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UniProtKB/Swiss-Prot entry Q9EQ06


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

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Entry information
Entry name DHB11_MOUSE
Primary accession number Q9EQ06
Secondary accession numbers Q3U2P6 Q8BR33 Q8C7S0
Integrated into Swiss-Prot on August 16, 2005
Sequence was last modified on March 1, 2001 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 61)
Name and origin of the protein
Protein name Estradiol 17-beta-dehydrogenase 11 [Precursor]
Synonyms EC 1.1.1.62
17-beta-hydroxysteroid dehydrogenase 11
17-beta-HSD 11
17betaHSD11
17bHSD11
17-beta-HSD XI
17betaHSDXI
Dehydrogenase/reductase SDR family member 8
Gene name
Name: Hsd17b11
Synonyms: Dhrs8, Pan1b
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] (ISOFORM 1), AND ENZYME ACTIVITY IN VITRO.
STRAIN=NIH Swiss;
DOI=10.1016/S0303-7207(00)00417-2; PubMed=11165019 [NCBI, ExPASy, EBI, Israel, Japan]
Brereton P., Suzuki T., Sasano H., Li K., Duarte C., Obeyesekere V., Haeseleer F., Palczewski K., Smith I., Komesaroff P., Krozowski Z.;
"Pan1b (17betaHSD11)-enzymatic activity and distribution in the lung.";
Mol. Cell. Endocrinol. 171:111-117(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=BALB/c;
Chen W., Napoli J.;
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, and NOD;
TISSUE=Corpora quadrigemina, Dendritic cell, Embryonic stem cell, and Inner ear;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N;
TISSUE=Mammary gland;
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).
[5]
POSSIBLE SUBCELLULAR LOCATION.
DOI=10.1210/en.2002-221030; PubMed=12697717 [NCBI, ExPASy, EBI, Israel, Japan]
Chai Z., Brereton P., Suzuki T., Sasano H., Obeyesekere V., Escher G., Saffery R., Fuller P., Enriquez C., Krozowski Z.;
"17 beta-hydroxysteroid dehydrogenase type XI localizes to human steroidogenic cells.";
Endocrinology 144:2084-2091(2003).
Comments
  • FUNCTION: Can convert androstan-3-alpha,17-beta-diol (3-alpha-diol) to androsterone in vitro, suggesting that it may participate in androgen metabolism during steroidogenesis. May act by metabolizing compounds that stimulate steroid synthesis and/or by generating metabolites that inhibit it. Has no activity toward DHEA (dehydroepiandrosterone), or A-dione (4-androste-3,17-dione), and only a slight activity toward testosterone to A-dione.
  • CATALYTIC ACTIVITY: Estradiol-17-beta + NAD(P)+ = estrone + NAD(P)H.
  • SUBCELLULAR LOCATION: Secreted (Potential). Cytoplasm. Note=According to PubMed:12697717 it is cytoplasmic. However the relevance of such result remains unclear.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ9EQ06-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ9EQ06-2
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_015013, VSP_015014.
  • SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. 17-beta-HSD 3 subfamily.
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
AF304306; AAG41413.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY053570; AAL14859.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK049355; BAC33704.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK154803; BAE32840.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK155174; BAE33094.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK155202; BAE33115.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK155327; BAE33194.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK158327; BAE34459.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK170939; BAE42129.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC038340; AAH38340.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_444492.1; -.
UniGene Mm.46019
3D structure databases
SMR Q9EQ06; 30-273.
ModBase Q9EQ06.
PTM databases
PhosphoSite Q9EQ06; -.
Organism-specific databases
MGI MGI:2149821; Hsd17b11.
Gene expression databases
ArrayExpress Q9EQ06; -.
CleanEx MM_HSD17B11; -.
GermOnline ENSMUSG00000029311; Mus musculus.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0004303; Molecular function: estradiol 17-beta-dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006694; Biological process: steroid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
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; FALSE_NEG.
ProtoNet Q9EQ06.
Genome annotation databases
Ensembl ENSMUSG00000029311; Mus musculus. [Contig view]
GeneID 114664; -.
KEGG mmu:114664; -.
Phylogenomic databases
HOGENOM Q9EQ06; -.
HOVERGEN Q9EQ06; -.
Other
NextBio 368648; -.
SOURCE Hsd17b11; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Cytoplasm; Lipid synthesis; NADP; Oxidoreductase; Secreted; Signal; Steroid biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    21  21     Potential. 
CHAIN   22   298  277     Estradiol 17-beta-dehydrogenase 11. PRO_0000031971
NP_BIND   40    64  25     NADP (By similarity). 
ACT_SITE   185   185        Proton acceptor (By similarity). 
BINDING   172   172        Substrate (By similarity). 
VAR_SEQ   232   232        N -> K (in isoform 2). VSP_015013
VAR_SEQ   233   298        Missing (in isoform 2). VSP_015014
Sequence information
Length: 298 AA [This is the length of the unprocessed precursor] Molecular weight: 32881 Da [This is the MW of the unprocessed precursor] CRC64: 8ED9279FFBF20EA1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKYLLDLILL LPLLIVFSIE SLVKLFIPKK KKSVAGEIVL ITGAGHGIGR LTAYEFAKLN 

        70         80         90        100        110        120 
TKLVLWDINK NGIEETAAKC RKLGAQAHPF VVDCSQREEI YSAAKKVKEE VGDVSILVNN 

       130        140        150        160        170        180 
AGVVYTADLF ATQDPQIEKT FEVNVLAHFW TTKAFLPVMM KNNHGHIVTV ASAAGHTVVP 

       190        200        210        220        230        240 
FLLAYCSSKF AAVGFHRALT DELAALGRTG VRTSCLCPNF INTGFIKNPS TNLGPTLEPE 

       250        260        270        280        290 
EVVEHLMHGI LTEKQMIFVP SSIALLTVLE RIVPERFLQV LKHRINVKFD AVVGYKDK 

Q9EQ06 in FASTA format

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View entry in raw text format (no links)
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