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O70351

- HCD2_RAT

UniProt

O70351 - HCD2_RAT

Protein

3-hydroxyacyl-CoA dehydrogenase type-2

Gene

Hsd17b10

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    (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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei155 – 1551Substrate1 Publication
    Active sitei168 – 1681Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 3726NADBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity Source: UniProtKB-EC
    2. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-EC
    3. acetoacetyl-CoA reductase activity Source: RGD
    4. beta-amyloid binding Source: RGD
    5. estradiol 17-beta-dehydrogenase activity Source: RGD
    6. estrogen receptor binding Source: RGD
    7. identical protein binding Source: RGD
    8. NAD binding Source: RGD
    9. steroid binding Source: RGD
    10. testosterone dehydrogenase [NAD(P)] activity Source: UniProtKB-EC

    GO - Biological processi

    1. cell aging Source: RGD
    2. Leydig cell differentiation Source: RGD
    3. protein homotetramerization Source: RGD
    4. tRNA processing Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    tRNA processing

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    SABIO-RKO70351.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-hydroxyacyl-CoA dehydrogenase type-2 (EC:1.1.1.35)
    Alternative name(s):
    17-beta-hydroxysteroid dehydrogenase 10 (EC:1.1.1.51)
    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 namesi
    Name:Hsd17b10
    Synonyms:Erab, Hadh2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi69231. Hsd17b10.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 2612603-hydroxyacyl-CoA dehydrogenase type-2PRO_0000054812Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei53 – 531N6-acetyllysine; alternateBy similarity
    Modified residuei53 – 531N6-succinyllysine; alternateBy similarity
    Modified residuei69 – 691N6-acetyllysineBy similarity
    Modified residuei99 – 991N6-acetyllysineBy similarity
    Modified residuei105 – 1051N6-acetyllysineBy similarity
    Modified residuei212 – 2121N6-acetyllysine; alternateBy similarity
    Modified residuei212 – 2121N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiO70351.
    PRIDEiO70351.

    Expressioni

    Gene expression databases

    GenevestigatoriO70351.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    IntActiO70351. 1 interaction.
    MINTiMINT-4568352.

    Structurei

    Secondary structure

    1
    261
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 165
    Turni17 – 193
    Helixi21 – 3212
    Beta strandi36 – 416
    Helixi47 – 548
    Beta strandi58 – 625
    Helixi68 – 8215
    Beta strandi87 – 904
    Beta strandi100 – 1023
    Turni103 – 1064
    Helixi111 – 12111
    Helixi123 – 13715
    Beta strandi148 – 1536
    Helixi157 – 1604
    Helixi166 – 18621
    Helixi187 – 1893
    Beta strandi191 – 1988
    Beta strandi201 – 2033
    Turni204 – 2063
    Helixi214 – 2174
    Helixi218 – 2203
    Beta strandi222 – 2243
    Helixi230 – 24213
    Beta strandi250 – 2545

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E3SX-ray2.00A/B/C/D2-261[»]
    1E3WX-ray2.00A/B/C/D2-261[»]
    1E6WX-ray1.70A/B/C/D2-261[»]
    ProteinModelPortaliO70351.
    SMRiO70351. Positions 7-261.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO70351.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1028.
    HOVERGENiHBG002145.
    InParanoidiO70351.
    KOiK08683.
    PhylomeDBiO70351.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view]
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O70351-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAVRSVKG LVAVITGGAS GLGLSTAKRL VGQGATAVLL DVPNSEGETE    50
    AKKLGGNCIF APANVTSEKE VQAALTLAKE KFGRIDVAVN CAGIAVAIKT 100
    YHEKKNQVHT LEDFQRVINV NLIGTFNVIR LVAGVMGQNE PDQGGQRGVI 150
    INTASVAAFE GQVGQAAYSA SKGGIVGMTL PIARDLAPIG IRVVTIAPGL 200
    FATPLLTTLP DKVRNFLASQ VPFPSRLGDP AEYAHLVQMV IENPFLNGEV 250
    IRLDGAIRMQ P 261
    Length:261
    Mass (Da):27,246
    Last modified:January 23, 2007 - v3
    Checksum:i117FD723B11EA227
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51V → C in AAF14853. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF049878 mRNA. Translation: AAC05747.1.
    AF069770 mRNA. Translation: AAF14853.1.
    RefSeqiNP_113870.1. NM_031682.1.
    UniGeneiRn.2700.

    Genome annotation databases

    GeneIDi63864.
    KEGGirno:63864.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF049878 mRNA. Translation: AAC05747.1 .
    AF069770 mRNA. Translation: AAF14853.1 .
    RefSeqi NP_113870.1. NM_031682.1.
    UniGenei Rn.2700.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E3S X-ray 2.00 A/B/C/D 2-261 [» ]
    1E3W X-ray 2.00 A/B/C/D 2-261 [» ]
    1E6W X-ray 1.70 A/B/C/D 2-261 [» ]
    ProteinModelPortali O70351.
    SMRi O70351. Positions 7-261.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O70351. 1 interaction.
    MINTi MINT-4568352.

    Proteomic databases

    PaxDbi O70351.
    PRIDEi O70351.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 63864.
    KEGGi rno:63864.

    Organism-specific databases

    CTDi 3028.
    RGDi 69231. Hsd17b10.

    Phylogenomic databases

    eggNOGi COG1028.
    HOVERGENi HBG002145.
    InParanoidi O70351.
    KOi K08683.
    PhylomeDBi O70351.

    Enzyme and pathway databases

    SABIO-RK O70351.

    Miscellaneous databases

    EvolutionaryTracei O70351.
    NextBioi 612472.
    PROi O70351.

    Gene expression databases

    Genevestigatori O70351.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view ]
    Pfami PF00106. adh_short. 1 hit.
    [Graphical view ]
    PRINTSi PR00081. GDHRDH.
    PR00080. SDRFAMILY.
    PROSITEi PS00061. ADH_SHORT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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, IDENTIFICATION BY 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.

    Entry informationi

    Entry nameiHCD2_RAT
    AccessioniPrimary (citable) accession number: O70351
    Secondary accession number(s): Q9QYD4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 114 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3