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Reviewed, UniProtKB/Swiss-Prot Q9R092 (H17B6_MOUSE)

Last modified February 9, 2010. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Hydroxysteroid 17-beta dehydrogenase 6
    EC=1.1.1.62
    EC=1.1.1.63
    EC=1.1.1.105
Alternative name(s):
    17-beta-HSD6
    17-beta-HSD9
    Oxidative 3-alpha hydroxysteroid dehydrogenase
    3-alpha->beta-hydroxysteroid epimerase
      Short name=3-alpha->beta-HSE
Gene names
Name: Hsd17b6
Synonyms: Gm182, Hsd17b9, Rdh8
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (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). Ref.1

Catalytic activity

Estradiol-17-beta + NAD(P)+ = estrone + NAD(P)H.

Testosterone + NAD+ = androst-4-ene-3,17-dione + NADH.

Retinol + NAD+ = retinal + NADH.

Subcellular location

Microsome membrane; Peripheral membrane protein; Lumenal side. Early endosome membrane; Peripheral membrane protein; Lumenal side Potential Ref.1.

Tissue specificity

Detected in liver. Ref.1

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 317300Hydroxysteroid 17-beta dehydrogenase 6
PRO_0000303212

Regions

Nucleotide binding33 – 5725NAD By similarity

Sites

Active site1761Proton acceptor By similarity
Binding site1641Substrate Potential

Amino acid modifications

Glycosylation711N-linked (GlcNAc...) Potential
Glycosylation1611N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q9R092-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 7B09D741424D3881

FASTA31736,103
        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

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References

« Hide 'large scale' references
[1]"Complementary deoxyribonucleic acid cloning and enzymatic characterization of a novel 17beta/3alpha-hydroxysteroid/retinoid short chain dehydrogenase/reductase."
Su J., Lin M., Napoli J.L.
Endocrinology 140:5275-5284(1999) [PubMed: 10537158] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Liver.
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Small intestine.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF103797 mRNA. Translation: AAF04761.1.
AK008212 mRNA. Translation: BAB25536.1.
BC021836 mRNA. Translation: AAH21836.1.
IPIIPI00127016.
RefSeqNP_038814.1.
UniGeneMm.26719

3D structure databases

HSSPHSSP built from PDB template 1FDS based on UniProtKB P14061.
SMRQ9R092. Positions 29-287.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9R092.

Proteomic databases

PRIDEQ9R092.

Genome annotation databases

EnsemblENSMUST00000026462; ENSMUSP00000026462; ENSMUSG00000025396; Mus musculus. [Genome view]
GeneID27400.
KEGGmmu:27400.
UCSCuc007hky.1. mouse.

Organism-specific databases

CTD27400.
MGIMGI:1351670. Hsd17b6.

Phylogenomic databases

eggNOGroNOG11851.
HOGENOMHBG750976.
HOVERGENQ9R092.
InParanoidQ9R092.
OMAGYFRTGM.
OrthoDBEOG947JCM.
PhylomeDBQ9R092.

Enzyme and pathway databases

BRENDA1.1.1.105. 244.
1.1.1.62. 244.
1.1.1.63. 244.

Gene expression databases

ArrayExpressQ9R092.
BgeeQ9R092.
CleanExMM_HSD17B6.
GenevestigatorQ9R092.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio305388.
SOURCESearch...

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Entry information

Entry nameH17B6_MOUSE
AccessionPrimary (citable) accession number: Q9R092
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 1, 2000
Last modified: February 9, 2010
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents