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17-beta-hydroxysteroid dehydrogenase type 6 (17-beta-HSD 6) (17-beta-HSD6) (EC 1.1.1.105) (EC 1.1.1.239) (EC 1.1.1.62) (3-alpha->beta-hydroxysteroid epimerase) (3-alpha->beta-HSE) (Oxidative 3-alpha hydroxysteroid dehydrogenase) (Short chain dehydrogenase/reductase family 9C member 6)

 H17B6_HUMAN             Reviewed;         317 AA.
O14756; O43275;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 154.
RecName: Full=17-beta-hydroxysteroid dehydrogenase type 6;
Short=17-beta-HSD 6;
Short=17-beta-HSD6;
EC=1.1.1.105;
EC=1.1.1.239;
EC=1.1.1.62;
AltName: Full=3-alpha->beta-hydroxysteroid epimerase;
Short=3-alpha->beta-HSE;
AltName: Full=Oxidative 3-alpha hydroxysteroid dehydrogenase;
AltName: Full=Short chain dehydrogenase/reductase family 9C member 6;
Flags: Precursor;
Name=HSD17B6; Synonyms=RODH, SDR9C6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Prostate;
PubMed=9188497; DOI=10.1074/jbc.272.25.15959;
Biswas M.G., Russell D.W.;
"Expression cloning and characterization of oxidative 17beta- and
3alpha-hydroxysteroid dehydrogenases from rat and human prostate.";
J. Biol. Chem. 272:15959-15966(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=10896656; DOI=10.1074/jbc.M000562200;
Huang X.-F., Luu-The V.;
"Molecular characterization of a first human 3(alpha-->beta)-
hydroxysteroid epimerase.";
J. Biol. Chem. 275:29452-29457(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[4]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
PubMed=11360992; DOI=10.1006/abbi.2000.2203;
Chetyrkin S.V., Hu J., Gough W.H., Dumaual N., Kedishvili N.Y.;
"Further characterization of human microsomal 3alpha-hydroxysteroid
dehydrogenase.";
Arch. Biochem. Biophys. 386:1-10(2001).
[5]
FUNCTION.
PubMed=11513953; DOI=10.1016/S0167-4781(01)00247-0;
Huang X.-F., Luu-The V.;
"Gene structure, chromosomal localization and analysis of 3-
ketosteroid reductase activity of the human 3(alpha-->beta)-
hydroxysteroid epimerase.";
Biochim. Biophys. Acta 1520:124-130(2001).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: NAD-dependent oxidoreductase with broad substrate
specificity that shows both oxidative and reductive activity (in
vitro). Has 17-beta-hydroxysteroid dehydrogenase activity towards
various steroids (in vitro). Converts 5-alpha-androstan-3-
alpha,17-beta-diol to androsterone and estradiol to estrone (in
vitro). Has 3-alpha-hydroxysteroid dehydrogenase activity towards
androsterone (in vitro). Has retinol dehydrogenase activity
towards all-trans-retinol (in vitro). Can convert androsterone to
epi-androsterone. Androsterone is first oxidized to 5-alpha-
androstane-3,17-dione and then reduced to epi-andosterone. Can act
on both C-19 and C-21 3-alpha-hydroxysteroids.
{ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992,
ECO:0000269|PubMed:11513953}.
-!- CATALYTIC ACTIVITY: 17-beta-estradiol + NAD(P)(+) = estrone +
NAD(P)H.
-!- CATALYTIC ACTIVITY: Testosterone + NAD(+) = androstenedione +
NADH.
-!- CATALYTIC ACTIVITY: All-trans-retinol-[cellular-retinol-binding-
protein] + NAD(+) = all-trans-retinal-[cellular-retinol-binding-
protein] + NADH.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.19 uM for NAD {ECO:0000269|PubMed:10896656,
ECO:0000269|PubMed:11360992};
KM=0.18 uM for NADH {ECO:0000269|PubMed:10896656,
ECO:0000269|PubMed:11360992};
KM=54 uM for NADPH {ECO:0000269|PubMed:10896656,
ECO:0000269|PubMed:11360992};
KM=940 uM for NADP {ECO:0000269|PubMed:10896656,
ECO:0000269|PubMed:11360992};
KM=3.2 uM for all-trans-retinol {ECO:0000269|PubMed:10896656,
ECO:0000269|PubMed:11360992};
KM=0.24 uM for allopregnanolone {ECO:0000269|PubMed:10896656,
ECO:0000269|PubMed:11360992};
KM=0.13 uM for 3-alpha-androstanediol
{ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992};
KM=0.23 uM for androsterone {ECO:0000269|PubMed:10896656,
ECO:0000269|PubMed:11360992};
KM=0.13 uM for dehydroepiandrosterone
{ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992};
Vmax=1.2 nmol/min/mg enzyme with all-trans-retinol
{ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992};
Vmax=14.7 nmol/min/mg enzyme with allopregnanolone
{ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992};
Vmax=16.5 nmol/min/mg enzyme with 3-alpha-androstanediol
{ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992};
Vmax=35 nmol/min/mg enzyme with androsterone
{ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992};
Vmax=0.90 nmol/min/mg enzyme with dehydroepiandrosterone
{ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992};
Note=The kinetic parameters were determined using microsomes
from transfected cells.;
-!- SUBCELLULAR LOCATION: Microsome membrane
{ECO:0000269|PubMed:11360992}; Peripheral membrane protein
{ECO:0000269|PubMed:11360992}; Lumenal side
{ECO:0000269|PubMed:11360992}. Early endosome membrane
{ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Lumenal
side {ECO:0000305}.
-!- TISSUE SPECIFICITY: Detected in liver and prostate (at protein
level). Detected in adult liver, lung, brain, placenta, prostate,
adrenal gland, testis, mammary gland, spleen, spinal cord and
uterus. Detected in caudate nucleus, and at lower levels in
amygdala, corpus callosum, hippocampus, substantia nigra and
thalamus. Detected in fetal lung, liver and brain.
{ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:9188497}.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB88252.1; Type=Frameshift; Positions=158, 174; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U89281; AAB88252.1; ALT_FRAME; mRNA.
EMBL; AF016509; AAB67236.1; -; mRNA.
EMBL; AF223225; AAF81017.1; -; mRNA.
EMBL; BC020710; AAH20710.1; -; mRNA.
CCDS; CCDS8925.1; -.
RefSeq; NP_003716.2; NM_003725.3.
RefSeq; XP_005269264.1; XM_005269207.1.
RefSeq; XP_005269265.1; XM_005269208.1.
RefSeq; XP_005269266.1; XM_005269209.1.
RefSeq; XP_006719735.1; XM_006719672.1.
RefSeq; XP_011537227.1; XM_011538925.1.
RefSeq; XP_011537228.1; XM_011538926.1.
RefSeq; XP_011537229.1; XM_011538927.1.
UniGene; Hs.524513; -.
ProteinModelPortal; O14756; -.
BioGrid; 114183; 13.
STRING; 9606.ENSP00000318631; -.
DrugBank; DB00139; Succinic acid.
SwissLipids; SLP:000000807; -.
iPTMnet; O14756; -.
PhosphoSitePlus; O14756; -.
PaxDb; O14756; -.
PeptideAtlas; O14756; -.
PRIDE; O14756; -.
DNASU; 8630; -.
Ensembl; ENST00000322165; ENSP00000318631; ENSG00000025423.
Ensembl; ENST00000554150; ENSP00000452273; ENSG00000025423.
Ensembl; ENST00000554643; ENSP00000451406; ENSG00000025423.
Ensembl; ENST00000555159; ENSP00000450698; ENSG00000025423.
Ensembl; ENST00000555805; ENSP00000451753; ENSG00000025423.
GeneID; 8630; -.
KEGG; hsa:8630; -.
UCSC; uc001smg.3; human.
CTD; 8630; -.
DisGeNET; 8630; -.
EuPathDB; HostDB:ENSG00000025423.11; -.
GeneCards; HSD17B6; -.
HGNC; HGNC:23316; HSD17B6.
HPA; HPA059141; -.
MIM; 606623; gene.
neXtProt; NX_O14756; -.
OpenTargets; ENSG00000025423; -.
PharmGKB; PA142671671; -.
eggNOG; KOG1610; Eukaryota.
eggNOG; ENOG410Y7FK; LUCA.
GeneTree; ENSGT00900000140775; -.
HOVERGEN; HBG005482; -.
InParanoid; O14756; -.
KO; K13369; -.
OMA; DVTKMES; -.
OrthoDB; EOG091G0LMI; -.
PhylomeDB; O14756; -.
TreeFam; TF325617; -.
BRENDA; 1.1.1.62; 2681.
Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
GeneWiki; HSD17B6; -.
GenomeRNAi; 8630; -.
PRO; PR:O14756; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000025423; -.
CleanEx; HS_HSD17B6; -.
ExpressionAtlas; O14756; baseline and differential.
Genevisible; O14756; HS.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; NAS:UniProtKB.
GO; GO:0003824; F:catalytic activity; TAS:ProtInc.
GO; GO:0009055; F:electron carrier activity; TAS:UniProtKB.
GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0016491; F:oxidoreductase activity; NAS:UniProtKB.
GO; GO:0004745; F:retinol dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
GO; GO:0006702; P:androgen biosynthetic process; NAS:UniProtKB.
GO; GO:0006710; P:androgen catabolic process; TAS:UniProtKB.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
Pfam; PF00106; adh_short; 1.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Endosome; Glycoprotein;
Lipid metabolism; Membrane; Microsome; NAD; Oxidoreductase;
Reference proteome; Signal; Steroid metabolism.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 317 17-beta-hydroxysteroid dehydrogenase type
6.
/FTId=PRO_0000303211.
NP_BIND 33 57 NAD. {ECO:0000250}.
ACT_SITE 176 176 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10001}.
BINDING 164 164 Substrate. {ECO:0000255}.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 256 256 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 63 63 E -> D (in Ref. 1; AAB88252).
{ECO:0000305}.
CONFLICT 105 105 G -> R (in Ref. 1; AAB88252).
{ECO:0000305}.
SEQUENCE 317 AA; 35966 MW; 46F1E940605CBEE9 CRC64;
MWLYLAAFVG LYYLLHWYRE RQVVSHLQDK YVFITGCDSG FGNLLARQLD ARGLRVLAAC
LTEKGAEQLR GQTSDRLETV TLDVTKMESI AAATQWVKEH VGDRGLWGLV NNAGILTPIT
LCEWLNTEDS MNMLKVNLIG VIQVTLSMLP LVRRARGRIV NVSSILGRVA FFVGGYCVSK
YGVEAFSDIL RREIQHFGVK ISIVEPGYFR TGMTNMTQSL ERMKQSWKEA PKHIKETYGQ
QYFDALYNIM KEGLLNCSTN LNLVTDCMEH ALTSVHPRTR YSAGWDAKFF FIPLSYLPTS
LADYILTRSW PKPAQAV


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