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O08756

- HCD2_MOUSE

UniProt

O08756 - HCD2_MOUSE

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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

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
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiO08756.
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

        10         20         30         40         50
MAAAVRSVKG LVAVVTGGAS GPWLATAKRL VGQGATAVLL DVPDSEGESQ
60 70 80 90 100
AKKLGESCIF APANVTSEKE IQAALTLAKE KFGRIDVAVN CAGIAVAIKT
110 120 130 140 150
YHQKKNKIHT LEDFQRVINV NLIGTFNVIR LVAGEMGQNE PDQGGQRGVI
160 170 180 190 200
INTASVAAFE GQVGQAAYSA SKGGIDGMTL PIARDLAPTG IRVVTIAPGL
210 220 230 240 250
FATPLLTTLP EKVRNFLASQ VPFPSRLGDP AEYAHLVQTI IENPFLNGEV
260
IRLDGAIRMQ P
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.
InParanoidi O08756.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 122 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