Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01245
Entry Name
UniProt Accession
Theoretical PI
7.65
Molecular Weight
26923.08
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
3-hydroxyacyl-CoA dehydrogenase type-2
Protein Synonyms/Alias
1.1.1.35; 17-beta-hydroxysteroid dehydrogenase 10; 17-beta-HSD 10; 1.1.1.51; 3-hydroxy-2-methylbutyryl-CoA dehydrogenase; 1.1.1.178; 3-hydroxyacyl-CoA dehydrogenase type II; Endoplasmic reticulum-associated amyloid beta-peptide-binding protein; Mitochondrial ribonuclease P protein 2; Mitochondrial RNase P protein 2; Short-chain type dehydrogenase/reductase XH98G2; Type II HADH;
Gene Name
HSD17B10
Gene Synonyms/Alias
ERAB; HADH2; MRPP2; SCHAD; XH98G2;
Created Date
01-NOV-1997
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
5
Canonical
***MAAACRSVKGLV
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
Functional Description
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 interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD).
Sequence Annotation
Nucleotide-binding: 12 41 NAD.
Active site: 168 168 Proton acceptor.
Binding site: 155 155 Substrate.
Binding site: 172 172 NAD.
Modified residue: 2 2 N-acetylalanine.
Modified residue: 53 53 N6-acetyllysine; alternate.
Modified residue: 53 53 N6-succinyllysine; alternate.
Modified residue: 69 69 N6-acetyllysine.
Modified residue: 99 99 N6-acetyllysine.
Modified residue: 105 105 N6-acetyllysine.
Modified residue: 212 212 N6-acetyllysine; alternate.
Modified residue: 212 212 N6-succinyllysine; alternate.
Protein Length
261 AA.
Protein Sequence
(Canonical)
MAAACRSVKG LVAVITGGAS GLGLATAERL VGQGASAVLL DLPNSGGEAQ AKKLGNNCVF  60
APADVTSEKD VQTALALAKG KFGRVDVAVN CAGIAVASKT YNLKKGQTHT LEDFQRVLDV  120
NLMGTFNVIR LVAGEMGQNE PDQGGQRGVI INTASVAAFE GQVGQAAYSA SKGGIVGMTL  180
PIARDLAPIG IRVMTIAPGL FGTPLLTSLP EKVCNFLASQ VPFPSRLGDP AEYAHLVQAI  240
IENPFLNGEV IRLDGAIRMQ P                                            261
FASTA
(Canonical)
>LipidDB-9606-01245|Q99714
MAAACRSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVF
APADVTSEKDVQTALALAKGKFGRVDVAVNCAGIAVASKTYNLKKGQTHTLEDFQRVLDV
NLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIVGMTL
PIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAI
IENPFLNGEVIRLDGAIRMQP
Gene Ontology
GO:0005737; C:cytoplasm; TAS:ProtInc
GO:0005783; C:endoplasmic reticulum; IEA:Ensembl
GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl
GO:0005759; C:mitochondrial matrix; TAS:Reactome
GO:0005739; C:mitochondrion; ISS:UniProtKB
GO:0005886; C:plasma membrane; TAS:ProtInc
GO:0047015; F:3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC
GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; EXP:Reactome
GO:0008709; F:cholate 7-alpha-dehydrogenase activity; TAS:ProtInc
GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB
GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; IEA:UniProtKB-EC
GO:0009083; P:branched-chain amino acid catabolic process; TAS:Reactome
GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome
GO:0006629; P:lipid metabolic process; TAS:ProtInc
GO:0044281; P:small molecule metabolic process; TAS:Reactome
GO:0008033; P:tRNA processing; IEA:UniProtKB-KW
Interpro
InterPro; IPR002198; DH_sc/Rdtase_SDR
InterPro; IPR002347; Glc/ribitol_DH
InterPro; IPR016040; NAD(P)-bd_dom
InterPro; IPR020904; Sc_DH/Rdtase_CS
Pfam
Pfam; PF00106; adh_short;
SMART
PROSITE
PROSITE; PS00061; ADH_SHORT;
PRINTS
PRINTS; PR00081; GDHRDH;
PRINTS; PR00080; SDRFAMILY;