Reviewed, UniProtKB/Swiss-Prot Q9EQ06 (DHB11_MOUSE)

Names and origin

Protein names

Recommended name:
    Estradiol 17-beta-dehydrogenase 11
    EC=1.1.1.62
Alternative name(s):
    17-beta-hydroxysteroid dehydrogenase 11
      Short name=17-beta-HSD 11
      Short name=17betaHSD11
      Short name=17bHSD11
    17-beta-HSD XI
      Short name=17betaHSDXI
    Dehydrogenase/reductase SDR family member 8

Gene names

Name:	Hsd17b11
Synonyms:	Dhrs8, Pan1b

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	298 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (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. Ref.1
Subcellular location	Secreted Potential. Cytoplasm. Note: According to Ref.5 it is cytoplasmic. However the relevance of such result remains unclear.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family. 17-beta-HSD 3 subfamily.

Ontologies

Keywords
Biological process	Lipid synthesis Steroid biosynthesis
Cellular component	Cytoplasm Secreted
Coding sequence diversity	Alternative splicing
Domain	Signal
Ligand	NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW steroid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	binding Inferred from electronic annotation. Source: InterPro estradiol 17-beta-dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9EQ06-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9EQ06-2)

The sequence of this isoform differs from the canonical sequence as follows:
     232-232: N → K
     233-298: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 298	277	Estradiol 17-beta-dehydrogenase 11		PRO_0000031971
Regions
	Nucleotide binding	40 – 64	25	NADP By similarity
Sites
	Active site	185	1	Proton acceptor By similarity
	Binding site	172	1	Substrate By similarity
Natural variations
	Alternative sequence	232	1	N → K in isoform 2.		VSP_015013
	Alternative sequence	233 – 298	66	Missing in isoform 2.		VSP_015014

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 8ED9279FFBF20EA1	FASTA	298	32,881
	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
	Isoform 2. Checksum: 459D085EEB194051	FASTA	232	25,347
	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 FLLAYCSSKF AAVGFHRALT DELAALGRTG VRTSCLCPNF INTGFIKNPS TK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Pan1b (17betaHSD11)-enzymatic activity and distribution in the lung." Brereton P., Suzuki T., Sasano H., Li K., Duarte C., Obeyesekere V., Haeseleer F., Palczewski K., Smith I., Komesaroff P., Krozowski Z. Mol. Cell. Endocrinol. 171:111-117(2001) [PubMed: 11165019] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY IN VITRO. Strain: NIH Swiss.
[2]	Chen W., Napoli J. Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: BALB/c.
[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. , 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] (ISOFORMS 1 AND 2). Strain: C57BL/6J and NOD. Tissue: Corpora quadrigemina, Dendritic cell, Embryonic stem cell and Inner ear.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: FVB/N. Tissue: Mammary gland.
[5]	"17 beta-hydroxysteroid dehydrogenase type XI localizes to human steroidogenic cells." Chai Z., Brereton P., Suzuki T., Sasano H., Obeyesekere V., Escher G., Saffery R., Fuller P., Enriquez C., Krozowski Z. Endocrinology 144:2084-2091(2003) [PubMed: 12697717] [Abstract] Cited for: POSSIBLE SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF304306 mRNA. Translation: AAG41413.1. AY053570 mRNA. Translation: AAL14859.1. AK049355 mRNA. Translation: BAC33704.1. AK154803 mRNA. Translation: BAE32840.1. AK155174 mRNA. Translation: BAE33094.1. AK155202 mRNA. Translation: BAE33115.1. AK155327 mRNA. Translation: BAE33194.1. AK158327 mRNA. Translation: BAE34459.1. AK170939 mRNA. Translation: BAE42129.1. BC038340 mRNA. Translation: AAH38340.1.
IPI	IPI00110224. IPI00648201.
RefSeq	NP_444492.1.
UniGene	Mm.46019
3D structure databases
SMR	Q9EQ06. Positions 30-273.
ModBase	Search...
Proteomic databases
PRIDE	Q9EQ06.
Genome annotation databases
Ensembl	ENSMUSG00000029311. Mus musculus. [Contig view]
GeneID	114664.
KEGG	mmu:114664.
Organism-specific databases
MGI	MGI:2149821. Hsd17b11.
Phylogenomic databases
HOGENOM	Q9EQ06.
HOVERGEN	Q9EQ06.
OMA	Q9EQ06. SCLCPNF.
Enzyme and pathway databases
BRENDA	1.1.1.62. 244.
Gene expression databases
ArrayExpress	Q9EQ06.
Bgee	Q9EQ06.
CleanEx	MM_HSD17B11.
GermOnline	ENSMUSG00000029311. Mus musculus.
Family and domain databases
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR19410. ADH_short_C2. 1 hit.
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
PROSITE	PS00061. ADH_SHORT. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	368648.
SOURCE	Search...

Entry information

Entry name

DHB11_MOUSE

Accession

Primary (citable) accession number: Q9EQ06
Secondary accession number(s): Q3U2P6, Q8BR33, Q8C7S0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	March 1, 2001
Last modified:	June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)