Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O08756

- HCD2_MOUSE

UniProt

O08756 - HCD2_MOUSE

Protein

3-hydroxyacyl-CoA dehydrogenase type-2

Gene

Hsd17b10

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 – 1551SubstrateBy similarity
    Active sitei168 – 1681Proton acceptorPROSITE-ProRule annotation

    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. testosterone dehydrogenase [NAD(P)] activity Source: UniProtKB-EC

    GO - Biological processi

    1. tRNA processing Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    tRNA processing

    Keywords - Ligandi

    NAD

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1333871. Hsd17b10.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: MGI
    2. mitochondrial inner membrane Source: MGI
    3. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 2612603-hydroxyacyl-CoA dehydrogenase type-2PRO_0000054811Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei53 – 531N6-acetyllysine; alternate1 Publication
    Modified residuei53 – 531N6-succinyllysine; alternate1 Publication
    Modified residuei69 – 691N6-acetyllysine1 Publication
    Modified residuei99 – 991N6-acetyllysine1 Publication
    Modified residuei105 – 1051N6-acetyllysine1 Publication
    Modified residuei107 – 1071N6-acetyllysine; alternate1 Publication
    Modified residuei107 – 1071N6-succinyllysine; alternate1 Publication
    Modified residuei212 – 2121N6-acetyllysine; alternate1 Publication
    Modified residuei212 – 2121N6-succinyllysine; alternate1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO08756.
    PaxDbiO08756.
    PRIDEiO08756.

    2D gel databases

    SWISS-2DPAGEO08756.

    PTM databases

    PhosphoSiteiO08756.

    Miscellaneous databases

    PMAP-CutDBO08756.

    Expressioni

    Gene expression databases

    CleanExiMM_HSD17B10.
    GenevestigatoriO08756.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    IntActiO08756. 3 interactions.
    MINTiMINT-1861176.

    Structurei

    3D structure databases

    ProteinModelPortaliO08756.
    SMRiO08756. Positions 7-261.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1028.
    HOVERGENiHBG002145.
    PhylomeDBiO08756.

    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.

    O08756-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAVRSVKG LVAVVTGGAS GPWLATAKRL VGQGATAVLL DVPDSEGESQ    50
    AKKLGESCIF APANVTSEKE IQAALTLAKE KFGRIDVAVN CAGIAVAIKT 100
    YHQKKNKIHT LEDFQRVINV NLIGTFNVIR LVAGEMGQNE PDQGGQRGVI 150
    INTASVAAFE GQVGQAAYSA SKGGIDGMTL PIARDLAPTG IRVVTIAPGL 200
    FATPLLTTLP EKVRNFLASQ VPFPSRLGDP AEYAHLVQTI IENPFLNGEV 250
    IRLDGAIRMQ P 261
    Length:261
    Mass (Da):27,419
    Last modified:January 23, 2007 - v4
    Checksum:i61213B13E2839D41
    GO

    Sequence cautioni

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96116 mRNA. Translation: AAB57689.1. Different initiation.
    CCDSiCCDS30471.1.
    UniGeneiMm.6994.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96116 mRNA. Translation: AAB57689.1 . Different initiation.
    CCDSi CCDS30471.1.
    UniGenei Mm.6994.

    3D structure databases

    ProteinModelPortali O08756.
    SMRi O08756. Positions 7-261.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O08756. 3 interactions.
    MINTi MINT-1861176.

    PTM databases

    PhosphoSitei O08756.

    2D gel databases

    SWISS-2DPAGE O08756.

    Proteomic databases

    MaxQBi O08756.
    PaxDbi O08756.
    PRIDEi O08756.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:1333871. Hsd17b10.

    Phylogenomic databases

    eggNOGi COG1028.
    HOVERGENi HBG002145.
    PhylomeDBi O08756.

    Miscellaneous databases

    ChiTaRSi HSD17B10. mouse.
    PMAP-CutDB O08756.
    PROi O08756.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_HSD17B10.
    Genevestigatori O08756.

    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. 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.

    Entry informationi

    Entry nameiHCD2_MOUSE
    AccessioniPrimary (citable) accession number: O08756
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 121 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3