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Protein

Peroxisomal multifunctional enzyme type 2

Gene

Hsd17b4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

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

  • 17-beta-hydroxysteroid dehydrogenase (NAD+) activity Source: RGD
  • 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity Source: UniProtKB-EC
  • 3-hydroxyacyl-CoA dehydratase activity Source: RGD
  • estradiol 17-beta-dehydrogenase activity Source: RGD
  • isomerase activity Source: UniProtKB-KW
  • protein homodimerization activity Source: RGD
  • testosterone dehydrogenase [NAD(P)] activity Source: RGD

GO - Biological processi

  • aging Source: RGD
  • cellular response to organic cyclic compound Source: RGD
  • cholesterol metabolic process Source: RGD
  • fatty acid beta-oxidation Source: UniProtKB-UniPathway
  • response to drug Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to steroid hormone Source: RGD
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.
ReactomeiR-RNO-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-RNO-2046106. alpha-linolenic acid (ALA) metabolism.
R-RNO-389887. Beta-oxidation of pristanoyl-CoA.
R-RNO-390247. 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
Proteomesi
  • UP000002494 Componenti: Chromosome 18

Organism-specific databases

RGDi621806. Hsd17b4.

Subcellular locationi

GO - Cellular componenti

  • peroxisome Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1075219.

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 residuei52 – 521PhosphoserineBy similarity
Modified residuei57 – 571N6-succinyllysineBy similarity
Modified residuei68 – 681N6-succinyllysineBy similarity
Modified residuei84 – 841N6-succinyllysineBy similarity
Modified residuei265 – 2651PhosphothreonineBy 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

iPTMnetiP97852.
PhosphoSiteiP97852.

Expressioni

Gene expression databases

BgeeiENSRNOG00000015840.
ExpressionAtlasiP97852. baseline and differential.
GenevisibleiP97852. RN.

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

IntActiP97852. 1 interaction.
STRINGi10116.ENSRNOP00000021646.

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

eggNOGiKOG1206. Eukaryota.
COG2030. LUCA.
GeneTreeiENSGT00530000062928.
HOGENOMiHOG000170895.
HOVERGENiHBG002174.
InParanoidiP97852.
KOiK12405.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
3.30.1050.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR029069. HotDog_dom.
IPR002539. MaoC_dom.
IPR016040. NAD(P)-bd_dom.
IPR003033. SCP2_sterol-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
PF02036. SCP2. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF54637. 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.
RefSeqiNP_077368.2. NM_024392.2.
UniGeneiRn.2082.

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...

Protein-protein interaction databases

IntActiP97852. 1 interaction.
STRINGi10116.ENSRNOP00000021646.

Chemistry

ChEMBLiCHEMBL1075219.

PTM databases

iPTMnetiP97852.
PhosphoSiteiP97852.

Proteomic databases

PaxDbiP97852.
PRIDEiP97852.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3295.
RGDi621806. Hsd17b4.

Phylogenomic databases

eggNOGiKOG1206. Eukaryota.
COG2030. LUCA.
GeneTreeiENSGT00530000062928.
HOGENOMiHOG000170895.
HOVERGENiHBG002174.
InParanoidiP97852.
KOiK12405.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciMetaCyc:MONOMER-14329.
ReactomeiR-RNO-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-RNO-2046106. alpha-linolenic acid (ALA) metabolism.
R-RNO-389887. Beta-oxidation of pristanoyl-CoA.
R-RNO-390247. Beta-oxidation of very long chain fatty acids.

Miscellaneous databases

EvolutionaryTraceiP97852.
PROiP97852.

Gene expression databases

BgeeiENSRNOG00000015840.
ExpressionAtlasiP97852. baseline and differential.
GenevisibleiP97852. RN.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
3.30.1050.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR029069. HotDog_dom.
IPR002539. MaoC_dom.
IPR016040. NAD(P)-bd_dom.
IPR003033. SCP2_sterol-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
PF02036. SCP2. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF54637. SSF54637. 2 hits.
SSF55718. SSF55718. 1 hit.
ProtoNetiSearch...

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: September 7, 2016
This is version 139 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.