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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   28-FEB-2018, entry version 137.
DE   RecName: Full=3-hydroxyacyl-CoA dehydrogenase type-2;
DE            EC=1.1.1.35 {ECO:0000250|UniProtKB:Q99714};
DE   AltName: Full=17-beta-hydroxysteroid dehydrogenase 10;
DE            Short=17-beta-HSD 10;
DE            EC=1.1.1.51 {ECO:0000250|UniProtKB:Q99714};
DE   AltName: Full=3-hydroxy-2-methylbutyryl-CoA dehydrogenase;
DE            EC=1.1.1.178 {ECO:0000250|UniProtKB:Q99714};
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; Myomorpha;
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: Mitochondrial dehydrogenase that catalyzes the beta-
CC       oxidation at position 17 of androgens and estrogens and has 3-
CC       alpha-hydroxysteroid dehydrogenase activity with androsterone.
CC       Catalyzes the third step in the beta-oxidation of fatty acids.
CC       Carries out oxidative conversions of 7-alpha-OH and 7-beta-OH bile
CC       acids. Also exhibits 20-beta-OH and 21-OH dehydrogenase activities
CC       with C21 steroids. By interacting with intracellular amyloid-beta,
CC       it may contribute to the neuronal dysfunction associated with
CC       Alzheimer disease (AD). Essential for structural and functional
CC       integrity of mitochondria. {ECO:0000250|UniProtKB:Q99714}.
CC   -!- FUNCTION: In addition to mitochondrial dehydrogenase activity,
CC       moonlights as a component of mitochondrial ribonuclease P, a
CC       complex that cleaves tRNA molecules in their 5'-ends. Together
CC       with HSD17B10/MRPP2, forms a subcomplex of the mitochondrial
CC       ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays
CC       functions that are independent of the ribonuclease P activity. The
CC       MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-
CC       methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9,
CC       respectively) in tRNAs; HSD17B10/MRPP2 acting as a non-catalytic
CC       subunit. The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation
CC       platform: following 5'-end cleavage by the mitochondrial
CC       ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the
CC       efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA
CC       product after ELAC2 processing and presents the nascent tRNA to
CC       the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme.
CC       {ECO:0000250|UniProtKB:Q99714}.
CC   -!- CATALYTIC ACTIVITY: (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA +
CC       NAD(+) = 2-methylacetoacetyl-CoA + NADH.
CC       {ECO:0000250|UniProtKB:Q99714}.
CC   -!- CATALYTIC ACTIVITY: Testosterone + NAD(P)(+) = androst-4-ene-3,17-
CC       dione + NAD(P)H. {ECO:0000250|UniProtKB:Q99714}.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
CC       + NADH. {ECO:0000250|UniProtKB:Q99714}.
CC   -!- SUBUNIT: Homotetramer. Component of mitochondrial ribonuclease P,
CC       a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and MRPP31.
CC       Interacts with TRMT10C/MRPP1; forming the MRPP1-MRPP2 subcomplex
CC       of the mitochondrial ribonuclease P complex.
CC       {ECO:0000250|UniProtKB:Q99714}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion
CC       {ECO:0000250|UniProtKB:Q99714}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family. {ECO:0000305}.
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; -.
DR   IntAct; O70351; 1.
DR   STRING; 10116.ENSRNOP00000043608; -.
DR   iPTMnet; O70351; -.
DR   PhosphoSitePlus; O70351; -.
DR   PaxDb; O70351; -.
DR   PRIDE; O70351; -.
DR   GeneID; 63864; -.
DR   KEGG; rno:63864; -.
DR   CTD; 3028; -.
DR   RGD; 69231; Hsd17b10.
DR   eggNOG; KOG1199; Eukaryota.
DR   eggNOG; ENOG410XNNW; LUCA.
DR   HOVERGEN; HBG002145; -.
DR   InParanoid; O70351; -.
DR   KO; K08683; -.
DR   PhylomeDB; O70351; -.
DR   SABIO-RK; O70351; -.
DR   EvolutionaryTrace; O70351; -.
DR   PRO; PR:O70351; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISO:RGD.
DR   GO; GO:0030678; C:mitochondrial ribonuclease P complex; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:RGD.
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; ISS:UniProtKB.
DR   GO; GO:0018454; F:acetoacetyl-CoA reductase activity; IDA:RGD.
DR   GO; GO:0001540; F:amyloid-beta 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:0003723; F:RNA binding; ISO:RGD.
DR   GO; GO:0005496; F:steroid binding; IDA:RGD.
DR   GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; ISS:UniProtKB.
DR   GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR   GO; GO:0007569; P:cell aging; IEP:RGD.
DR   GO; GO:0033327; P:Leydig cell differentiation; IEP:RGD.
DR   GO; GO:1990180; P:mitochondrial tRNA 3'-end processing; ISS:UniProtKB.
DR   GO; GO:0097745; P:mitochondrial tRNA 5'-end processing; ISS:UniProtKB.
DR   GO; GO:0070901; P:mitochondrial tRNA methylation; ISS:UniProtKB.
DR   GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:RGD.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
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|UniProtKB:Q99714}.
FT   CHAIN         2    261       3-hydroxyacyl-CoA dehydrogenase type-2.
FT                                /FTId=PRO_0000054812.
FT   NP_BIND      12     37       NAD. {ECO:0000250|UniProtKB:Q99714}.
FT   ACT_SITE    168    168       Proton acceptor.
FT                                {ECO:0000269|PubMed:11023795}.
FT   BINDING     155    155       Substrate. {ECO:0000269|PubMed:11023795}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:Q99714}.
FT   MOD_RES      53     53       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:O08756}.
FT   MOD_RES      53     53       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:O08756}.
FT   MOD_RES      69     69       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:O08756}.
FT   MOD_RES      99     99       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:O08756}.
FT   MOD_RES     105    105       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:O08756}.
FT   MOD_RES     212    212       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:O08756}.
FT   MOD_RES     212    212       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:O08756}.
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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