Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O08756 (HCD2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-hydroxyacyl-CoA dehydrogenase type-2

EC=1.1.1.35
Alternative name(s):
17-beta-hydroxysteroid dehydrogenase 10
Short name=17-beta-HSD 10
EC=1.1.1.51
3-hydroxy-2-methylbutyryl-CoA dehydrogenase
EC=1.1.1.178
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 names
Name:Hsd17b10
Synonyms:Erab, Hadh2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions in mitochondrial tRNA maturation. Part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/TRMT10C, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5'-ends. 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 similarity.

Catalytic activity

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.

(2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD+ = 2-methylacetoacetyl-CoA + NADH.

Testosterone + NAD(P)+ = androst-4-ene-3,17-dione + NAD(P)H.

Subunit structure

Homotetramer. Interacts with MRPP1/TRMT10C and MRPP3/KIAA0391 By similarity.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Sequence caution

The sequence AAB57689.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 2612603-hydroxyacyl-CoA dehydrogenase type-2
PRO_0000054811

Regions

Nucleotide binding12 – 3726NAD By similarity

Sites

Active site1681Proton acceptor By similarity
Binding site1551Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.2
Modified residue531N6-acetyllysine; alternate Ref.5
Modified residue531N6-succinyllysine; alternate Ref.4
Modified residue691N6-acetyllysine Ref.5
Modified residue991N6-acetyllysine Ref.5
Modified residue1051N6-acetyllysine Ref.5
Modified residue1071N6-acetyllysine; alternate Ref.5
Modified residue1071N6-succinyllysine; alternate Ref.4
Modified residue2121N6-acetyllysine; alternate Ref.5
Modified residue2121N6-succinyllysine; alternate Ref.4

Sequences

Sequence LengthMass (Da)Tools
O08756 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 61213B13E2839D41

FASTA26127,419
        10         20         30         40         50         60 
MAAAVRSVKG LVAVVTGGAS GPWLATAKRL VGQGATAVLL DVPDSEGESQ AKKLGESCIF 

        70         80         90        100        110        120 
APANVTSEKE IQAALTLAKE KFGRIDVAVN CAGIAVAIKT YHQKKNKIHT LEDFQRVINV 

       130        140        150        160        170        180 
NLIGTFNVIR LVAGEMGQNE PDQGGQRGVI INTASVAAFE GQVGQAAYSA SKGGIDGMTL 

       190        200        210        220        230        240 
PIARDLAPTG IRVVTIAPGL FATPLLTTLP EKVRNFLASQ VPFPSRLGDP AEYAHLVQTI 

       250        260 
IENPFLNGEV IRLDGAIRMQ P 

« Hide

References

« Hide 'large scale' references
[1]Fu J., Chen X., Stern D., Yan S.D.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6 X CBA.
[2]Bienvenut W.V.
Submitted (JUL-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-6; 193-212 AND 215-226, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Liver.
[3]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 70-79 AND 131-147, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[4]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-53; LYS-107 AND LYS-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
[5]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53; LYS-69; LYS-99; LYS-105; LYS-107 AND LYS-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U96116 mRNA. Translation: AAB57689.1. Different initiation.
UniGeneMm.6994.

3D structure databases

ProteinModelPortalO08756.
SMRO08756. Positions 7-261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO08756. 2 interactions.
MINTMINT-1861176.

PTM databases

PhosphoSiteO08756.

2D gel databases

SWISS-2DPAGEO08756.

Proteomic databases

PaxDbO08756.
PRIDEO08756.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:1333871. Hsd17b10.

Phylogenomic databases

eggNOGCOG1028.
HOVERGENHBG002145.
PhylomeDBO08756.

Gene expression databases

CleanExMM_HSD17B10.
GenevestigatorO08756.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHSD17B10. mouse.
PMAP-CutDBO08756.
PROO08756.
SOURCESearch...

Entry information

Entry nameHCD2_MOUSE
AccessionPrimary (citable) accession number: O08756
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 118 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot