ID HCD2_RAT Reviewed; 261 AA.
AC O70351; Q9QYD4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-APR-2013, entry version 104.
DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase type-2;
DE EC=1.1.1.35;
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase 10;
DE Short=17-beta-HSD 10;
DE AltName: Full=3-hydroxy-2-methylbutyryl-CoA dehydrogenase;
DE EC=1.1.1.178;
DE AltName: Full=3-hydroxyacyl-CoA dehydrogenase type II;
DE AltName: Full=Endoplasmic reticulum-associated amyloid beta-peptide-binding protein;
DE AltName: Full=Mitochondrial ribonuclease P protein 2;
DE Short=Mitochondrial RNase P protein 2;
DE AltName: Full=Type II HADH;
GN Name=Hsd17b10; Synonyms=Erab, Hadh2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Gunn-Moore F.J., Tavare J.M.;
RT "Rattus norvegicus amyloid beta-peptide binding protein (ERAB) mRNA.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Yang S.-Y., He X.-Y.;
RT "Molecular cloning and characterization of the cDNA of rat brain short
RT chain L-3-hydroxyacyl-CoA dehydrogenase.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 117-130 AND 193-212, AND MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD AND
RP SUBSTRATE.
RC TISSUE=Brain;
RX PubMed=11023795; DOI=10.1006/jmbi.2000.4139;
RA Powell A.J., Read J.A., Banfield M.J., Gunn-Moore F., Yan S.D.,
RA Lustbader J., Stern A.R., Stern D.M., Brady R.L.;
RT "Recognition of structurally diverse substrates by type II 3-
RT hydroxyacyl-CoA dehydrogenase (HADH II)/amyloid-beta binding alcohol
RT dehydrogenase (ABAD).";
RL J. Mol. Biol. 303:311-327(2000).
CC -!- FUNCTION: Functions in mitochondrial tRNA maturation. Part of
CC mitochondrial ribonuclease P, an enzyme composed of MRPP1/TRMT10C,
CC MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in
CC their 5'-ends (By similarity).
CC -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
CC + NADH.
CC -!- CATALYTIC ACTIVITY: (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA +
CC NAD(+) = 2-methylacetoacetyl-CoA + NADH.
CC -!- SUBUNIT: Homotetramer. Interacts with MRPP1/TRMT10C and
CC MRPP3/KIAA0391 (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC (SDR) family.
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DR EMBL; AF049878; AAC05747.1; -; mRNA.
DR EMBL; AF069770; AAF14853.1; -; mRNA.
DR IPI; IPI00886470; -.
DR RefSeq; NP_113870.1; NM_031682.1.
DR UniGene; Rn.2700; -.
DR PDB; 1E3S; X-ray; 2.00 A; A/B/C/D=1-261.
DR PDB; 1E3W; X-ray; 2.00 A; A/B/C/D=1-261.
DR PDB; 1E6W; X-ray; 1.70 A; A/B/C/D=2-261.
DR PDBsum; 1E3S; -.
DR PDBsum; 1E3W; -.
DR PDBsum; 1E6W; -.
DR ProteinModelPortal; O70351; -.
DR SMR; O70351; 7-261.
DR IntAct; O70351; 1.
DR PaxDb; O70351; -.
DR PRIDE; O70351; -.
DR GeneID; 63864; -.
DR KEGG; rno:63864; -.
DR CTD; 3028; -.
DR RGD; 69231; Hsd17b10.
DR eggNOG; COG1028; -.
DR HOVERGEN; HBG002145; -.
DR InParanoid; O70351; -.
DR KO; K08683; -.
DR OrthoDB; EOG46MBKC; -.
DR SABIO-RK; O70351; -.
DR EvolutionaryTrace; O70351; -.
DR NextBio; 612472; -.
DR ArrayExpress; O70351; -.
DR Genevestigator; O70351; -.
DR GermOnline; ENSRNOG00000003049; Rattus norvegicus.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0047015; F:3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; IEA:EC.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:EC.
DR GO; GO:0018454; F:acetoacetyl-CoA reductase activity; IDA:RGD.
DR GO; GO:0001540; F:beta-amyloid binding; IDA:RGD.
DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IDA:RGD.
DR GO; GO:0051287; F:NAD binding; IDA:RGD.
DR GO; GO:0005496; F:steroid binding; IDA:RGD.
DR GO; GO:0007569; P:cell aging; IEP:RGD.
DR GO; GO:0033327; P:Leydig cell differentiation; IEP:RGD.
DR GO; GO:0051289; P:protein homotetramerization; IDA:RGD.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR InterPro; IPR002347; Glc/ribitol_DH.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase;
KW Reference proteome; tRNA processing.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 261 3-hydroxyacyl-CoA dehydrogenase type-2.
FT /FTId=PRO_0000054812.
FT NP_BIND 12 37 NAD (By similarity).
FT ACT_SITE 168 168 Proton acceptor.
FT BINDING 155 155 Substrate.
FT MOD_RES 2 2 N-acetylalanine (By similarity).
FT CONFLICT 5 5 V -> C (in Ref. 2; AAF14853).
FT STRAND 12 16
FT TURN 17 19
FT HELIX 21 32
FT STRAND 36 41
FT HELIX 47 54
FT STRAND 58 62
FT HELIX 68 82
FT STRAND 87 90
FT STRAND 100 102
FT TURN 103 106
FT HELIX 111 121
FT HELIX 123 137
FT STRAND 148 153
FT HELIX 157 160
FT HELIX 166 186
FT HELIX 187 189
FT STRAND 191 198
FT STRAND 201 203
FT TURN 204 206
FT HELIX 214 217
FT HELIX 218 220
FT STRAND 222 224
FT HELIX 230 242
FT STRAND 250 254
SQ SEQUENCE 261 AA; 27246 MW; 117FD723B11EA227 CRC64;
MAAAVRSVKG LVAVITGGAS GLGLSTAKRL VGQGATAVLL DVPNSEGETE AKKLGGNCIF
APANVTSEKE VQAALTLAKE KFGRIDVAVN CAGIAVAIKT YHEKKNQVHT LEDFQRVINV
NLIGTFNVIR LVAGVMGQNE PDQGGQRGVI INTASVAAFE GQVGQAAYSA SKGGIVGMTL
PIARDLAPIG IRVVTIAPGL FATPLLTTLP DKVRNFLASQ VPFPSRLGDP AEYAHLVQMV
IENPFLNGEV IRLDGAIRMQ P
//
