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 AK1C3_HUMAN             Reviewed;         323 AA.
P42330; A8K2V0; B4DL37; Q5T2L1; Q96DJ1; Q96KI8; Q99530; Q9UCX1;
Q9UII3; Q9UKL9;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 4.
30-AUG-2017, entry version 188.
RecName: Full=Aldo-keto reductase family 1 member C3;
EC=1.-.-.-;
AltName: Full=17-beta-hydroxysteroid dehydrogenase type 5;
Short=17-beta-HSD 5;
AltName: Full=3-alpha-HSD type II, brain;
AltName: Full=3-alpha-hydroxysteroid dehydrogenase type 2;
Short=3-alpha-HSD type 2;
EC=1.1.1.357 {ECO:0000269|PubMed:10622721, ECO:0000269|PubMed:11165022, ECO:0000269|PubMed:7650035, ECO:0000269|PubMed:9415401, ECO:0000269|PubMed:9927279};
AltName: Full=Chlordecone reductase homolog HAKRb;
AltName: Full=Dihydrodiol dehydrogenase 3;
Short=DD-3;
Short=DD3;
AltName: Full=Dihydrodiol dehydrogenase type I;
AltName: Full=HA1753;
AltName: Full=Indanol dehydrogenase;
EC=1.1.1.112;
AltName: Full=Prostaglandin F synthase;
Short=PGFS;
EC=1.1.1.188 {ECO:0000269|PubMed:10622721, ECO:0000269|PubMed:11165022, ECO:0000269|PubMed:7650035, ECO:0000269|PubMed:9415401, ECO:0000269|PubMed:9927279};
AltName: Full=Testosterone 17-beta-dehydrogenase 5;
EC=1.1.1.239 {ECO:0000269|PubMed:10622721, ECO:0000269|PubMed:11165022, ECO:0000269|PubMed:7650035, ECO:0000269|PubMed:9415401, ECO:0000269|PubMed:9927279};
EC=1.1.1.64 {ECO:0000269|PubMed:10622721, ECO:0000269|PubMed:11165022, ECO:0000269|PubMed:7650035, ECO:0000269|PubMed:9415401, ECO:0000269|PubMed:9927279};
AltName: Full=Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase;
EC=1.3.1.20;
Name=AKR1C3; Synonyms=DDH1, HSD17B5, KIAA0119, PGFS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLN-5 AND
ILE-175.
TISSUE=Liver;
PubMed=8274401; DOI=10.1016/0960-0760(93)90308-J;
Qin K.-N., New M.I., Cheng K.-C.;
"Molecular cloning of multiple cDNAs encoding human enzymes
structurally related to 3 alpha-hydroxysteroid dehydrogenase.";
J. Steroid Biochem. Mol. Biol. 46:673-679(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY,
CHARACTERIZATION, TISSUE SPECIFICITY, AND VARIANTS GLN-5 AND ILE-175.
PubMed=7650035; DOI=10.1074/jbc.270.34.20162;
Khanna M., Qin K.-N., Wang R.W., Cheng K.-C.;
"Substrate specificity, gene structure, and tissue-specific
distribution of multiple human 3 alpha-hydroxysteroid
dehydrogenases.";
J. Biol. Chem. 270:20162-20168(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLN-5.
TISSUE=Liver;
PubMed=7626489; DOI=10.1016/0960-0760(95)00019-V;
Khanna M., Qin K.-N., Cheng K.-C.;
"Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and
molecular cloning of multiple cDNAs encoding structurally related
proteins in humans.";
J. Steroid Biochem. Mol. Biol. 53:41-46(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
SPECIFICITY, AND VARIANT GLN-5.
TISSUE=Prostate;
PubMed=9415401; DOI=10.1210/mend.11.13.0026;
Lin H.-K., Jez J.M., Schlegel B.P., Peehl D.M., Pachter J.A.,
Penning T.M.;
"Expression and characterization of recombinant type 2 3 alpha-
hydroxysteroid dehydrogenase (HSD) from human prostate: demonstration
of bifunctional 3 alpha/17 beta-HSD activity and cellular
distribution.";
Mol. Endocrinol. 11:1971-1984(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC
DNA] OF 124-190, FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION,
TISSUE SPECIFICITY, AND VARIANT GLN-5.
