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Database: UniProt
Entry: O70351
LinkDB: O70351
Original site: O70351 
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   19-MAR-2014, entry version 111.
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            EC=1.1.1.51;
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. Catalyzes the beta-oxidation at position 17 of
CC       androgens and estrogens and has 3-alpha-hydroxysteroid
CC       dehydrogenase activity with androsterone. Catalyzes the third step
CC       in the beta-oxidation of fatty acids. Carries out oxidative
CC       conversions of 7-alpha-OH and 7-beta-OH bile acids. Also exhibits
CC       20-beta-OH and 21-OH dehydrogenase activities with C21 steroids
CC       (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   -!- CATALYTIC ACTIVITY: Testosterone + NAD(P)(+) = androst-4-ene-3,17-
CC       dione + NAD(P)H.
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   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   MINT; MINT-4568352; -.
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   SABIO-RK; O70351; -.
DR   EvolutionaryTrace; O70351; -.
DR   NextBio; 612472; -.
DR   PRO; PR:O70351; -.
DR   Genevestigator; O70351; -.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0047015; F:3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-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:0030283; F:testosterone dehydrogenase [NAD(P)] activity; IEA:UniProtKB-EC.
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   MOD_RES      53     53       N6-acetyllysine; alternate (By
FT                                similarity).
FT   MOD_RES      53     53       N6-succinyllysine; alternate (By
FT                                similarity).
FT   MOD_RES      69     69       N6-acetyllysine (By similarity).
FT   MOD_RES      99     99       N6-acetyllysine (By similarity).
FT   MOD_RES     105    105       N6-acetyllysine (By similarity).
FT   MOD_RES     212    212       N6-acetyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     212    212       N6-succinyllysine; alternate (By
FT                                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
//
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