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UniProtKB/Swiss-Prot entry O88736


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

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Entry information
Entry name DHB7_MOUSE
Primary accession number O88736
Secondary accession numbers Q8K5C9 Q921L1
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on November 1, 1998 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 62)
Name and origin of the protein
Protein name 3-keto-steroid reductase
Synonyms EC 1.1.1.270
Estradiol 17-beta-dehydrogenase 7
EC 1.1.1.62
17-beta-hydroxysteroid dehydrogenase 7
17-beta-HSD 7
Gene name
Name: Hsd17b7
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].
STRAIN=BALB/c;
TISSUE=Mammary gland;
DOI=10.1210/me.12.7.1048; PubMed=9658408 [NCBI, ExPASy, EBI, Israel, Japan]
Nokelainen P., Peltoketo H., Vihko R., Vihko P.;
"Expression cloning of a novel estrogenic mouse 17 beta-hydroxysteroid dehydrogenase/17-ketosteroid reductase (m17HSD7), previously described as a prolactin receptor-associated protein (PRAP) in rat.";
Mol. Endocrinol. 12:1048-1059(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Nokelainen P., Vihko P.;
"Characterization of mouse 17beta-hydroxysteroid dehydrogenase type 7 gene.";
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Liver, and Placenta;
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].
STRAIN=FVB/N;
TISSUE=Mammary tumor;
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]
NUCLEOTIDE SEQUENCE OF 1-301.
Ohnesorg T., Adamski J.;
"Characterization of mouse gene for 17-beta-hydroxysteroid dehydrogenase type 7.";
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
Comments
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
Y15733; CAA75742.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ291459; CAC88119.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ291460; CAC88119.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ291461; CAC88119.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ291463; CAC88119.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ291465; CAC88119.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ291466; CAC88119.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ291464; CAC88119.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ291462; CAC88119.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK028380; BAC25918.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK050211; BAC34124.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011464; AAH11464.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF367475; AAM21211.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_034606.3; -.
UniGene Mm.12882
3D structure databases
ModBase O88736.
Organism-specific databases
MGI MGI:1330808; Hsd17b7.
Gene expression databases
ArrayExpress O88736; -.
CleanEx MM_HSD17B7; -.
GermOnline ENSMUSG00000026675; Mus musculus.
Ontologies
GO
GO:0005783; Cellular component: endoplasmic reticulum (inferred from direct assay from MGI).
GO:0000253; Molecular function: 3-keto sterol reductase activity (inferred from direct assay from MGI).
GO:0006695; Biological process: cholesterol biosynthetic process (inferred from direct assay from MGI).
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.
PROSITE PS00061; ADH_SHORT; FALSE_NEG.
BLOCKS O88736.
Genome annotation databases
Ensembl ENSMUSG00000026675; Mus musculus. [Contig view]
GeneID 15490; -.
KEGG mmu:15490; -.
Phylogenomic databases
HOGENOM O88736; -.
HOVERGEN O88736; -.
Other
SOURCE Hsd17b7; Mus musculus.
ProtoNet O88736.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Glycoprotein; Lipid synthesis; Membrane; NAD; NADP; Oxidoreductase; Steroid biosynthesis; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   334  334     3-keto-steroid reductase. PRO_0000054587
TOPO_DOM   1   229  229     Extracellular (Potential). 
TRANSMEM   230   250  21     Potential. 
TOPO_DOM   251   334  84     Cytoplasmic (Potential). 
NP_BIND   8    15  8     NAD (Potential). 
ACT_SITE   193   193        Proton acceptor (By similarity). 
BINDING   171   171        Substrate (By similarity). 
CARBOHYD   37    37        N-linked (GlcNAc...) (Potential). 
CARBOHYD   127   127        N-linked (GlcNAc...) (Potential). 
CARBOHYD   178   178        N-linked (GlcNAc...) (Potential). 
CARBOHYD   229   229        N-linked (GlcNAc...) (Potential). 
CONFLICT   160   160        A -> V (in Ref. 2 and 4). 
Sequence information
Length: 334 AA [This is the length of the unprocessed precursor] Molecular weight: 37317 Da [This is the MW of the unprocessed precursor] CRC64: E05F0716465BC160 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRKVVLITGA SSGIGLALCG RLLAEDDDLH LCLACRNLSK ARAVRDTLLA SHPSAEVSIV 

        70         80         90        100        110        120 
QMDVSSLQSV VRGAEEVKQK FQRLDYLYLN AGILPNPQFN LKAFFCGIFS RNVIHMFTTA 

       130        140        150        160        170        180 
EGILTQNDSV TADGLQEVFE TNLFGHFILI RELEPLLCHA DNPSQLIWTS SRNAKKANFS 

       190        200        210        220        230        240 
LEDIQHSKGP EPYSSSKYAT DLLNVALNRN FNQKGLYSSV MCPGVVMTNM TYGILPPFIW 

       250        260        270        280        290        300 
TLLLPIMWLL RFFVNALTVT PYNGAEALVW LFHQKPESLN PLTKYASATS GFGTNYVTGQ 

       310        320        330 
KMDIDEDTAE KFYEVLLELE KRVRTTVQKS DHPS 

O88736 in FASTA format

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