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Reviewed, UniProtKB/Swiss-Prot Q8NBQ5 (DHB11_HUMAN)

Last modified January 19, 2010. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
    Retinal short-chain dehydrogenase/reductase 2
      Short name=retSDR2
    Cutaneous T-cell lymphoma-associated antigen HD-CL-03
    CTCL tumor antigen HD-CL-03
Gene names
Name: HSD17B11
Synonyms: DHRS8, PAN1B
ORF Names: PSEC0029, UNQ207/PRO233
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length300 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Tumor-associated antigen in cutaneous T-cell lymphoma.

Catalytic activity

Estradiol-17-beta + NAD(P)+ = estrone + NAD(P)H. Ref.8

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. Ref.8 Ref.1 Ref.6 Ref.7

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family. 17-beta-HSD 3 subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 300281Estradiol 17-beta-dehydrogenase 11
PRO_0000031970

Regions

Nucleotide binding40 – 6425NADP By similarity

Sites

Active site1851Proton acceptor By similarity
Binding site1721Substrate By similarity

Experimental info

Sequence conflict231V → E in AAH08650. Ref.5
Sequence conflict381I → T in BAC11560. Ref.4
Sequence conflict1061K → N in AAH08650. Ref.5
Sequence conflict1071V → C in AAH08650. Ref.5
Sequence conflict2281N → K in AAH08650. Ref.5
Sequence conflict2291P → M in AAH08650. Ref.5
Sequence conflict2631I → N in AAH08650. Ref.5
Sequence conflict2641A → C in AAH08650. Ref.5
Sequence conflict2651F → I in AAH08650. Ref.5

Secondary structure

..................................... 300
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8NBQ5-1 [UniParc].

Last modified August 16, 2005. Version 2.
Checksum: 51DC0EAA205EBE86

FASTA30032,964
        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 

« Hide

References

« Hide 'large scale' references
[1]"Short-chain dehydrogenases/reductases in retina."
Haeseleer F., Palczewski K.
Methods Enzymol. 316:372-383(2000) [PubMed: 10800688] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Retina.
[2]"SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma."
Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S.
Br. J. Dermatol. 150:252-258(2004) [PubMed: 14996095] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lymphoma.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
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. expand/collapse author list , 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.
Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed: 16303743] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Teratocarcinoma.
[5]"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].
Tissue: Bone marrow, Colon, Kidney, Liver and Urinary bladder.
[6]"Cloning and expression of a novel tissue specific 17beta-hydroxysteroid dehydrogenase."
Li K.X.Z., Smith R.E., Krozowski Z.S.
Endocr. Res. 24:663-667(1998) [PubMed: 9888557] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"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: TISSUE SPECIFICITY.
[8]"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: ENZYME ACTIVITY IN VITRO, TISSUE SPECIFICITY.
[9]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]"Crystal structure of human 17-beta-hydroxysteroid dehydrogenase type XI."
Lukacik P., Bunkoczi G., Kavanagh K., Ng S., Von delft F., Bray J., Edwards A., Arrowsmith C., Sundstrom M., Oppermann U.
Submitted (DEC-2004) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 28-275.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF126780 mRNA. Translation: AAF06939.1.
AF273056 mRNA. Translation: AAM44459.1.
AY358553 mRNA. Translation: AAQ88917.1.
AK075348 mRNA. Translation: BAC11560.1.
BC008650 mRNA. Translation: AAH08650.1.
BC014327 mRNA. Translation: AAH14327.1.
BC016367 mRNA. Translation: AAH16367.1.
BC021673 mRNA. Translation: AAH21673.1.
BC036001 mRNA. Translation: AAH36001.1.
IPIIPI00329598.
RefSeqNP_057329.2.
UniGeneHs.594923

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YB1X-ray1.95A/B28-275[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ8NBQ5. 3 interactions.
STRINGQ8NBQ5.

Proteomic databases

PRIDEQ8NBQ5.

Genome annotation databases

EnsemblENST00000358290; ENSP00000351035; ENSG00000198189; Homo sapiens. [Genome view]
GeneID51170.
KEGGhsa:51170.
UCSCuc003hqp.2. human.

Organism-specific databases

CTD51170.
GeneCardsGC04M088477.
H-InvDBHIX0004358.
HGNCHGNC:22960. HSD17B11.
HPAHPA021608.
PharmGKBPA134981822.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG11153.
HOGENOMHBG750976.
HOVERGENQ8NBQ5.
InParanoidQ8NBQ5.
PhylomeDBQ8NBQ5.

Enzyme and pathway databases

BRENDA1.1.1.62. 247.

Gene expression databases

ArrayExpressQ8NBQ5.
BgeeQ8NBQ5.
CleanExHS_HSD17B11.
GenevestigatorQ8NBQ5.
GermOnlineENSG00000198189. Homo sapiens.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio54111.

Entry information

Entry nameDHB11_HUMAN
AccessionPrimary (citable) accession number: Q8NBQ5
Secondary accession number(s): Q96HF6, Q9UKU4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: January 19, 2010
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents