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Protein

3-hydroxyacyl-CoA dehydrogenase type-2

Gene

HSD17B10

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. poly(A) RNA binding Source: Ensembl
  4. testosterone dehydrogenase [NAD(P)] activity Source: UniProtKB-EC

GO - Biological processi

  1. tRNA processing Source: UniProtKB-KW
Complete GO annotation...

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
Complete GO annotation...

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.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG002145.
InParanoidiO02691.
KOiK08683.
OMAiLMGLVNC.
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

        10         20         30         40         50
MAAACRSVKG LVALITGGAS GLGLATAERL VGQGATAVLL DLPNSDGETQ
60 70 80 90 100
AKKLGKSCAF APADVTSEKD VQAALTLARE KFGRVDVAVN CAGIAVASKT
110 120 130 140 150
YNLKKSQAHT LEDFQRVINV NLIGTFNVIR LVAGEMGQNE PDQGGQRGVI
160 170 180 190 200
INTASVAAFE GQVGQAAYSA SKGGIVGMTL PIARDLAPMG IRVMTIAPGL
210 220 230 240 250
FGTPLLTTLP DKVRNFLASQ VPFPSRLGDP AEYAHLVQAI IENSFLNGEV
260
IRLDGAIRMQ P
Length:261
Mass (Da):27,140
Last modified:January 23, 2007 - v3
Checksum:i8C7572B6A9A49780
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AB002156 mRNA. Translation: BAA19510.1.
BC110264 mRNA. Translation: AAI10265.1.
RefSeqiNP_776759.1. NM_174334.3.
UniGeneiBt.5231.

3D structure databases

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

Protein-protein interaction databases

IntActiO02691. 1 interaction.
STRINGi9913.ENSBTAP00000023642.

Proteomic databases

PaxDbiO02691.
PRIDEiO02691.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3028.

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG002145.
InParanoidiO02691.
KOiK08683.
OMAiLMGLVNC.
OrthoDBiEOG7JT6X7.
TreeFamiTF354307.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi20805721.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 110 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.