ID DHB11_MACFA Reviewed; 300 AA. AC Q4JK73; DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 16-JUN-2009, entry version 26. DE RecName: Full=Estradiol 17-beta-dehydrogenase 11; DE EC=1.1.1.62; DE AltName: Full=17-beta-hydroxysteroid dehydrogenase 11; DE Short=17-beta-HSD 11; DE Short=17betaHSD11; DE Short=17bHSD11; DE AltName: Full=17-beta-HSD XI; DE Short=17betaHSDXI; DE AltName: Full=Dehydrogenase/reductase SDR family member 8; DE Flags: Precursor; GN Name=HSD17B11; Synonyms=DHRS8; OS Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Liu H., Labrie F., Luu-The V.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Can convert androstan-3-alpha,17-beta-diol (3-alpha- CC diol) to androsterone in vitro, suggesting that it may participate CC in androgen metabolism during steroidogenesis. May act by CC metabolizing compounds that stimulate steroid synthesis and/or by CC generating metabolites that inhibit it. Has no activity toward CC DHEA (dehydroepiandrosterone), or A-dione (4-androste-3,17-dione), CC and only a slight activity toward testosterone to A-dione (By CC similarity). CC -!- CATALYTIC ACTIVITY: Estradiol-17-beta + NAD(P)(+) = estrone + CC NAD(P)H. CC -!- SUBCELLULAR LOCATION: Secreted (Potential). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. 17-beta-HSD 3 subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DQ078724; AAY84570.1; -; mRNA. DR SMR; Q4JK73; 30-273. DR HOVERGEN; Q4JK73; -. DR BRENDA; 1.1.1.62; 3438. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR19410; ADH_short_C2; 1. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; FALSE_NEG. PE 2: Evidence at transcript level; KW Lipid synthesis; NADP; Oxidoreductase; Secreted; Signal; KW Steroid biosynthesis. FT SIGNAL 1 18 Potential. FT CHAIN 19 300 Estradiol 17-beta-dehydrogenase 11. FT /FTId=PRO_0000042582. FT NP_BIND 40 67 NADP (By similarity). FT ACT_SITE 185 185 Proton acceptor (By similarity). FT BINDING 172 172 Substrate (By similarity). FT BINDING 189 189 NADP (By similarity). SQ SEQUENCE 300 AA; 32920 MW; 25B38CCF2A8A5D8D CRC64; MKILLDLLLL LPLLIVCCLE SFVKLFIPKR RKSVAGEIVL ITGAGHGIGR LTAYEFAKLK SKLVLWDINK HGLEETAAKC KGLGAKVYTF VVDCSNREDI YSSAKKVKAE IGDVSILVNN AGVVYTSDLF ATQDAQIEKT FEVNILAHFW TTKAFLPAMM KNNHGHVVTV ASAAGHISVP FLLAYCSSKF SAVGFHKALT DELAALQITG VKTTCLCPNF VNTGFIKNPS TSLGPALEPE EVVNRLMNGI LTEQKMIFSP SSIAFLTILE RILPERFLAV LKRKINIKFD AVIGYKMKAQ //