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Estradiol 17-beta-dehydrogenase 8 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit) (KAR alpha subunit) (3-oxoacyl-[acyl-carrier-protein] reductase) (EC 1.1.1.-) (Protein Ke6) (Ke-6) (Testosterone 17-beta-dehydrogenase 8) (EC 1.1.1.239)

 DHB8_MOUSE              Reviewed;         259 AA.
P50171; Q5M9K0; Q60958; Q60959; Q9Z1W2;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
20-APR-2010, sequence version 2.
20-JUN-2018, entry version 155.
RecName: Full=Estradiol 17-beta-dehydrogenase 8;
EC=1.1.1.62 {ECO:0000269|PubMed:9712896};
AltName: Full=17-beta-hydroxysteroid dehydrogenase 8;
Short=17-beta-HSD 8;
AltName: Full=3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit {ECO:0000250|UniProtKB:Q92506};
Short=KAR alpha subunit {ECO:0000250|UniProtKB:Q92506};
AltName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
EC=1.1.1.- {ECO:0000250|UniProtKB:Q92506};
AltName: Full=Protein Ke6;
Short=Ke-6;
AltName: Full=Testosterone 17-beta-dehydrogenase 8;
EC=1.1.1.239 {ECO:0000269|PubMed:9712896};
Name=Hsd17b8; Synonyms=H2-Ke6, Hke6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DBA/2J; TISSUE=Kidney;
PubMed=8441417; DOI=10.1128/MCB.13.3.1847;
Aziz N., Maxwell M.M., St Jacques B., Brenner B.M.;
"Downregulation of Ke 6, a novel gene encoded within the major
histocompatibility complex, in murine polycystic kidney disease.";
Mol. Cell. Biol. 13:1847-1853(1993).
[2]
ERRATUM.
Aziz N., Maxwell M.M., St Jacques B., Brenner B.M.;
Mol. Cell. Biol. 13:6614-6614(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=7559658; DOI=10.1074/jbc.270.42.25213;
Maxwell M.M., Nearing J., Aziz N.;
"Ke 6 gene. Sequence and organization and aberrant regulation in
murine polycystic kidney disease.";
J. Biol. Chem. 270:25213-25219(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=129/SvJ;
Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L.,
Hall J., Lasky S., Hood L.;
"Sequence of the mouse major histocomaptibility locus class II
region.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
CATALYTIC ACTIVITY, FUNCTION, PATHWAY, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=9712896; DOI=10.1074/jbc.273.35.22664;
Fomitcheva J., Baker M.E., Anderson E., Lee G.Y., Aziz N.;
"Characterization of Ke 6, a new 17beta-hydroxysteroid dehydrogenase,
and its expression in gonadal tissues.";
J. Biol. Chem. 273:22664-22671(1998).
[7]
SUBCELLULAR LOCATION.
PubMed=15923359; DOI=10.1369/jhc.5A6692.2005;
Pelletier G., Luu-The V., Li S., Labrie F.;
"Localization of type 8 17beta-hydroxysteroid dehydrogenase mRNA in
mouse tissues as studied by in situ hybridization.";
J. Histochem. Cytochem. 53:1257-1271(2005).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-158 AND LYS-171, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23576753; DOI=10.1073/pnas.1302961110;
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
"Label-free quantitative proteomics of the lysine acetylome in
mitochondria identifies substrates of SIRT3 in metabolic pathways.";
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
-!- FUNCTION: NAD-dependent 17-beta-hydroxysteroid dehydrogenase with
highest activity towards estradiol. Has very low activity towards
testosterone (PubMed:9712896). The heterotetramer with CBR4 has
NADH-dependent 3-ketoacyl-acyl carrier protein reductase activity,
and thereby plays a role in mitochondrial fatty acid biosynthesis.
Within the heterotetramer, HSD17B8 binds NADH; CBR4 binds NADPD.
{ECO:0000250|UniProtKB:Q92506, ECO:0000269|PubMed:9712896}.
-!- CATALYTIC ACTIVITY: 17-beta-estradiol + NAD(P)(+) = estrone +
NAD(P)H. {ECO:0000269|PubMed:9712896}.
-!- CATALYTIC ACTIVITY: Testosterone + NAD(+) = androstenedione +
NADH. {ECO:0000269|PubMed:9712896}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.110 uM for estradiol {ECO:0000269|PubMed:9712896};
KM=0.422 uM for testosterone {ECO:0000269|PubMed:9712896};
KM=0.368 uM for estrone {ECO:0000269|PubMed:9712896};
KM=0.360 uM for dihydrotestosterone
{ECO:0000269|PubMed:9712896};
Vmax=0.405 nmol/min/mg enzyme for estradiol as substrate
{ECO:0000269|PubMed:9712896};
Vmax=0.123 nmol/min/mg enzyme for testosterone as substrate
{ECO:0000269|PubMed:9712896};
Vmax=0.186 nmol/min/mg enzyme for estrone as substrate
{ECO:0000269|PubMed:9712896};
Vmax=0.081 nmol/min/mg enzyme for dihydrotestosterone as
substrate {ECO:0000269|PubMed:9712896};
-!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
{ECO:0000250|UniProtKB:Q92506}.
-!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
{ECO:0000269|PubMed:9712896}.
