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O88736 (DHB7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-keto-steroid reductase

EC=1.1.1.270
Alternative name(s):
17-beta-hydroxysteroid dehydrogenase 7
Short name=17-beta-HSD 7
Estradiol 17-beta-dehydrogenase 7
EC=1.1.1.62
Gene names
Name:Hsd17b7
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Responsible for the reduction of the keto group on the C-3 of sterols.

Catalytic activity

A 3-beta-hydroxysteroid + NADP+ = a 3-oxosteroid + NADPH.

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

Pathway

Steroid biosynthesis; estrogen biosynthesis.

Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 5/6.

Subcellular location

Cell membrane; Single-pass membrane protein.

Tissue specificity

Most abundant in ovaries of pregnant animals. Present also in nonpregnant animals in ovaries, mammary gland, liver, kidney and testis.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family. ERG27 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3343343-keto-steroid reductase
PRO_0000054587

Regions

Topological domain1 – 229229Extracellular Potential
Transmembrane230 – 25021Helical; Potential
Topological domain251 – 33484Cytoplasmic Potential
Nucleotide binding8 – 158NAD Potential

Sites

Active site1931Proton acceptor By similarity
Binding site1711Substrate By similarity

Amino acid modifications

Glycosylation371N-linked (GlcNAc...) Potential
Glycosylation1271N-linked (GlcNAc...) Potential
Glycosylation1781N-linked (GlcNAc...) Potential
Glycosylation2291N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1601A → V in CAC88119. Ref.2
Sequence conflict1601A → V in BC011464. Ref.4

Sequences

Sequence LengthMass (Da)Tools
O88736 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: E05F0716465BC160

FASTA33437,317
        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 

« Hide

References

« Hide 'large scale' references
[1]"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."
Nokelainen P., Peltoketo H., Vihko R., Vihko P.
Mol. Endocrinol. 12:1048-1059(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Mammary gland.
[2]"Characterization of mouse 17beta-hydroxysteroid dehydrogenase type 7 gene."
Nokelainen P., Vihko P.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver and Placenta.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
[5]"Characterization of mouse gene for 17-beta-hydroxysteroid dehydrogenase type 7."
Ohnesorg T., Adamski J.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE OF 1-301.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y15733 mRNA. Translation: CAA75742.1.
AJ291459 expand/collapse EMBL AC list , AJ291460, AJ291461, AJ291463, AJ291465, AJ291466, AJ291464, AJ291462 Genomic DNA. Translation: CAC88119.1.
AK028380 mRNA. Translation: BAC25918.1.
AK050211 mRNA. Translation: BAC34124.1.
BC011464 mRNA. No translation available.
AF367475 Genomic DNA. Translation: AAM21211.1.
RefSeqNP_034606.3. NM_010476.3.
UniGeneMm.12882.

3D structure databases

ProteinModelPortalO88736.
SMRO88736. Positions 2-321.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200436. 1 interaction.
IntActO88736. 1 interaction.
MINTMINT-1862744.

PTM databases

PhosphoSiteO88736.

Proteomic databases

PaxDbO88736.
PRIDEO88736.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027989; ENSMUSP00000027989; ENSMUSG00000026675.
GeneID15490.
KEGGmmu:15490.
UCSCuc007dlp.1. mouse.

Organism-specific databases

CTD51478.
MGIMGI:1330808. Hsd17b7.

Phylogenomic databases

eggNOGCOG1028.
GeneTreeENSGT00390000013340.
HOGENOMHOG000253921.
HOVERGENHBG058236.
KOK13373.
OMACHSDNPS.
OrthoDBEOG7S4X6D.
TreeFamTF105433.

Enzyme and pathway databases

UniPathwayUPA00769.
UPA00770; UER00758.

Gene expression databases

ArrayExpressO88736.
BgeeO88736.
CleanExMM_HSD17B7.
GenevestigatorO88736.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
ProtoNetSearch...

Other

NextBio288362.
PROO88736.
SOURCESearch...

Entry information

Entry nameDHB7_MOUSE
AccessionPrimary (citable) accession number: O88736
Secondary accession number(s): Q8K5C9, Q921L1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: March 19, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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