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UniProtKB/Swiss-Prot entry Q8NBQ5


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

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Entry information
Entry name DHB11_HUMAN
Primary accession number Q8NBQ5
Secondary accession numbers Q96HF6 Q9UKU4
Integrated into Swiss-Prot on August 16, 2005
Sequence was last modified on August 16, 2005 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 55)
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
Retinal short-chain dehydrogenase/reductase 2
retSDR2
Cutaneous T-cell lymphoma-associated antigen HD-CL-03
CTCL tumor antigen HD-CL-03
Gene name
Name: HSD17B11
Synonyms: DHRS8, PAN1B
ORFNames: PSEC0029, UNQ207/PRO233
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Retina;
DOI=10.1016/S0076-6879(00)16736-9; PubMed=10800688 [NCBI, ExPASy, EBI, Israel, Japan]
Haeseleer F., Palczewski K.;
"Short-chain dehydrogenases/reductases in retina.";
Methods Enzymol. 316:372-383(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lymphoma;
DOI=10.1111/j.1365-2133.2004.05651.x; PubMed=14996095 [NCBI, ExPASy, EBI, Israel, Japan]
Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S.;
"SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma.";
Br. J. Dermatol. 150:252-258(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.1293003; PubMed=12975309 [NCBI, ExPASy, EBI, Israel, Japan]
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ota T., Nishikawa T., Suzuki Y., Kawai-Hio Y., Hayashi K., Ishii S., Saito K., Yamamoto J., Wakamatsu A., Nagai T., Nakamura Y., Nagahari K., Sugano S., Isogai T.;
"HRI human cDNA sequencing project.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow, Colon, Kidney, Liver, and Urinary bladder;
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).
[6]
TISSUE SPECIFICITY.
PubMed=9888557 [NCBI, ExPASy, EBI, Israel, Japan]
Li K.X.Z., Smith R.E., Krozowski Z.S.;
"Cloning and expression of a novel tissue specific 17beta-hydroxysteroid dehydrogenase.";
Endocr. Res. 24:663-667(1998).
[7]
TISSUE SPECIFICITY.
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).
[8]
ENZYME ACTIVITY IN VITRO, AND TISSUE SPECIFICITY.
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).
[9]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 28-275.
Lukacik P., Bunkoczi G., Kavanagh K., Ng S., Von delft F., Bray J., Edwards A., Arrowsmith C., Sundstrom M., Oppermann U.;
"Crystal structure of human 17-beta-hydroxysteroid dehydrogenase type XI.";
Submitted (DEC-2004) to the PDB data bank.
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. Tumor-associated antigen in cutaneous T-cell lymphoma.
  • CATALYTIC ACTIVITY: Estradiol-17-beta + NAD(P)+ = estrone + NAD(P)H.
  • SUBCELLULAR LOCATION: Secreted (Potential).
  • TISSUE SPECIFICITY: Present at high level in steroidogenic cells such as syncytiotrophoblasts, sebaceous gland, Leydig cells, and granulosa cells of the dominant follicle and corpus luteum. In lung, it is detected in the ciliated epithelium and in acini of adult trachea, in bronchioles, but not in alveoli. In the eye, it is detected in the nonpigmented epithelium of the ciliary body and, at lower level, in the inner nuclear layer of the retina (at protein level). Widely expressed. Highly expressed in retina, pancreas, kidney, liver, lung, adrenal, small intestine, ovary and heart.
  • 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
AF126780; AAF06939.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF273056; AAM44459.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY358553; AAQ88917.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK075348; BAC11560.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008650; AAH08650.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC014327; AAH14327.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC016367; AAH16367.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021673; AAH21673.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC036001; AAH36001.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_057329.2; -.
UniGene Hs.284414
3D structure databases
PDB
1YB1; X-ray; 1.95 A; A/B=28-275.[ExPASy / RCSB / EBI]
PDBsum 1YB1; -.
ModBase Q8NBQ5.
Organism-specific databases
H-InvDB HIX0004358; -.
HGNC HGNC:22960; HSD17B11.
GenAtlas HSD17B11.
PharmGKB PA134981822; -.
GeneCards Q8NBQ5.
Gene expression databases
ArrayExpress Q8NBQ5; -.
CleanEx HS_HSD17B11; -.
GermOnline ENSG00000198189; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from HGNC).
GO:0016229; Molecular function: steroid dehydrogenase activity (inferred from direct assay from HGNC).
GO:0006710; Biological process: androgen catabolic process (inferred from direct assay from HGNC).
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.
BLOCKS Q8NBQ5.
Genome annotation databases
Ensembl ENSG00000198189; Homo sapiens. [Contig view]
GeneID 51170; -.
KEGG hsa:51170; -.
Phylogenomic databases
HOGENOM Q8NBQ5; -.
HOVERGEN Q8NBQ5; -.
Other
ProtoNet Q8NBQ5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Lipid synthesis; NADP; Oxidoreductase; Secreted; Signal; Steroid biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    19  19     Potential. 
CHAIN   20   300  281     Estradiol 17-beta-dehydrogenase 11. PRO_0000031970
NP_BIND   40    64  25     NADP (By similarity). 
ACT_SITE   185   185        Proton acceptor (By similarity). 
BINDING   172   172        Substrate (By similarity). 
CONFLICT   23    23        V -> E (in Ref. 5; AAH08650). 
CONFLICT   38    38        I -> T (in Ref. 4; BAC11560). 
CONFLICT   106   106        K -> N (in Ref. 5; AAH08650). 
CONFLICT   107   107        V -> C (in Ref. 5; AAH08650). 
CONFLICT   228   228        N -> K (in Ref. 5; AAH08650). 
CONFLICT   229   229        P -> M (in Ref. 5; AAH08650). 
CONFLICT   263   263        I -> N (in Ref. 5; AAH08650). 
CONFLICT   264   264        A -> C (in Ref. 5; AAH08650). 
CONFLICT   265   265        F -> I (in Ref. 5; AAH08650). 
STRAND   38    42  5      
TURN   43    45  3      
HELIX   47    58  12      
STRAND   62    68  7      
HELIX   70    82  13      
STRAND   87    91  5      
HELIX   97   110  14      
STRAND   115   119  5      
HELIX   130   132  3      
HELIX   133   144  12      
HELIX   146   161  16      
STRAND   165   170  6      
HELIX   179   205  27      
STRAND   211   218  8      
HELIX   220   223  4      
HELIX   230   233  4      
HELIX   239   251  13      
STRAND   255   259  5      
HELIX   265   270  6      
Sequence information
Length: 300 AA [This is the length of the unprocessed precursor] Molecular weight: 32964 Da [This is the MW of the unprocessed precursor] CRC64: 51DC0EAA205EBE86 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKFLLDILLL LPLLIVCSLE SFVKLFIPKR RKSVTGEIVL ITGAGHGIGR LTAYEFAKLK 

        70         80         90        100        110        120 
SKLVLWDINK HGLEETAAKC KGLGAKVHTF VVDCSNREDI YSSAKKVKAE IGDVSILVNN 

       130        140        150        160        170        180 
AGVVYTSDLF ATQDPQIEKT FEVNVLAHFW TTKAFLPAMT KNNHGHIVTV ASAAGHVSVP 

       190        200        210        220        230        240 
FLLAYCSSKF AAVGFHKTLT DELAALQITG VKTTCLCPNF VNTGFIKNPS TSLGPTLEPE 

       250        260        270        280        290        300 
EVVNRLMHGI LTEQKMIFIP SSIAFLTTLE RILPERFLAV LKRKISVKFD AVIGYKMKAQ 

Q8NBQ5 in FASTA format

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