-!- SUBUNIT: Heterotetramer with CBR4; contains two molecules of
HSD17B8 and CBR4. {ECO:0000250|UniProtKB:Q92506}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000250|UniProtKB:Q92506}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Short;
IsoId=P50171-1; Sequence=Displayed;
Name=Long;
IsoId=P50171-2; Sequence=VSP_006030;
-!- TISSUE SPECIFICITY: Kidney, liver, testis, ovary, oviduct, uterus,
mammary gland, vagina, prostate, clitoral gland and moderately in
spleen, heart, dorsal skin, brain and lung.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC69902.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U34072; AAC53573.1; -; Genomic_DNA.
EMBL; U34072; AAC53574.1; -; Genomic_DNA.
EMBL; AF100956; AAC69902.1; ALT_SEQ; Genomic_DNA.
EMBL; BC086927; AAH86927.1; -; mRNA.
CCDS; CCDS50071.1; -. [P50171-1]
PIR; A48154; A48154.
RefSeq; NP_038571.2; NM_013543.2. [P50171-1]
UniGene; Mm.275452; -.
ProteinModelPortal; P50171; -.
SMR; P50171; -.
IntAct; P50171; 1.
MINT; P50171; -.
STRING; 10090.ENSMUSP00000038069; -.
iPTMnet; P50171; -.
PhosphoSitePlus; P50171; -.
REPRODUCTION-2DPAGE; P50171; -.
EPD; P50171; -.
MaxQB; P50171; -.
PaxDb; P50171; -.
PeptideAtlas; P50171; -.
PRIDE; P50171; -.
Ensembl; ENSMUST00000045467; ENSMUSP00000038069; ENSMUSG00000073422. [P50171-1]
GeneID; 14979; -.
KEGG; mmu:14979; -.
UCSC; uc008cat.2; mouse. [P50171-1]
CTD; 14979; -.
MGI; MGI:95911; H2-Ke6.
eggNOG; KOG1200; Eukaryota.
eggNOG; COG1028; LUCA.
GeneTree; ENSGT00920000148965; -.
HOVERGEN; HBG002145; -.
InParanoid; P50171; -.
KO; K13370; -.
OMA; GSRNIRC; -.
OrthoDB; EOG091G0N2V; -.
PhylomeDB; P50171; -.
TreeFam; TF313099; -.
Reactome; R-MMU-75105; Fatty acyl-CoA biosynthesis.
SABIO-RK; P50171; -.
UniPathway; UPA00094; -.
UniPathway; UPA00769; -.
PRO; PR:P50171; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000073422; -.
CleanEx; MM_H2-KE6; -.
ExpressionAtlas; P50171; baseline and differential.
Genevisible; P50171; MM.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005740; C:mitochondrial envelope; IDA:MGI.
GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; ISO:MGI.
GO; GO:0047025; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADH) activity; ISS:UniProtKB.
GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IDA:MGI.
GO; GO:0070404; F:NADH binding; ISS:UniProtKB.
GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; IDA:MGI.
GO; GO:0008209; P:androgen metabolic process; IDA:MGI.
GO; GO:0006703; P:estrogen biosynthetic process; ISS:UniProtKB.
GO; GO:0008210; P:estrogen metabolic process; IDA:MGI.
GO; GO:0006633; P:fatty acid biosynthetic process; ISS:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; ISO:MGI.
GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome;
Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
Lipid metabolism; Mitochondrion; NAD; Oxidoreductase; Phosphoprotein;
Reference proteome; Steroid biosynthesis.
CHAIN 1 259 Estradiol 17-beta-dehydrogenase 8.
/FTId=PRO_0000054599.
NP_BIND 13 21 NAD. {ECO:0000250|UniProtKB:Q92506}.
NP_BIND 40 41 NAD. {ECO:0000250|UniProtKB:Q92506}.
NP_BIND 72 74 NAD. {ECO:0000250|UniProtKB:Q92506}.
NP_BIND 167 171 NAD. {ECO:0000250|UniProtKB:Q92506}.
NP_BIND 200 202 NAD. {ECO:0000250|UniProtKB:Q92506}.
ACT_SITE 167 167 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10001}.
BINDING 154 154 Substrate. {ECO:0000250}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 66 66 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 158 158 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 171 171 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
VAR_SEQ 256 259 GLFM -> MRPSWGGGQENRTQVVMRK (in isoform
Long). {ECO:0000305}.
/FTId=VSP_006030.
CONFLICT 229 229 E -> EG (in Ref. 1; AAC53573/AAC53574).
{ECO:0000305}.
SEQUENCE 259 AA; 26588 MW; C4704F02B63C275F CRC64;
MASQLRLRSA LALVTGAGSG IGRAISVRLA AEGAAVAACD LDGAAAQDTV RLLGSPGSED
GAPRGKHAAF QADVSQGPAA RRLLEEVQAC FSRPPSVVVS CAGITRDEFL LHMSEEDWDR
VIAVNLKGTF LVTQAAAQAL VSSGGRGSII NISSIIGKVG NIGQTNYASS KAGVIGLTQT
AARELGRHGI RCNSVLPGFI ATPMTQKMPE KVKDKVTAMI PLGHMGDPED VADVVAFLAS
EDSGYITGAS VEVSGGLFM


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