TISSUE=Lung;
PubMed=10622721; DOI=10.1016/S0014-5793(99)01551-3;
Suzuki-Yamamoto T., Nishizawa M., Fukui M., Okuda-Ashitaka E.,
Nakajima T., Ito S., Watanabe K.;
"cDNA cloning, expression and characterization of human prostaglandin
F synthase.";
FEBS Lett. 462:335-340(1999).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES,
TISSUE SPECIFICITY, AND VARIANT GLN-5.
TISSUE=Brain;
PubMed=10557352; DOI=10.1073/pnas.96.23.13512;
Griffin L.D., Mellon S.H.;
"Selective serotonin reuptake inhibitors directly alter activity of
neurosteroidogenic enzymes.";
Proc. Natl. Acad. Sci. U.S.A. 96:13512-13517(1999).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=10672042; DOI=10.1046/j.1365-2443.2000.00310.x;
Nishizawa M., Nakajima T., Yasuda K., Kanzaki H., Sasaguri Y.,
Watanabe K., Ito S.;
"Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with
three aldo-keto reductase genes.";
Genes Cells 5:111-125(2000).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY,
CHARACTERIZATION, AND TISSUE SPECIFICITY.
TISSUE=Prostate;
PubMed=11165022; DOI=10.1016/S0303-7207(00)00426-3;
Penning T.M., Burczynski M.E., Jez J.M., Lin H.-K., Ma H., Moore M.,
Ratnam K., Palackal N.;
"Structure-function aspects and inhibitor design of type 5 17beta-
hydroxysteroid dehydrogenase (AKR1C3).";
Mol. Cell. Endocrinol. 171:137-149(2001).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-5.
TISSUE=Bone marrow;
PubMed=7788527; DOI=10.1093/dnares/2.1.37;
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. III.
The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:37-43(1995).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon, and Urinary bladder;
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).
[15]
CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, TISSUE SPECIFICITY,
CHARACTERIZATION OF VARIANT ILE-175, AND MUTAGENESIS OF LYS-75.
PubMed=9927279; DOI=10.1210/endo.140.2.6531;
Dufort I., Rheault P., Huang X.-F., Soucy P., Luu-The V.;
"Characteristics of a highly labile human type 5 17beta-hydroxysteroid
dehydrogenase.";
Endocrinology 140:568-574(1999).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
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).
[18]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH PROSTAGLANDIN
H(2); NADPH AND RUTIN.
PubMed=14979715; DOI=10.1021/bi036046x;
Komoto J., Yamada T., Watanabe K., Takusagawa F.;
"Crystal structure of human prostaglandin F synthase (AKR1C3).";
Biochemistry 43:2188-2198(2004).
[19]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH FLUFENAMIC ACID
AND INDOMETHACIN.
PubMed=14996743; DOI=10.1158/0008-5472.CAN-03-2847;
Lovering A.L., Ride J.P., Bunce C.M., Desmond J.C., Cummings S.M.,
White S.A.;
"Crystal structures of prostaglandin D(2) 11-ketoreductase (AKR1C3) in
complex with the nonsteroidal anti-inflammatory drugs flufenamic acid
and indomethacin.";
Cancer Res. 64:1802-1810(2004).
[20]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NADP AND
DELTA4-3 ANDROSTENE-3,17-DIONE, AND IMPORTANCE OF TRP-227 AND PHE-306
IN LIGAND RECOGNITION AND PRODUCT RELEASE.
PubMed=15087468; DOI=10.1210/me.2004-0032;
Qiu W., Zhou M., Labrie F., Lin S.-X.;
"Crystal structures of the multispecific 17beta-hydroxysteroid
dehydrogenase type 5: critical androgen regulation in human peripheral
tissues.";
Mol. Endocrinol. 18:1798-1807(2004).
