Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P97852

- DHB4_RAT

UniProt

P97852 - DHB4_RAT

(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)

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

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. osteoblast differentiation Source: Ensembl
  7. Sertoli cell development Source: Ensembl
  8. very long-chain fatty acid metabolic process Source: Ensembl
  9. 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

BioCyciMetaCyc:MONOMER-14329.
ReactomeiREACT_198818. alpha-linolenic acid (ALA) metabolism.
REACT_239598. Beta-oxidation of pristanoyl-CoA.
REACT_253630. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_256178. Beta-oxidation of very long chain fatty acids.
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
Complete GO annotation...

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 – 144Combined sources
Turni15 – 184Combined sources
Helixi20 – 3112Combined sources
Beta strandi35 – 395Combined sources
Helixi53 – 6412Combined sources
Beta strandi68 – 725Combined sources
Helixi76 – 783Combined sources
Helixi79 – 8911Combined sources
Beta strandi95 – 984Combined sources
Helixi108 – 1103Combined sources
Helixi113 – 14129Combined sources
Beta strandi144 – 1496Combined sources
Helixi152 – 1565Combined sources
Helixi162 – 18120Combined sources
Helixi183 – 1853Combined sources
Beta strandi187 – 1959Combined sources
Turni199 – 2013Combined sources
Helixi202 – 2043Combined sources
Helixi207 – 2126Combined sources
Helixi215 – 2173Combined sources
Helixi219 – 2257Combined sources
Beta strandi236 – 2405Combined sources
Beta strandi243 – 2519Combined sources
Helixi266 – 2716Combined sources
Helixi273 – 2764Combined sources
Helixi288 – 30215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP97852.
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

        10         20         30         40         50
MASPLRFDGR VVLVTGAGGG LGRAYALAFA ERGALVVVND LGGDFKGVGK
60 70 80 90 100
GSSAADKVVE EIRRRGGKAV ANYDSVEAGE KLVKTALDTF GRIDVVVNNA
110 120 130 140 150
GILRDRSFSR ISDEDWDIIQ RVHLRGSFQV TRAAWDHMKK QNYGRIIMTA
160 170 180 190 200
SASGIYGNFG QANYSAAKLG LLGLANTLVI EGRKNNIHCN TIAPNAGSRM
210 220 230 240 250
TETVMPEDLV EALKPEYVAP LVLWLCHESC EENGGLFEVG AGWIGKLRWE
260 270 280 290 300
RTLGAIVRKR NQPMTPEAVR DNWVKICDFS NASKPKSIQE STGGIIEVLH
310 320 330 340 350
KIDSEGISQN HTGQVASADA SGFAGVVGHK LPSFSSSYTE LQCIMYALGV
360 370 380 390 400
GASVKNPKDL KFVYEGSADF SCLPTFGVIV AQKSLMSGGL AEVPGLSINF
410 420 430 440 450
AKVLHGEQYL ELYKPLPRSG ELKCEAVIAD ILDKGSGIVI VMDVYSYSGK
460 470 480 490 500
ELICYNQFSV FVVGSGGFGG KRTSEKLKAA VAVPSRPPDA VLRDTTSLNQ
510 520 530 540 550
AALYRLSGDS NPLHIDPSFA SIAGFEKPIL HGLCTFGFSA RHVLQQFADN
560 570 580 590 600
DVSRFKAIKV RFAKPVYPGQ TLQTEMWKEG NRIHFQTKVQ ETGDIVISNA
610 620 630 640 650
YVDLVPTSGV SAQTPSEGGA LQSALVFGEI GRRLKDVGRE VVKKVNAVFE
660 670 680 690 700
WHITKNGNVA AKWTIDLKNG SGEVYQGPAK GSADTTITIS DEDFMEVVLG
710 720 730
KLNPQNAFFS GRLKARGNIM LSQKLQMILK DYAKL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P97852.
KOi K12405.
OMAi TETIMPP.
OrthoDBi EOG7RBZ7V.

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci MetaCyc:MONOMER-14329.
Reactomei REACT_198818. alpha-linolenic acid (ALA) metabolism.
REACT_239598. Beta-oxidation of pristanoyl-CoA.
REACT_253630. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_256178. Beta-oxidation of very long chain fatty acids.

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: November 26, 2014
This is version 124 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