Reviewed,
UniProtKB/Swiss-Prot O08756 (HCD2_MOUSE)
Last modified
January 19, 2010.
Version 89.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
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 |
| ||||
| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
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 | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tRNA processingInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | endoplasmic reticulum Inferred from direct assay. Source: MGI mitochondrial inner membraneInferred from direct assay. Source: MGI |
| Molecular function | 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity Inferred from electronic annotation. Source: EC 3-hydroxyacyl-CoA dehydrogenase activityInferred from electronic annotation. Source: EC bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.2 | ||||||
| Chain | 2 – 261 | 260 | 3-hydroxyacyl-CoA dehydrogenase type-2 | PRO_0000054811 | |||||
Regions | |||||||||
| Nucleotide binding | 12 – 37 | 26 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 168 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 155 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine Ref.2 | ||||||
Sequences
| ||||||||||||||||||
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, 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, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U96116 mRNA. Translation: AAB57689.1. Different initiation. |
| IPI | IPI00320847. |
| UniGene | Mm.6994 |
3D structure databases | |
| SMR | O08756. Positions 7-261. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | O08756. |
2-D gel databases | |
| SWISS-2DPAGE | O08756. |
Proteomic databases | |
| PRIDE | O08756. |
Genome annotation databases | |
| Ensembl | ENSMUST00000026289; ENSMUSP00000026289; ENSMUSG00000025260; Mus musculus. [Genome view] |
Organism-specific databases | |
| MGI | MGI:1333871. Hsd17b10. |
Phylogenomic databases | |
| eggNOG | roNOG12500. |
| HOVERGEN | O08756. |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.178. 244. 1.1.1.35. 244. |
Gene expression databases | |
| ArrayExpress | O08756. |
| Bgee | O08756. |
| CleanEx | MM_HSD17B10. |
| Genevestigator | O08756. |
| GermOnline | ENSMUSG00000025260. Mus musculus. |
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 | |
| PMAP-CutDB | O08756. |
| SOURCE | Search... |
Entry information
| Entry name | HCD2_MOUSE | ||||||||
| Accession | Primary (citable) accession number: O08756 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


