Reviewed, UniProtKB/Swiss-Prot O70351 (HCD2_RAT)

Names and origin

Protein names

Recommended name:
    3-hydroxyacyl-CoA dehydrogenase type-2
    EC=1.1.1.35
Alternative name(s):
    3-hydroxyacyl-CoA dehydrogenase type II
    Type II HADH
    3-hydroxy-2-methylbutyryl-CoA dehydrogenase
    EC=1.1.1.178
    17-beta-hydroxysteroid dehydrogenase 10
    Mitochondrial ribonuclease P protein 2
      Short name=Mitochondrial RNase P protein 2
    Endoplasmic reticulum-associated amyloid beta-peptide-binding protein

Gene names

Name:	Hsd17b10
Synonyms:	Erab, Hadh2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Functions in mitochondrial tRNA maturation. Part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/RG9MTD1, 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/RG9MTD1 and MRPP3/KIAA0391 By similarity.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Mitochondrion
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	Leydig cell differentiation Inferred from expression pattern. Source: RGD cell aging Inferred from expression pattern. Source: RGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW protein homotetramerization Ref.4 Inferred from direct assay. Source: RGD tRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity Inferred from electronic annotation. Source: EC 3-hydroxyacyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: EC NAD or NADH binding Ref.4 Inferred from direct assay. Source: RGD acetoacetyl-CoA reductase activity Ref.4 Inferred from direct assay. Source: RGD beta-amyloid binding Ref.4 Inferred from direct assay. Source: RGD estradiol 17-beta-dehydrogenase activity Ref.4 Inferred from direct assay. Source: RGD identical protein binding Ref.4 Inferred from direct assay. Source: RGD steroid binding Ref.4 Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 261

260

3-hydroxyacyl-CoA dehydrogenase type-2

PRO_0000054812

Regions

Nucleotide binding

12 – 37

26

NAD By similarity

Sites

Active site

168

1

Proton acceptor

Binding site

155

1

Substrate

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Experimental info

Sequence conflict

5

1

V → C in AAF14853. Ref.2

Secondary structure

1

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261

Helix Strand Turn

Details...

Beta strand

12 – 16

5

Turn

17 – 19

3

Helix

21 – 32

12

Beta strand

36 – 41

6

Helix

47 – 53

7

Beta strand

58 – 62

5

Helix

68 – 82

15

Beta strand

87 – 90

4

Beta strand

100 – 102

3

Turn

103 – 106

4

Helix

111 – 121

11

Helix

123 – 137

15

Beta strand

148 – 153

6

Helix

156 – 158

3

Helix

166 – 186

21

Helix

187 – 189

3

Beta strand

191 – 198

8

Beta strand

222 – 224

3

Helix

230 – 242

13

Beta strand

250 – 254

5

Sequences

	Sequence		Length	Mass (Da)
	O70351-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 117FD723B11EA227	FASTA	261	27,246
	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

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: 11023795] [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.

IPI

IPI00886470.

RefSeq

NP_113870.1.

UniGene

Rn.2700

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E3S	X-ray	2.00	A/B/C/D	1-261	[»]
1E3W	X-ray	2.00	A/B/C/D	1-261	[»]
1E6W	X-ray	1.70	A/B/C/D	2-261	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

O70351.

Proteomic databases

PRIDE

O70351.

Genome annotation databases

Ensembl

ENSRNOT00000043559; ENSRNOP00000043608; ENSRNOG00000003049; Rattus norvegicus. [Genome view]

GeneID

63864.

KEGG

rno:63864.

UCSC

NM_031682. rat.

Organism-specific databases

CTD

63864.

RGD

69231. Hadh2.

Phylogenomic databases

eggNOG

roNOG12500.

HOVERGEN

O70351.

InParanoid

O70351.

Enzyme and pathway databases

BRENDA

1.1.1.178. 248.
1.1.1.35. 248.

Gene expression databases

ArrayExpress

O70351.

Genevestigator

O70351.

GermOnline

ENSRNOG00000003049. Rattus norvegicus.

Family and domain databases

InterPro

IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR19410. ADH_short_C2. 1 hit.

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.
PR00080. SDRFAMILY.

PROSITE

PS00061. ADH_SHORT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

612472.

Entry information

Entry name

HCD2_RAT

Accession

Primary (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:	January 19, 2010
This is version 81 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)