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O70351 (HCD2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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 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.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 2612603-hydroxyacyl-CoA dehydrogenase type-2
PRO_0000054812

Regions

Nucleotide binding12 – 3726NAD By similarity

Sites

Active site1681Proton acceptor
Binding site1551Substrate

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Experimental info

Sequence conflict51V → C in AAF14853. Ref.2

Secondary structure

1 ............................................ 261
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O70351 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 117FD723B11EA227

FASTA26127,246
        10         20         30         40         50         60 
MAAAVRSVKG LVAVITGGAS GLGLSTAKRL VGQGATAVLL DVPNSEGETE AKKLGGNCIF 

        70         80         90        100        110        120 
APANVTSEKE VQAALTLAKE KFGRIDVAVN CAGIAVAIKT YHEKKNQVHT LEDFQRVINV 

       130        140        150        160        170        180 
NLIGTFNVIR LVAGVMGQNE PDQGGQRGVI INTASVAAFE GQVGQAAYSA SKGGIVGMTL 

       190        200        210        220        230        240 
PIARDLAPIG IRVVTIAPGL FATPLLTTLP DKVRNFLASQ VPFPSRLGDP AEYAHLVQMV 

       250        260 
IENPFLNGEV IRLDGAIRMQ P

« Hide

References

[1]"Rattus norvegicus amyloid beta-peptide binding protein (ERAB) mRNA."
Gunn-Moore F.J., Tavare J.M.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Molecular cloning and characterization of the cDNA of rat brain short chain L-3-hydroxyacyl-CoA dehydrogenase."
Yang S.-Y., He X.-Y.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
[3]Lubec G., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 117-130 AND 193-212, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus.
[4]"Recognition of structurally diverse substrates by type II 3-hydroxyacyl-CoA dehydrogenase (HADH II)/amyloid-beta binding alcohol dehydrogenase (ABAD)."
Powell A.J., Read J.A., Banfield M.J., Gunn-Moore F., Yan S.D., Lustbader J., Stern A.R., Stern D.M., Brady R.L.
J. Mol. Biol. 303:311-327(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF049878 mRNA. Translation: AAC05747.1.
AF069770 mRNA. Translation: AAF14853.1.
IPIIPI00886470.
RefSeqNP_113870.1. NM_031682.1.
UniGeneRn.2700.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E3SX-ray2.00A/B/C/D1-261[»]
1E3WX-ray2.00A/B/C/D1-261[»]
1E6WX-ray1.70A/B/C/D2-261[»]
ProteinModelPortalO70351.
SMRO70351. Positions 7-261.
ModBaseSearch...

Protein-protein interaction databases

IntActO70351. 1 interaction.

Proteomic databases

PaxDbO70351.
PRIDEO70351.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID63864.
KEGGrno:63864.

Organism-specific databases

CTD3028.
RGD69231. Hsd17b10.

Phylogenomic databases

eggNOGCOG1028.
HOVERGENHBG002145.
InParanoidO70351.
KOK08683.
OrthoDBEOG46MBKC.

Enzyme and pathway databases

SABIO-RKO70351.

Gene expression databases

ArrayExpressO70351.
GenevestigatorO70351.
GermOnlineENSRNOG00000003049. Rattus norvegicus.

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

EvolutionaryTraceO70351.
NextBio612472.

Entry information

Entry nameHCD2_RAT
AccessionPrimary (citable) accession number: O70351
Secondary accession number(s): Q9QYD4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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