Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O02691 (HCD2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-hydroxyacyl-CoA dehydrogenase type-2

EC=1.1.1.35
Alternative name(s):
17-beta-hydroxysteroid dehydrogenase 10
Short name=17-beta-HSD 10
EC=1.1.1.51
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 names
Name:HSD17B10
Synonyms:HADH2
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

(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.

Subunit structure

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

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 2612603-hydroxyacyl-CoA dehydrogenase type-2
PRO_0000054809

Regions

Nucleotide binding12 – 3726NAD By similarity

Sites

Active site1681Proton acceptor By similarity
Binding site1551Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue531N6-acetyllysine; alternate By similarity
Modified residue531N6-succinyllysine; alternate By similarity
Modified residue691N6-acetyllysine By similarity
Modified residue991N6-acetyllysine By similarity
Modified residue1051N6-acetyllysine By similarity
Modified residue2121N6-acetyllysine; alternate By similarity
Modified residue2121N6-succinyllysine; alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
O02691 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8C7572B6A9A49780

FASTA26127,140
        10         20         30         40         50         60 
MAAACRSVKG LVALITGGAS GLGLATAERL VGQGATAVLL DLPNSDGETQ AKKLGKSCAF 

        70         80         90        100        110        120 
APADVTSEKD VQAALTLARE KFGRVDVAVN CAGIAVASKT YNLKKSQAHT LEDFQRVINV 

       130        140        150        160        170        180 
NLIGTFNVIR LVAGEMGQNE PDQGGQRGVI INTASVAAFE GQVGQAAYSA SKGGIVGMTL 

       190        200        210        220        230        240 
PIARDLAPMG IRVMTIAPGL FGTPLLTTLP DKVRNFLASQ VPFPSRLGDP AEYAHLVQAI 

       250        260 
IENSFLNGEV IRLDGAIRMQ P 

« Hide

References

« Hide 'large scale' references
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB002156 mRNA. Translation: BAA19510.1.
BC110264 mRNA. Translation: AAI10265.1.
RefSeqNP_776759.1. NM_174334.3.
UniGeneBt.5231.

3D structure databases

ProteinModelPortalO02691.
SMRO02691. Positions 7-261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO02691. 1 interaction.
STRING9913.ENSBTAP00000023642.

Proteomic databases

PaxDbO02691.
PRIDEO02691.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000023642; ENSBTAP00000023642; ENSBTAG00000017779.
GeneID281809.
KEGGbta:281809.

Organism-specific databases

CTD3028.

Phylogenomic databases

eggNOGCOG1028.
GeneTreeENSGT00710000106273.
HOVERGENHBG002145.
InParanoidO02691.
KOK08683.
OMALMGANEP.
OrthoDBEOG7JT6X7.
TreeFamTF354307.

Enzyme and pathway databases

BioCycRETL1328306-WGS:GSTH-6663-MONOMER.
BRENDA1.1.1.135. 908.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20805721.

Entry information

Entry nameHCD2_BOVIN
AccessionPrimary (citable) accession number: O02691
Secondary accession number(s): Q2TBG6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families