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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   26-NOV-2014, entry version 115.
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 IDENTIFICATION BY MASS
RP   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). {ECO:0000250}.
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). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family. {ECO:0000305}.
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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=2-261.
DR   PDB; 1E3W; X-ray; 2.00 A; A/B/C/D=2-261.
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   PhylomeDB; O70351; -.
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:0030331; F:estrogen receptor binding; IPI: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. {ECO:0000250}.
FT   CHAIN         2    261       3-hydroxyacyl-CoA dehydrogenase type-2.
FT                                /FTId=PRO_0000054812.
FT   NP_BIND      12     37       NAD. {ECO:0000250}.
FT   ACT_SITE    168    168       Proton acceptor.
FT   BINDING     155    155       Substrate. {ECO:0000269|PubMed:11023795}.
FT   MOD_RES       2      2       N-acetylalanine. {ECO:0000250}.
FT   MOD_RES      53     53       N6-acetyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      53     53       N6-succinyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      69     69       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES      99     99       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     105    105       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     212    212       N6-acetyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES     212    212       N6-succinyllysine; alternate.
FT                                {ECO:0000250}.
FT   CONFLICT      5      5       V -> C (in Ref. 2; AAF14853).
FT                                {ECO:0000305}.
FT   STRAND       12     16       {ECO:0000244|PDB:1E6W}.
FT   TURN         17     19       {ECO:0000244|PDB:1E6W}.
FT   HELIX        21     32       {ECO:0000244|PDB:1E6W}.
FT   STRAND       36     41       {ECO:0000244|PDB:1E6W}.
FT   HELIX        47     54       {ECO:0000244|PDB:1E6W}.
FT   STRAND       58     62       {ECO:0000244|PDB:1E6W}.
FT   HELIX        68     82       {ECO:0000244|PDB:1E6W}.
FT   STRAND       87     90       {ECO:0000244|PDB:1E6W}.
FT   STRAND      100    102       {ECO:0000244|PDB:1E6W}.
FT   TURN        103    106       {ECO:0000244|PDB:1E6W}.
FT   HELIX       111    121       {ECO:0000244|PDB:1E6W}.
FT   HELIX       123    137       {ECO:0000244|PDB:1E6W}.
FT   STRAND      148    153       {ECO:0000244|PDB:1E6W}.
FT   HELIX       157    160       {ECO:0000244|PDB:1E6W}.
FT   HELIX       166    186       {ECO:0000244|PDB:1E6W}.
FT   HELIX       187    189       {ECO:0000244|PDB:1E6W}.
FT   STRAND      191    198       {ECO:0000244|PDB:1E6W}.
FT   STRAND      201    203       {ECO:0000244|PDB:1E6W}.
FT   TURN        204    206       {ECO:0000244|PDB:1E6W}.
FT   HELIX       214    217       {ECO:0000244|PDB:1E6W}.
FT   HELIX       218    220       {ECO:0000244|PDB:1E6W}.
FT   STRAND      222    224       {ECO:0000244|PDB:1E6W}.
FT   HELIX       230    242       {ECO:0000244|PDB:1E6W}.
FT   STRAND      250    254       {ECO:0000244|PDB:1E6W}.
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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