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UniProtKB/Swiss-Prot entry Q9R092


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name H17B6_MOUSE
Primary accession number Q9R092
Secondary accession numbers None
Integrated into Swiss-Prot on September 11, 2007
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 60)
Name and origin of the protein
Protein name Hydroxysteroid 17-beta dehydrogenase 6 [Precursor]
Synonyms EC 1.1.1.62
EC 1.1.1.63
EC 1.1.1.105
17-beta-HSD6
17-beta-HSD9
Oxidative 3-alpha hydroxysteroid dehydrogenase
3-alpha->beta-hydroxysteroid epimerase
3-alpha->beta-HSE
Gene name
Name: Hsd17b6
Synonyms: Gm182, Hsd17b9, Rdh8
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Liver;
DOI=10.1210/en.140.11.5275; PubMed=10537158 [NCBI, ExPASy, EBI, Israel, Japan]
Su J., Lin M., Napoli J.L.;
"Complementary deoxyribonucleic acid cloning and enzymatic characterization of a novel 17beta/3alpha-hydroxysteroid/retinoid short chain dehydrogenase/reductase.";
Endocrinology 140:5275-5284(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Small intestine;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Liver;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
  • 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).
  • CATALYTIC ACTIVITY: Estradiol-17-beta + NAD(P)+ = estrone + NAD(P)H.
  • CATALYTIC ACTIVITY: Testosterone + NAD+ = androst-4-ene-3,17-dione + NADH.
  • CATALYTIC ACTIVITY: Retinol + NAD+ = retinal + NADH.
  • SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane protein; Lumenal side. Early endosome membrane; Peripheral membrane protein; Lumenal side (Potential).
  • TISSUE SPECIFICITY: Detected in liver.
  • SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF103797; AAF04761.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK008212; BAB25536.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021836; AAH21836.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_038814.1; -.
UniGene Mm.26719
3D structure databases
HSSP P14061; 1FDU. [HSSP ENTRY / PDB]
ModBase Q9R092.
Organism-specific databases
MGI MGI:1351670; Hsd17b6.
Gene expression databases
ArrayExpress Q9R092; -.
CleanEx MM_HSD17B6; -.
Ontologies
GO
GO:0004303; Molecular function: estradiol 17-beta-dehydrogenase activity (inferred from electronic annotation from EC).
GO:0004745; Molecular function: retinol dehydrogenase activity (inferred from electronic annotation from EC).
GO:0050327; Molecular function: testosterone 17-beta-dehydrogenase activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR19410; ADH_short_C2; 1.
Pfam PF00106; adh_short; 1.
Pfam graphical view of domain structure.
PRINTS PR00081; GDHRDH.
PR00080; SDRFAMILY.
PROSITE PS00061; ADH_SHORT; 1.
BLOCKS Q9R092.
Genome annotation databases
Ensembl ENSMUSG00000025396; Mus musculus. [Contig view]
GeneID 27400; -.
KEGG mmu:27400; -.
Phylogenomic databases
HOGENOM Q9R092; -.
HOVERGEN Q9R092; -.
Other
SOURCE Hsd17b6; Mus musculus.
ProtoNet Q9R092.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Endoplasmic reticulum; Endosome; Glycoprotein; Lipid metabolism; Membrane; Microsome; NAD; Oxidoreductase; Signal; Steroid metabolism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    17  17     Potential. 
CHAIN   18   317  300     Hydroxysteroid 17-beta dehydrogenase 6. PRO_0000303212
NP_BIND   33    57  25     NAD (By similarity). 
ACT_SITE   176   176        Proton acceptor (By similarity). 
BINDING   164   164        Substrate (Potential). 
CARBOHYD   71    71        N-linked (GlcNAc...) (Potential). 
CARBOHYD   161   161        N-linked (GlcNAc...) (Potential). 
Sequence information
Length: 317 AA [This is the length of the unprocessed precursor] Molecular weight: 36103 Da [This is the MW of the unprocessed precursor] CRC64: 7B09D741424D3881 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MWFYLVTLVG LYHLLRWYRE RQVVSHLQDK YVFITGCDSG FGNLLARQLD RRGMRVLAAC 

        70         80         90        100        110        120 
LTEKGAEELR NKTSDRLETV ILDVTKTESI VAATQWVKER VGDRGLWGLV NNAGVLQPFA 

       130        140        150        160        170        180 
YIEWYRPEDY MPIFQVNLIG LTQVTISMLF LVKKARGRIV NVSSALGRVA LFGGFYSCSK 

       190        200        210        220        230        240 
YGVEAFSDVL RHEVQDFGVK VSIIEPGSFK TEMTDAELTI ERTKKVWEAA PEHIKESYGQ 

       250        260        270        280        290        300 
QFFDDFCSTT KRELMKCSRN LSLVTDCMEH ALTSTHPRTR YSAGWDAKFF FIPLSYLPAS 

       310 
LVDYLLAISR GKPAQAA 

Q9R092 in FASTA format

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