-!- FUNCTION: Catalyzes the conversion of aldehydes and ketones to
alcohols. Catalyzes the reduction of prostaglandin (PG) D2, PGH2
and phenanthrenequinone (PQ) and the oxidation of 9-alpha,11-beta-
PGF2 to PGD2. Functions as a bi-directional 3-alpha-, 17-beta- and
20-alpha HSD. Can interconvert active androgens, estrogens and
progestins with their cognate inactive metabolites. Preferentially
transforms androstenedione (4-dione) to testosterone.
-!- CATALYTIC ACTIVITY: Trans-1,2-dihydrobenzene-1,2-diol + NADP(+) =
catechol + NADPH.
-!- CATALYTIC ACTIVITY: A 3-alpha-hydroxysteroid + NAD(P)(+) = a 3-
oxosteroid + NAD(P)H. {ECO:0000269|PubMed:10622721,
ECO:0000269|PubMed:11165022, ECO:0000269|PubMed:7650035,
ECO:0000269|PubMed:9415401, ECO:0000269|PubMed:9927279}.
-!- CATALYTIC ACTIVITY: (5Z,13E)-(15S)-9-alpha,11-alpha,15-
trihydroxyprosta-5,13-dienoate + NADP(+) = (5Z,13E)-(15S)-9-
alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH.
{ECO:0000269|PubMed:10622721, ECO:0000269|PubMed:11165022,
ECO:0000269|PubMed:7650035, ECO:0000269|PubMed:9415401,
ECO:0000269|PubMed:9927279}.
-!- CATALYTIC ACTIVITY: Testosterone + NAD(+) = androstenedione +
NADH. {ECO:0000269|PubMed:10622721, ECO:0000269|PubMed:11165022,
ECO:0000269|PubMed:7650035, ECO:0000269|PubMed:9415401,
ECO:0000269|PubMed:9927279}.
-!- CATALYTIC ACTIVITY: Testosterone + NADP(+) = androst-4-ene-3,17-
dione + NADPH. {ECO:0000269|PubMed:10622721,
ECO:0000269|PubMed:11165022, ECO:0000269|PubMed:7650035,
ECO:0000269|PubMed:9415401, ECO:0000269|PubMed:9927279}.
-!- CATALYTIC ACTIVITY: Indan-1-ol + NAD(P)(+) = indanone + NAD(P)H.
-!- ENZYME REGULATION: Strongly inhibited by nonsteroidal anti-
inflammatory drugs (NSAID) including flufenamic acid and
indomethacin. Also inhibited by the flavinoid, rutin, and by
selective serotonin inhibitors (SSRIs).
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=142.1 uM for progesterone {ECO:0000269|PubMed:10557352};
KM=2.37 uM for 5-alpha-dihydrotestosterone
{ECO:0000269|PubMed:10557352};
KM=1.0 uM for androstanediol {ECO:0000269|PubMed:10557352};
Vmax=20.1 nmol/min/mg enzyme with progesterone as substrate
{ECO:0000269|PubMed:10557352};
Vmax=1.8 nmol/min/mg enzyme with 5-alpha-dihydrotestosterone as
substrate {ECO:0000269|PubMed:10557352};
Vmax=4.4 nmol/min/mg enzyme with androstanediol as substrate
{ECO:0000269|PubMed:10557352};
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P42330-1; Sequence=Displayed;
Name=2;
IsoId=P42330-2; Sequence=VSP_055798;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in many tissues including adrenal
gland, brain, kidney, liver, lung, mammary gland, placenta, small
intestine, colon, spleen, prostate and testis. The dominant HSD in
prostate and mammary gland. In the prostate, higher levels in
epithelial cells than in stromal cells. In the brain, expressed in
medulla, spinal cord, frontotemporal lobes, thalamus, subthalamic
nuclei and amygdala. Weaker expression in the hippocampus,
substantia nigra and caudate. {ECO:0000269|PubMed:10557352,
ECO:0000269|PubMed:10622721, ECO:0000269|PubMed:11165022,
ECO:0000269|PubMed:7650035, ECO:0000269|PubMed:9415401,
ECO:0000269|PubMed:9927279}.
