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Protein

3-hydroxyacyl-CoA dehydrogenase type-2

Gene

Hsd17b10

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Mitochondrial dehydrogenase that catalyzes the beta-oxidation at position 17 of androgens and estrogens and has 3-alpha-hydroxysteroid dehydrogenase activity with androsterone. Catalyzes the third step in the beta-oxidation of fatty acids. Carries out oxidative conversions of 7-alpha-OH and 7-beta-OH bile acids. Also exhibits 20-beta-OH and 21-OH dehydrogenase activities with C21 steroids. By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD). Essential for structural and functional integrity of mitochondria.By similarity
In addition to mitochondrial dehydrogenase activity, moonlights as a component of mitochondrial ribonuclease P, a complex that cleaves tRNA molecules in their 5'-ends. Together with HSD17B10/MRPP2, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity. The MRPP1-MRPP2 subcomplex catalyzes the formation of N1-methylguanine and N1-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; HSD17B10/MRPP2 acting as a non-catalytic subunit. The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme.By similarity

Catalytic activityi

(2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD+ = 2-methylacetoacetyl-CoA + NADH.By similarity
Testosterone + NAD(P)+ = androst-4-ene-3,17-dione + NAD(P)H.By similarity
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei155Substrate1 Publication1
Active sitei168Proton acceptor1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 37NADBy similarityAdd BLAST26

GO - Molecular functioni

  • 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity Source: UniProtKB-EC
  • 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB
  • acetoacetyl-CoA reductase activity Source: RGD
  • amyloid-beta binding Source: RGD
  • estradiol 17-beta-dehydrogenase activity Source: RGD
  • identical protein binding Source: RGD
  • NAD binding Source: RGD
  • steroid binding Source: RGD
  • testosterone dehydrogenase [NAD(P)] activity Source: UniProtKB
  • tRNA binding Source: UniProtKB

GO - Biological processi

  • cell aging Source: RGD
  • Leydig cell differentiation Source: RGD
  • mitochondrial tRNA 3'-end processing Source: UniProtKB
  • mitochondrial tRNA 5'-end processing Source: UniProtKB
  • mitochondrial tRNA methylation Source: UniProtKB
  • protein homotetramerization Source: RGD

Keywordsi

Molecular functionOxidoreductase
Biological processtRNA processing
LigandNAD

Enzyme and pathway databases

SABIO-RKiO70351

Names & Taxonomyi

Protein namesi
Recommended name:
3-hydroxyacyl-CoA dehydrogenase type-2 (EC:1.1.1.35By similarity)
Alternative name(s):
17-beta-hydroxysteroid dehydrogenase 10 (EC:1.1.1.51By similarity)
Short name:
17-beta-HSD 10
3-hydroxy-2-methylbutyryl-CoA dehydrogenase (EC:1.1.1.178By similarity)
3-hydroxyacyl-CoA dehydrogenase type II
Endoplasmic reticulum-associated amyloid beta-peptide-binding protein
Mitochondrial ribonuclease P protein 2
Short name:
Mitochondrial RNase P protein 2
Type II HADH
Gene namesi
Name:Hsd17b10
Synonyms:Erab, Hadh2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69231 Hsd17b10

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000548122 – 2613-hydroxyacyl-CoA dehydrogenase type-2Add BLAST260

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei53N6-acetyllysine; alternateBy similarity1
Modified residuei53N6-succinyllysine; alternateBy similarity1
Modified residuei69N6-acetyllysineBy similarity1
Modified residuei99N6-acetyllysineBy similarity1
Modified residuei105N6-acetyllysineBy similarity1
Modified residuei212N6-acetyllysine; alternateBy similarity1
Modified residuei212N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiO70351
PRIDEiO70351

PTM databases

iPTMnetiO70351
PhosphoSitePlusiO70351

Interactioni

Subunit structurei

Homotetramer. Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and MRPP31. Interacts with TRMT10C/MRPP1; forming the MRPP1-MRPP2 subcomplex of the mitochondrial ribonuclease P complex.By similarity

GO - Molecular functioni

  • identical protein binding Source: RGD

Protein-protein interaction databases

IntActiO70351, 1 interactor
STRINGi10116.ENSRNOP00000043608

Structurei

Secondary structure

1261
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 16Combined sources5
Turni17 – 19Combined sources3
Helixi21 – 32Combined sources12
Beta strandi36 – 41Combined sources6
Helixi47 – 54Combined sources8
Beta strandi58 – 62Combined sources5
Helixi68 – 82Combined sources15
Beta strandi87 – 90Combined sources4
Beta strandi100 – 102Combined sources3
Turni103 – 106Combined sources4
Helixi111 – 121Combined sources11
Helixi123 – 137Combined sources15
Beta strandi148 – 153Combined sources6
Helixi157 – 160Combined sources4
Helixi166 – 186Combined sources21
Helixi187 – 189Combined sources3
Beta strandi191 – 198Combined sources8
Beta strandi201 – 203Combined sources3
Turni204 – 206Combined sources3
Helixi214 – 217Combined sources4
Helixi218 – 220Combined sources3
Beta strandi222 – 224Combined sources3
Helixi230 – 242Combined sources13
Beta strandi250 – 254Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E3SX-ray2.00A/B/C/D2-261[»]
1E3WX-ray2.00A/B/C/D2-261[»]
1E6WX-ray1.70A/B/C/D2-261[»]
ProteinModelPortaliO70351
SMRiO70351
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO70351

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1199 Eukaryota
ENOG410XNNW LUCA
HOVERGENiHBG002145
InParanoidiO70351
KOiK08683
PhylomeDBiO70351

Family and domain databases

InterProiView protein in InterPro
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam
PfamiView protein in Pfam
PF00106 adh_short, 1 hit
PRINTSiPR00081 GDHRDH
PR00080 SDRFAMILY
SUPFAMiSSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00061 ADH_SHORT, 1 hit

Sequencei

Sequence statusi: Complete.

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

O70351-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAVRSVKG LVAVITGGAS GLGLSTAKRL VGQGATAVLL DVPNSEGETE
60 70 80 90 100
AKKLGGNCIF APANVTSEKE VQAALTLAKE KFGRIDVAVN CAGIAVAIKT
110 120 130 140 150
YHEKKNQVHT LEDFQRVINV NLIGTFNVIR LVAGVMGQNE PDQGGQRGVI
160 170 180 190 200
INTASVAAFE GQVGQAAYSA SKGGIVGMTL PIARDLAPIG IRVVTIAPGL
210 220 230 240 250
FATPLLTTLP DKVRNFLASQ VPFPSRLGDP AEYAHLVQMV IENPFLNGEV
260
IRLDGAIRMQ P
Length:261
Mass (Da):27,246
Last modified:January 23, 2007 - v3
Checksum:i117FD723B11EA227
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5V → C in AAF14853 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF049878 mRNA Translation: AAC05747.1
AF069770 mRNA Translation: AAF14853.1
RefSeqiNP_113870.1, NM_031682.1
UniGeneiRn.2700

Genome annotation databases

GeneIDi63864
KEGGirno:63864

Similar proteinsi

Entry informationi

Entry nameiHCD2_RAT
AccessioniPrimary (citable) accession number: O70351
Secondary accession number(s): Q9QYD4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 138 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

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

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