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Protein

3-hydroxyacyl-CoA dehydrogenase type-2

Gene

Hsd17b10

Organism
Mus musculus (Mouse)
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 (By similarity). Catalyzes the third step in the beta-oxidation of fatty acids (By similarity). Carries out oxidative conversions of 7-alpha-OH and 7-beta-OH bile acids (By similarity). Also exhibits 20-beta-OH and 21-OH dehydrogenase activities with C21 steroids (By similarity). By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD) (By similarity). Essential for structural and functional integrity of mitochondria (PubMed:20077426).By similarity1 Publication
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 sitei155SubstrateBy similarity1
Active sitei168Proton acceptorPROSITE-ProRule annotation1

Regions

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processtRNA processing
LigandNAD

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1333871 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

Pathology & Biotechi

Disruption phenotypei

Conditional knockout mice are fertile but rapidly die around week 26. Mitochondrial morphology is severely altered in the central and peripheral nervous system, as well as in the cerebellum.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000548112 – 2613-hydroxyacyl-CoA dehydrogenase type-2Add BLAST260

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei53N6-acetyllysine; alternateCombined sources1
Modified residuei53N6-succinyllysine; alternateCombined sources1
Modified residuei69N6-acetyllysineCombined sources1
Modified residuei99N6-acetyllysineCombined sources1
Modified residuei105N6-acetyllysineCombined sources1
Modified residuei107N6-acetyllysine; alternateCombined sources1
Modified residuei107N6-succinyllysine; alternateCombined sources1
Modified residuei212N6-acetyllysine; alternateCombined sources1
Modified residuei212N6-succinyllysine; alternateCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiO08756
MaxQBiO08756
PaxDbiO08756
PeptideAtlasiO08756
PRIDEiO08756

2D gel databases

SWISS-2DPAGEiO08756

PTM databases

iPTMnetiO08756
PhosphoSitePlusiO08756
SwissPalmiO08756

Miscellaneous databases

PMAP-CutDBiO08756

Expressioni

Gene expression databases

CleanExiMM_HSD17B10

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

Protein-protein interaction databases

IntActiO08756, 3 interactors
MINTiO08756
STRINGi10090.ENSMUSP00000026289

Structurei

3D structure databases

ProteinModelPortaliO08756
SMRiO08756
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1199 Eukaryota
ENOG410XNNW LUCA
HOVERGENiHBG002145
InParanoidiO08756
PhylomeDBiO08756

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.

O08756-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAVRSVKG LVAVVTGGAS GPWLATAKRL VGQGATAVLL DVPDSEGESQ
60 70 80 90 100
AKKLGESCIF APANVTSEKE IQAALTLAKE KFGRIDVAVN CAGIAVAIKT
110 120 130 140 150
YHQKKNKIHT LEDFQRVINV NLIGTFNVIR LVAGEMGQNE PDQGGQRGVI
160 170 180 190 200
INTASVAAFE GQVGQAAYSA SKGGIDGMTL PIARDLAPTG IRVVTIAPGL
210 220 230 240 250
FATPLLTTLP EKVRNFLASQ VPFPSRLGDP AEYAHLVQTI IENPFLNGEV
260
IRLDGAIRMQ P
Length:261
Mass (Da):27,419
Last modified:January 23, 2007 - v4
Checksum:i61213B13E2839D41
GO

Sequence cautioni

The sequence AAB57689 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96116 mRNA Translation: AAB57689.1 Different initiation.
CCDSiCCDS30471.1
UniGeneiMm.6994

Similar proteinsi

Entry informationi

Entry nameiHCD2_MOUSE
AccessioniPrimary (citable) accession number: O08756
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 145 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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