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O02691

- HCD2_BOVIN

UniProt

O02691 - HCD2_BOVIN

Protein

3-hydroxyacyl-CoA dehydrogenase type-2

Gene

HSD17B10

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (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 – 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

    Enzyme and pathway databases

    BioCyciRETL1328306-WGS:GSTH-6663-MONOMER.
    BRENDAi1.1.1.135. 908.
    ReactomeiREACT_216656. Branched-chain amino acid catabolism.

    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
    Mitochondrial ribonuclease P protein 2
    Short name:
    Mitochondrial RNase P protein 2
    Type II HADH
    Gene namesi
    Name:HSD17B10
    Synonyms:HADH2
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome X

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: Ensembl
    2. mitochondrial inner membrane Source: Ensembl
    3. 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_0000054809Add
    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

    PaxDbiO02691.
    PRIDEiO02691.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    IntActiO02691. 1 interaction.
    STRINGi9913.ENSBTAP00000023642.

    Structurei

    3D structure databases

    ProteinModelPortaliO02691.
    SMRiO02691. Positions 7-261.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1028.
    GeneTreeiENSGT00710000106273.
    HOVERGENiHBG002145.
    InParanoidiO02691.
    KOiK08683.
    OMAiLMGANEP.
    OrthoDBiEOG7JT6X7.
    TreeFamiTF354307.

    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.

    O02691-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAACRSVKG LVALITGGAS GLGLATAERL VGQGATAVLL DLPNSDGETQ    50
    AKKLGKSCAF APADVTSEKD VQAALTLARE KFGRVDVAVN CAGIAVASKT 100
    YNLKKSQAHT LEDFQRVINV NLIGTFNVIR LVAGEMGQNE PDQGGQRGVI 150
    INTASVAAFE GQVGQAAYSA SKGGIVGMTL PIARDLAPMG IRVMTIAPGL 200
    FGTPLLTTLP DKVRNFLASQ VPFPSRLGDP AEYAHLVQAI IENSFLNGEV 250
    IRLDGAIRMQ P 261
    Length:261
    Mass (Da):27,140
    Last modified:January 23, 2007 - v3
    Checksum:i8C7572B6A9A49780
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB002156 mRNA. Translation: BAA19510.1.
    BC110264 mRNA. Translation: AAI10265.1.
    RefSeqiNP_776759.1. NM_174334.3.
    UniGeneiBt.5231.

    Genome annotation databases

    EnsembliENSBTAT00000023642; ENSBTAP00000023642; ENSBTAG00000017779.
    GeneIDi281809.
    KEGGibta:281809.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB002156 mRNA. Translation: BAA19510.1 .
    BC110264 mRNA. Translation: AAI10265.1 .
    RefSeqi NP_776759.1. NM_174334.3.
    UniGenei Bt.5231.

    3D structure databases

    ProteinModelPortali O02691.
    SMRi O02691. Positions 7-261.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O02691. 1 interaction.
    STRINGi 9913.ENSBTAP00000023642.

    Proteomic databases

    PaxDbi O02691.
    PRIDEi O02691.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000023642 ; ENSBTAP00000023642 ; ENSBTAG00000017779 .
    GeneIDi 281809.
    KEGGi bta:281809.

    Organism-specific databases

    CTDi 3028.

    Phylogenomic databases

    eggNOGi COG1028.
    GeneTreei ENSGT00710000106273.
    HOVERGENi HBG002145.
    InParanoidi O02691.
    KOi K08683.
    OMAi LMGANEP.
    OrthoDBi EOG7JT6X7.
    TreeFami TF354307.

    Enzyme and pathway databases

    BioCyci RETL1328306-WGS:GSTH-6663-MONOMER.
    BRENDAi 1.1.1.135. 908.
    Reactomei REACT_216656. Branched-chain amino acid catabolism.

    Miscellaneous databases

    NextBioi 20805721.

    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. "Cloning and expression of cDNA for a newly identified isozyme of bovine liver 3-hydroxyacyl-CoA dehydrogenase and its import into mitochondria."
      Furuta S., Kobayashi A., Miyazawa S., Hashimoto T.
      Biochim. Biophys. Acta 1350:317-324(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Liver.
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus.
      Tissue: Liver.

    Entry informationi

    Entry nameiHCD2_BOVIN
    AccessioniPrimary (citable) accession number: O02691
    Secondary accession number(s): Q2TBG6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 108 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3