-!- SIMILARITY: Belongs to the aldo/keto reductase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA04619.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/AKR1C3ID612ch10p15.html";
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EMBL; S68288; AAD14011.1; -; mRNA.
EMBL; L43839; AAB41916.1; -; Genomic_DNA.
EMBL; L43831; AAB41916.1; JOINED; Genomic_DNA.
EMBL; L43832; AAB41916.1; JOINED; Genomic_DNA.
EMBL; L43833; AAB41916.1; JOINED; Genomic_DNA.
EMBL; L43834; AAB41916.1; JOINED; Genomic_DNA.
EMBL; L43835; AAB41916.1; JOINED; Genomic_DNA.
EMBL; L43836; AAB41916.1; JOINED; Genomic_DNA.
EMBL; L43837; AAB41916.1; JOINED; Genomic_DNA.
EMBL; L43838; AAB41916.1; JOINED; Genomic_DNA.
EMBL; AB018580; BAA88488.1; -; mRNA.
EMBL; AB028065; BAA88489.1; -; Genomic_DNA.
EMBL; AF149416; AAF07272.2; -; mRNA.
EMBL; AB032157; BAA92892.1; -; Genomic_DNA.
EMBL; D17793; BAA04619.2; ALT_INIT; mRNA.
EMBL; BT007286; AAP35950.1; -; mRNA.
EMBL; AK290365; BAF83054.1; -; mRNA.
EMBL; AK296829; BAG59399.1; -; mRNA.
EMBL; AL391427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471072; EAW86454.1; -; Genomic_DNA.
EMBL; BC001479; AAH01479.1; -; mRNA.
EMBL; BC019230; AAH19230.1; -; mRNA.
CCDS; CCDS7063.1; -. [P42330-1]
PIR; B57407; B57407.
PIR; I73674; I73674.
RefSeq; NP_001240837.1; NM_001253908.1.
RefSeq; NP_003730.4; NM_003739.5. [P42330-1]
UniGene; Hs.78183; -.
PDB; 1RY0; X-ray; 1.69 A; A/B=1-323.
PDB; 1RY8; X-ray; 1.69 A; A/B=1-323.
PDB; 1S1P; X-ray; 1.20 A; A=1-323.
PDB; 1S1R; X-ray; 2.00 A; A=1-323.
PDB; 1S2A; X-ray; 1.70 A; A=1-323.
PDB; 1S2C; X-ray; 1.80 A; A=1-323.
PDB; 1XF0; X-ray; 2.00 A; A=1-323.
PDB; 1ZQ5; X-ray; 1.30 A; A=1-323.
PDB; 2F38; X-ray; 2.00 A; A=1-323.
PDB; 2FGB; X-ray; 1.35 A; A=1-323.
PDB; 3R43; X-ray; 2.00 A; A=1-323.
PDB; 3R58; X-ray; 2.30 A; A=1-323.
PDB; 3R6I; X-ray; 1.95 A; A=1-323.
PDB; 3R7M; X-ray; 2.10 A; A=1-323.
PDB; 3R8G; X-ray; 1.80 A; A=1-323.
PDB; 3R8H; X-ray; 1.90 A; A=1-323.
PDB; 3R94; X-ray; 2.01 A; A=1-323.
PDB; 3UFY; X-ray; 1.90 A; A=1-323.
PDB; 3UG8; X-ray; 1.73 A; A=1-323.
PDB; 3UGR; X-ray; 1.65 A; A=1-323.
PDB; 3UWE; X-ray; 1.68 A; A=1-323.
PDB; 4DBS; X-ray; 1.85 A; A/B=1-323.
PDB; 4DBU; X-ray; 2.53 A; A/B=1-323.
PDB; 4DBW; X-ray; 1.80 A; A/B=1-323.
PDB; 4DZ5; X-ray; 1.70 A; A=1-323.
PDB; 4FA3; X-ray; 2.20 A; A=1-323.
PDB; 4FAL; X-ray; 2.00 A; A=1-323.
PDB; 4FAM; X-ray; 2.00 A; A/B=1-323.
PDB; 4H7C; X-ray; 1.97 A; A=1-323.
