL KFVYEGSADF SCLPTFGVIV AQKSLMSGGL AEVPGLSINF 400
    AKVLHGEQYL ELYKPLPRSG ELKCEAVIAD ILDKGSGIVI VMDVYSYSGK 450
    ELICYNQFSV FVVGSGGFGG KRTSEKLKAA VAVPSRPPDA VLRDTTSLNQ 500
    AALYRLSGDS NPLHIDPSFA SIAGFEKPIL HGLCTFGFSA RHVLQQFADN 550
    DVSRFKAIKV RFAKPVYPGQ TLQTEMWKEG NRIHFQTKVQ ETGDIVISNA 600
    YVDLVPTSGV SAQTPSEGGA LQSALVFGEI GRRLKDVGRE VVKKVNAVFE 650
    WHITKNGNVA AKWTIDLKNG SGEVYQGPAK GSADTTITIS DEDFMEVVLG 700
    KLNPQNAFFS GRLKARGNIM LSQKLQMILK DYAKL 735
    Length:735
    Mass (Da):79,428
    Last modified:January 23, 2007 - v3
    Checksum:iE14F15FFD35FC7D8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 22MA → M in CAA64427. (PubMed:8856068)Curated
    Sequence conflicti12 – 121V → G in CAA64427. (PubMed:8856068)Curated
    Sequence conflicti26 – 261A → G in CAA64427. (PubMed:8856068)Curated
    Sequence conflicti76 – 761V → G in AAB09724. (PubMed:9003397)Curated
    Sequence conflicti106 – 1061R → P in CAA64427. (PubMed:8856068)Curated
    Sequence conflicti157 – 1571G → S in AAB09724. (PubMed:9003397)Curated
    Sequence conflicti284 – 2841K → E in CAA64427. (PubMed:8856068)Curated
    Sequence conflicti368 – 3681A → P in CAA64427. (PubMed:8856068)Curated
    Sequence conflicti376 – 3761F → I in CAA64427. (PubMed:8856068)Curated
    Sequence conflicti386 – 3861M → T in AAB09724. (PubMed:9003397)Curated
    Sequence conflicti485 – 4851S → D in AAB09724. (PubMed:9003397)Curated
    Sequence conflicti498 – 4981L → V in CAA64427. (PubMed:8856068)Curated
    Sequence conflicti521 – 5211S → G in CAA64427. (PubMed:8856068)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S83279 mRNA. Translation: AAB49519.1.
    U37486 mRNA. Translation: AAB09724.1.
    X94978 mRNA. Translation: CAA64427.1.
    RefSeqiNP_077368.2. NM_024392.2.
    UniGeneiRn.2082.

    Genome annotation databases

    EnsembliENSRNOT00000021646; ENSRNOP00000021646; ENSRNOG00000015840.
    GeneIDi79244.
    KEGGirno:79244.
    UCSCiRGD:621806. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S83279 mRNA. Translation: AAB49519.1 .
    U37486 mRNA. Translation: AAB09724.1 .
    X94978 mRNA. Translation: CAA64427.1 .
    RefSeqi NP_077368.2. NM_024392.2.
    UniGenei Rn.2082.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GZ6 X-ray 2.38 A/B/C/D 1-319 [» ]
    ProteinModelPortali P97852.
    SMRi P97852. Positions 3-303, 322-604, 621-735.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P97852. 1 interaction.
    STRINGi 10116.ENSRNOP00000043755.

    Chemistry

    ChEMBLi CHEMBL1075219.

    PTM databases

    PhosphoSitei P97852.

    Proteomic databases

    PaxDbi P97852.
    PRIDEi P97852.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000021646 ; ENSRNOP00000021646 ; ENSRNOG00000015840 .
    GeneIDi 79244.
    KEGGi rno:79244.
    UCSCi RGD:621806. rat.

    Organism-specific databases

    CTDi 3295.
    RGDi 621806. Hsd17b4.

    Phylogenomic databases

    eggNOGi COG1028.
    GeneTreei ENSGT00530000062928.
    HOGENOMi HOG000170895.
    HOVERGENi HBG002174.
    KOi K12405.
    OMAi TETIMPP.
    OrthoDBi EOG7RBZ7V.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci MetaCyc:MONOMER-14329.
    Reactomei REACT_198818. alpha-linolenic acid (ALA) metabolism.

    Miscellaneous databases

    EvolutionaryTracei P97852.
    NextBioi 614694.
    PROi P97852.

    Gene expression databases

    Genevestigatori P97852.

    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.
    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.
    ProtoNeti Search...

    Publicationsi

    1. "Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized by separate multifunctional proteins."
      Dieuaide-Noubhani M., Novikov D., Baumgart E., Vanhooren J.C.T., Fransen M., Goethals M., Vandekerckhove J., Van Veldhoven P.P., Mannaerts G.P.
      Eur. J. Biochem. 240:660-666(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-30; 32-44; 110-115; 132-139 AND 270-274, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE.
      Tissue: Liver.
    2. "Rat 17 beta-hydroxysteroid dehydrogenase type IV is a novel peroxisome proliferator-inducible gene."
      Corton J.C., Bocos C., Moreno E.S., Merritt A., Marsman D.S., Sausen P.J., Cattley R.C., Gustafsson J.-A.
      Mol. Pharmacol. 50:1157-1166(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    3. "Peroxisomal multifunctional enzyme of beta-oxidation metabolizing D-3-hydroxyacyl-CoA esters in rat liver: molecular cloning, expression and characterization."
      Qin Y.M., Poutanen M.H., Helander H.M., Kvist A.P., Siivari K.M., Schmitz W., Conzelmann E., Hellman U., Hiltunen J.K.
      Biochem. J. 321:21-28(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 318-330; 479-505; 542-554; 562-576 AND 583-587, ENZYME CATALYSIS.
    4. "Identification and characterization of the 2-enoyl-CoA hydratases involved in peroxisomal beta-oxidation in rat liver."
      Dieuaide-Noubhani M., Novikov D., Vandekerckhove J., Veldhoven P.P., Mannaerts G.P.
      Biochem. J. 321:253-259(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 312-324, PROTEOLYTIC CLEAVAGE.
    5. "Binary structure of the two-domain (3R)-hydroxyacyl-CoA dehydrogenase from rat peroxisomal multifunctional enzyme type 2 at 2.38 A resolution."
      Haapalainen A.M., Koski M.K., Qin Y.-M., Hiltunen J.K., Glumoff T.
      Structure 11:87-97(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 1-319 IN COMPLEX WITH NAD, HOMODIMERIZATION.

    Entry informationi

    Entry nameiDHB4_RAT
    AccessioniPrimary (citable) accession number: P97852
    Secondary accession number(s): P70523, P70540
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 122 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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3