Entry euk:HCD2_MOUSE

ID   HCD2_MOUSE              Reviewed;         261 AA.
AC   O08756;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   10-MAY-2017, entry version 139.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA;
RA   Fu J., Chen X., Stern D., Yan S.D.;
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-6; 193-212 AND 215-226, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RA   Bienvenut W.V.;
RL   Submitted (JUL-2005) to UniProtKB.
RN   [3]
RP   PROTEIN SEQUENCE OF 70-79 AND 131-147, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-53; LYS-107 AND LYS-212,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast, and Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
RA   Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53; LYS-69; LYS-99; LYS-105;
RP   LYS-107 AND LYS-212, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
RA   Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in
RT   mitochondria identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB57689.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U96116; AAB57689.1; ALT_INIT; mRNA.
DR   CCDS; CCDS30471.1; -.
DR   UniGene; Mm.6994; -.
DR   ProteinModelPortal; O08756; -.
DR   SMR; O08756; -.
DR   IntAct; O08756; 3.
DR   MINT; MINT-1861176; -.
DR   STRING; 10090.ENSMUSP00000026289; -.
DR   iPTMnet; O08756; -.
DR   PhosphoSitePlus; O08756; -.
DR   SwissPalm; O08756; -.
DR   SWISS-2DPAGE; O08756; -.
DR   EPD; O08756; -.
DR   MaxQB; O08756; -.
DR   PaxDb; O08756; -.
DR   PeptideAtlas; O08756; -.
DR   PRIDE; O08756; -.
DR   MGI; MGI:1333871; Hsd17b10.
DR   eggNOG; KOG1199; Eukaryota.
DR   eggNOG; ENOG410XNNW; LUCA.
DR   HOVERGEN; HBG002145; -.
DR   InParanoid; O08756; -.
DR   PhylomeDB; O08756; -.
DR   ChiTaRS; Hsd17b10; mouse.
DR   PMAP-CutDB; O08756; -.
DR   PRO; PR:O08756; -.
DR   Proteomes; UP000000589; Unplaced.
DR   CleanEx; MM_HSD17B10; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA: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; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; ISO:MGI.
DR   GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; IEA:UniProtKB-EC.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
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   Acetylation; Complete proteome; Direct protein sequencing;
KW   Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW   tRNA processing.
FT   INIT_MET      1      1       Removed. {ECO:0000269|Ref.2}.
FT   CHAIN         2    261       3-hydroxyacyl-CoA dehydrogenase type-2.
FT                                /FTId=PRO_0000054811.
FT   NP_BIND      12     37       NAD. {ECO:0000250}.
FT   ACT_SITE    168    168       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10001}.
FT   BINDING     155    155       Substrate. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylalanine. {ECO:0000269|Ref.2}.
FT   MOD_RES      53     53       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES      53     53       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES      69     69       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES      99     99       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     105    105       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     107    107       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     107    107       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     212    212       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     212    212       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        12    211       ipfam:adh_short [T]
FT   MYHIT       155    183       ipat:ADH_SHORT [T]
SQ   SEQUENCE   261 AA;  27419 MW;  61213B13E2839D41 CRC64;
     MAAAVRSVKG LVAVVTGGAS GPWLATAKRL VGQGATAVLL DVPDSEGESQ AKKLGESCIF
     APANVTSEKE IQAALTLAKE KFGRIDVAVN CAGIAVAIKT YHQKKNKIHT LEDFQRVINV
     NLIGTFNVIR LVAGEMGQNE PDQGGQRGVI INTASVAAFE GQVGQAAYSA SKGGIDGMTL
     PIARDLAPTG IRVVTIAPGL FATPLLTTLP EKVRNFLASQ VPFPSRLGDP AEYAHLVQTI
     IENPFLNGEV IRLDGAIRMQ P
//