PDB; 4HMN; X-ray; 2.40 A; A=1-323.
PDB; 4WDT; X-ray; 1.50 A; A=1-323.
PDB; 4WDU; X-ray; 1.70 A; A=1-323.
PDB; 4WDW; X-ray; 1.94 A; A/B=1-323.
PDB; 4WDX; X-ray; 1.64 A; A/B=1-323.
PDB; 4WRH; X-ray; 1.60 A; A=1-323.
PDB; 4XVD; X-ray; 2.81 A; A/B=1-323.
PDB; 4XVE; X-ray; 1.55 A; A=1-323.
PDB; 4YVV; X-ray; 2.30 A; A/B=1-323.
PDB; 4YVX; X-ray; 2.30 A; A/B=1-323.
PDB; 4ZFC; X-ray; 2.00 A; A/B=1-323.
PDB; 5HNT; X-ray; 2.00 A; A/C=6-320.
PDB; 5HNU; X-ray; 2.00 A; A/C=6-320.
PDB; 5JM5; X-ray; 1.99 A; A/B=1-323.
PDBsum; 1RY0; -.
PDBsum; 1RY8; -.
PDBsum; 1S1P; -.
PDBsum; 1S1R; -.
PDBsum; 1S2A; -.
PDBsum; 1S2C; -.
PDBsum; 1XF0; -.
PDBsum; 1ZQ5; -.
PDBsum; 2F38; -.
PDBsum; 2FGB; -.
PDBsum; 3R43; -.
PDBsum; 3R58; -.
PDBsum; 3R6I; -.
PDBsum; 3R7M; -.
PDBsum; 3R8G; -.
PDBsum; 3R8H; -.
PDBsum; 3R94; -.
PDBsum; 3UFY; -.
PDBsum; 3UG8; -.
PDBsum; 3UGR; -.
PDBsum; 3UWE; -.
PDBsum; 4DBS; -.
PDBsum; 4DBU; -.
PDBsum; 4DBW; -.
PDBsum; 4DZ5; -.
PDBsum; 4FA3; -.
PDBsum; 4FAL; -.
PDBsum; 4FAM; -.
PDBsum; 4H7C; -.
PDBsum; 4HMN; -.
PDBsum; 4WDT; -.
PDBsum; 4WDU; -.
PDBsum; 4WDW; -.
PDBsum; 4WDX; -.
PDBsum; 4WRH; -.
PDBsum; 4XVD; -.
PDBsum; 4XVE; -.
PDBsum; 4YVV; -.
PDBsum; 4YVX; -.
PDBsum; 4ZFC; -.
PDBsum; 5HNT; -.
PDBsum; 5HNU; -.
PDBsum; 5JM5; -.
ProteinModelPortal; P42330; -.
SMR; P42330; -.
BioGrid; 114196; 9.
IntAct; P42330; 5.
MINT; MINT-1379107; -.
STRING; 9606.ENSP00000369927; -.
BindingDB; P42330; -.
ChEMBL; CHEMBL4681; -.
DrugBank; DB03461; 2'-Monophosphoadenosine 5'-Diphosphoribose.
DrugBank; DB01536; 4-Androstenedione.
DrugBank; DB00905; Bimatoprost.
DrugBank; DB00997; Doxorubicin.
DrugBank; DB02266; Flufenamic Acid.
DrugBank; DB00157; NADH.
DrugBank; DB01698; Rutin.
GuidetoPHARMACOLOGY; 1382; -.
SwissLipids; SLP:000000804; -.
SwissLipids; SLP:000001647; -. [P42330-1]
iPTMnet; P42330; -.
PhosphoSitePlus; P42330; -.
BioMuta; AKR1C3; -.
DMDM; 308153646; -.
DOSAC-COBS-2DPAGE; P42330; -.
EPD; P42330; -.
MaxQB; P42330; -.
PaxDb; P42330; -.
PeptideAtlas; P42330; -.
PRIDE; P42330; -.
DNASU; 8644; -.
Ensembl; ENST00000380554; ENSP00000369927; ENSG00000196139. [P42330-1]
GeneID; 8644; -.
KEGG; hsa:8644; -.
UCSC; uc001ihu.4; human. [P42330-1]
CTD; 8644; -.
DisGeNET; 8644; -.
GeneCards; AKR1C3; -.
HGNC; HGNC:386; AKR1C3.
HPA; CAB010874; -.
HPA; HPA068265; -.
MIM; 603966; gene.
neXtProt; NX_P42330; -.
OpenTargets; ENSG00000196139; -.
PharmGKB; PA24679; -.
eggNOG; KOG1577; Eukaryota.
eggNOG; COG0656; LUCA.
GeneTree; ENSGT00760000119041; -.
HOVERGEN; HBG000020; -.
InParanoid; P42330; -.
KO; K04119; -.
OrthoDB; EOG091G0D69; -.
PhylomeDB; P42330; -.
TreeFam; TF106492; -.
BioCyc; MetaCyc:HS03054-MONOMER; -.
BRENDA; 1.1.1.188; 2681.
BRENDA; 1.1.1.21; 2681.
BRENDA; 1.1.1.213; 2681.
BRENDA; 1.1.1.239; 2681.
BRENDA; 1.1.1.357; 2681.
BRENDA; 1.1.1.64; 2681.
BRENDA; 1.3.1.20; 2681.
Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-HSA-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
Reactome; R-HSA-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
Reactome; R-HSA-5365859; RA biosynthesis pathway.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
SABIO-RK; P42330; -.
ChiTaRS; AKR1C3; human.
EvolutionaryTrace; P42330; -.
GeneWiki; AKR1C3; -.
GenomeRNAi; 8644; -.
PRO; PR:P42330; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000196139; -.
CleanEx; HS_AKR1C3; -.
ExpressionAtlas; P42330; baseline and differential.
Genevisible; P42330; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; IDA:LIFEdb.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0047020; F:15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity; IDA:UniProtKB.
GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IDA:UniProtKB.
GO; GO:0004033; F:aldo-keto reductase (NADP) activity; TAS:UniProtKB.
GO; GO:0047023; F:androsterone dehydrogenase activity; IDA:UniProtKB.
GO; GO:0047787; F:delta4-3-oxosteroid 5beta-reductase activity; IDA:UniProtKB.
GO; GO:0035410; F:dihydrotestosterone 17-beta-dehydrogenase activity; IDA:UniProtKB.
GO; GO:0045550; F:geranylgeranyl reductase activity; IDA:UniProtKB.
GO; GO:0047718; F:indanol dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0045703; F:ketoreductase activity; IDA:UniProtKB.
GO; GO:0047086; F:ketosteroid monooxygenase activity; IDA:UniProtKB.
GO; GO:0052650; F:NADP-retinol dehydrogenase activity; TAS:Reactome.
GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:UniProtKB.
GO; GO:0018636; F:phenanthrene 9,10-monooxygenase activity; IDA:UniProtKB.
GO; GO:0036131; F:prostaglandin D2 11-ketoreductase activity; TAS:Reactome.
GO; GO:0036130; F:prostaglandin H2 endoperoxidase reductase activity; TAS:Reactome.
GO; GO:0047017; F:prostaglandin-F synthase activity; IEA:UniProtKB-EC.
GO; GO:0001758; F:retinal dehydrogenase activity; IDA:UniProtKB.
GO; GO:0004745; F:retinol dehydrogenase activity; IDA:UniProtKB.
GO; GO:0047045; F:testosterone 17-beta-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
GO; GO:0047115; F:trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0071276; P:cellular response to cadmium ion; IDA:UniProtKB.
GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
GO; GO:0071384; P:cellular response to corticosteroid stimulus; IDA:UniProtKB.
GO; GO:0071395; P:cellular response to jasmonic acid stimulus; IDA:UniProtKB.
GO; GO:0071799; P:cellular response to prostaglandin D stimulus; IDA:UniProtKB.
GO; GO:0071379; P:cellular response to prostaglandin stimulus; IDA:UniProtKB.
GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:UniProtKB.
GO; GO:0009267; P:cellular response to starvation; IEP:UniProtKB.
GO; GO:0019371; P:cyclooxygenase pathway; TAS:Reactome.
GO; GO:0044597; P:daunorubicin metabolic process; IMP:UniProtKB.
GO; GO:0044598; P:doxorubicin metabolic process; IMP:UniProtKB.
GO; GO:0016488; P:farnesol catabolic process; IDA:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0030216; P:keratinocyte differentiation; IEP:UniProtKB.
GO; GO:0008584; P:male gonad development; IEP:UniProtKB.
GO; GO:0044259; P:multicellular organismal macromolecule metabolic process; IEP:UniProtKB.
GO; GO:1900053; P:negative regulation of retinoic acid biosynthetic process; IDA:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0010942; P:positive regulation of cell death; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IDA:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IDA:UniProtKB.
GO; GO:0042448; P:progesterone metabolic process; IDA:UniProtKB.
GO; GO:0006693; P:prostaglandin metabolic process; IEP:UniProtKB.
GO; GO:0000060; P:protein import into nucleus, translocation; IDA:UniProtKB.
GO; GO:0048385; P:regulation of retinoic acid receptor signaling pathway; IDA:UniProtKB.
GO; GO:2000224; P:regulation of testosterone biosynthetic process; IMP:UniProtKB.
GO; GO:0070293; P:renal absorption; NAS:UniProtKB.
GO; GO:0007584; P:response to nutrient; IEP:UniProtKB.
GO; GO:0042574; P:retinal metabolic process; IDA:UniProtKB.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0008202; P:steroid metabolic process; IEP:UniProtKB.
GO; GO:0061370; P:testosterone biosynthetic process; IMP:UniProtKB.
CDD; cd06660; Aldo_ket_red; 1.
Gene3D; 3.20.20.100; -; 1.
InterPro; IPR018170; Aldo/ket_reductase_CS.
InterPro; IPR020471; Aldo/keto_reductase.
InterPro; IPR023210; NADP_OxRdtase_dom.
PANTHER; PTHR11732; PTHR11732; 1.
Pfam; PF00248; Aldo_ket_red; 1.
PIRSF; PIRSF000097; AKR; 1.
PRINTS; PR00069; ALDKETRDTASE.
SUPFAM; SSF51430; SSF51430; 1.
PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm; NAD;
NADP; Oxidoreductase; Polymorphism; Reference proteome.
CHAIN 1 323 Aldo-keto reductase family 1 member C3.
/FTId=PRO_0000124638.
NP_BIND 13 22 NADP. {ECO:0000255}.
NP_BIND 217 280 NADP. {ECO:0000250}.
ACT_SITE 55 55 Proton donor. {ECO:0000250}.
BINDING 117 117 Substrate. {ECO:0000250}.
SITE 54 54 Important for substrate specificity.
{ECO:0000250}.
SITE 84 84 Lowers pKa of active site Tyr.
{ECO:0000250}.
SITE 227 227 Involved in ligand recognition and
product release.
SITE 306 306 Involved in ligand recognition and
product release.
VAR_SEQ 1 119 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055798.
VARIANT 5 5 H -> Q (in dbSNP:rs12529).
{ECO:0000269|PubMed:10557352,
ECO:0000269|PubMed:10622721,
ECO:0000269|PubMed:7626489,
ECO:0000269|PubMed:7650035,
ECO:0000269|PubMed:7788527,
ECO:0000269|PubMed:8274401,
ECO:0000269|PubMed:9415401}.
/FTId=VAR_013288.
VARIANT 66 66 R -> Q (in dbSNP:rs35961894).
/FTId=VAR_032767.
VARIANT 77 77 E -> G (in dbSNP:rs11551177).
/FTId=VAR_061001.
VARIANT 170 170 R -> C (in dbSNP:rs35575889).
/FTId=VAR_032768.
VARIANT 175 175 M -> I (no effect on 17beta-HSD activity;
dbSNP:rs1131132).
{ECO:0000269|PubMed:7650035,
ECO:0000269|PubMed:8274401,
ECO:0000269|PubMed:9927279}.
/FTId=VAR_013289.
VARIANT 180 180 P -> S (in dbSNP:rs34186955).
/FTId=VAR_032769.
MUTAGEN 75 75 K->E: No effect on 17beta-HSD activity.
{ECO:0000269|PubMed:9927279}.
CONFLICT 3 3 S -> P (in Ref. 3; no nucleotide entry).
{ECO:0000305}.
CONFLICT 6 6 Q -> K (in Ref. 3; no nucleotide entry).
{ECO:0000305}.
CONFLICT 38 38 T -> S (in Ref. 6; AAF07272).
{ECO:0000305}.
CONFLICT 75 75 K -> E (in Ref. 1; AAD14011 and 3; no
nucleotide entry). {ECO:0000305}.
CONFLICT 75 75 K -> M (in Ref. 2; AAB41916).
{ECO:0000305}.
CONFLICT 89 89 F -> S (in Ref. 6; AAF07272).
{ECO:0000305}.
CONFLICT 270 270 K -> R (in Ref. 6; AAF07272).
{ECO:0000305}.
STRAND 7 9 {ECO:0000244|PDB:1S1P}.
STRAND 15 22 {ECO:0000244|PDB:1S1P}.
HELIX 33 44 {ECO:0000244|PDB:1S1P}.
STRAND 48 50 {ECO:0000244|PDB:1S1P}.
HELIX 53 55 {ECO:0000244|PDB:1S1P}.
HELIX 58 70 {ECO:0000244|PDB:1S1P}.
HELIX 76 78 {ECO:0000244|PDB:1S1P}.
STRAND 80 85 {ECO:0000244|PDB:1S1P}.
HELIX 87 89 {ECO:0000244|PDB:1S1P}.
HELIX 92 94 {ECO:0000244|PDB:1S1P}.
HELIX 95 106 {ECO:0000244|PDB:1S1P}.
STRAND 111 116 {ECO:0000244|PDB:1S1P}.
STRAND 124 126 {ECO:0000244|PDB:1ZQ5}.
STRAND 133 135 {ECO:0000244|PDB:4WDU}.
HELIX 144 156 {ECO:0000244|PDB:1S1P}.
STRAND 159 167 {ECO:0000244|PDB:1S1P}.
HELIX 170 177 {ECO:0000244|PDB:1S1P}.
STRAND 187 192 {ECO:0000244|PDB:1S1P}.
HELIX 200 208 {ECO:0000244|PDB:1S1P}.
STRAND 212 217 {ECO:0000244|PDB:1S1P}.
TURN 225 227 {ECO:0000244|PDB:1S1P}.
HELIX 235 237 {ECO:0000244|PDB:1S1P}.
HELIX 239 248 {ECO:0000244|PDB:1S1P}.
HELIX 252 262 {ECO:0000244|PDB:1S1P}.
STRAND 266 270 {ECO:0000244|PDB:1S1P}.
HELIX 274 280 {ECO:0000244|PDB:1S1P}.
HELIX 281 285 {ECO:0000244|PDB:1S1P}.
HELIX 290 297 {ECO:0000244|PDB:1S1P}.
HELIX 309 312 {ECO:0000244|PDB:1S1P}.
HELIX 318 320 {ECO:0000244|PDB:4WRH}.
SEQUENCE 323 AA; 36853 MW; 86A7690D9498C6FD CRC64;
MDSKHQCVKL NDGHFMPVLG FGTYAPPEVP RSKALEVTKL AIEAGFRHID SAHLYNNEEQ
VGLAIRSKIA DGSVKREDIF YTSKLWSTFH RPELVRPALE NSLKKAQLDY VDLYLIHSPM
SLKPGEELSP TDENGKVIFD IVDLCTTWEA MEKCKDAGLA KSIGVSNFNR RQLEMILNKP
GLKYKPVCNQ VECHPYFNRS KLLDFCKSKD IVLVAYSALG SQRDKRWVDP NSPVLLEDPV
LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTA EDMKAIDGLD
RNLHYFNSDS FASHPNYPYS DEY


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