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UniProtKB/Swiss-Prot entry Q53GQ0


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

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Entry information
Entry name DHB12_HUMAN
Primary accession number Q53GQ0
Secondary accession numbers Q96JU2 Q9Y6G8
Integrated into Swiss-Prot on September 5, 2006
Sequence was last modified on October 2, 2007 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 33)
Name and origin of the protein
Protein name Estradiol 17-beta-dehydrogenase 12
Synonyms EC 1.1.1.62
17-beta-hydroxysteroid dehydrogenase 12
17-beta-HSD 12
3-ketoacyl-CoA reductase
KAR
EC 1.3.1.-
Gene name
Name: HSD17B12
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].
Liu T., Zhang J., Fu G., Zhang Q., Ye M., Zhou J., Wu J., Shen Y., Yu M., Chen S., Mao M., Chen Z.;
"Human steroid dehydrogenase homologue, complete cds.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-280.
TISSUE=Thyroid;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-280.
TISSUE=Liver;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
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).
[5]
PROTEIN SEQUENCE OF 26-35; 65-72; 104-117; 157-179 AND 207-221, AND MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (JUN-2005) to UniProtKB.
[6]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1074/jbc.M211684200; PubMed=12482854 [NCBI, ExPASy, EBI, Israel, Japan]
Moon Y.-A., Horton J.D.;
"Identification of two mammalian reductases involved in the two-carbon fatty acyl elongation cascade.";
J. Biol. Chem. 278:7335-7343(2003).
[7]
TISSUE SPECIFICITY.
DOI=10.1267/THRO05020412; PubMed=16113833 [NCBI, ExPASy, EBI, Israel, Japan]
Gnatenko D.V., Cupit L.D., Huang E.C., Dhundale A., Perrotta P.L., Bahou W.F.;
"Platelets express steroidogenic 17beta-hydroxysteroid dehydrogenases. Distinct profiles predict the essential thrombocythemic phenotype.";
Thromb. Haemost. 94:412-421(2005).
[8]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND MUTAGENESIS OF VAL-196 AND PHE-234.
DOI=10.1210/me.2005-0058; PubMed=16166196 [NCBI, ExPASy, EBI, Israel, Japan]
Luu-The V., Tremblay P., Labrie F.;
"Characterization of type 12 17beta-hydroxysteroid dehydrogenase, an isoform of type 3 17beta-hydroxysteroid dehydrogenase responsible for estradiol formation in women.";
Mol. Endocrinol. 20:437-443(2006).
Comments
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
AF078850; AAD44482.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK027882; BAB55429.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK222881; BAD96601.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012043; AAH12043.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_057226.1; -.
UniGene Hs.132513
3D structure databases
ModBase Q53GQ0.
PTM databases
PhosphoSite Q53GQ0; -.
Organism-specific databases
HGNC HGNC:18646; HSD17B12.
GenAtlas HSD17B12.
HPA HPA016427; -.
MIM 609574; gene. [NCBI / EBI]
PharmGKB PA38618; -.
GeneCards Q53GQ0.
Gene expression databases
ArrayExpress Q53GQ0; -.
CleanEx HS_HSD17B12; -.
GermOnline ENSG00000149084; Homo sapiens.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
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; 1.
BLOCKS Q53GQ0.
Genome annotation databases
Ensembl ENSG00000149084; Homo sapiens. [Contig view]
GeneID 51144; -.
KEGG hsa:51144; -.
NMPDR fig|9606.3.peg.5483; -.
Phylogenomic databases
HOGENOM Q53GQ0; -.
HOVERGEN Q53GQ0; -.
Other
SOURCE HSD17B12; Homo sapiens.
ProtoNet Q53GQ0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Direct protein sequencing; Endoplasmic reticulum; Lipid synthesis; Membrane; NADP; Oxidoreductase; Polymorphism; Steroid biosynthesis; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   312  312     Estradiol 17-beta-dehydrogenase 12. PRO_0000248368
TRANSMEM   4    24  21     Potential. 
TRANSMEM   182   202  21     Potential. 
TRANSMEM   271   291  21     Potential. 
NP_BIND   50    79  30     NADP (By similarity). 
MOTIF   308   312  5     Di-lysine motif. 
ACT_SITE   202   202        Proton acceptor (By similarity). 
BINDING   189   189        Substrate (By similarity). 
VARIANT   280   280  1     S -> L (in dbSNP:rs11555762 [NCBI]). VAR_027277 
MUTAGEN   196   196        V->W: No effect. 
MUTAGEN   234   234        F->A: Allows the conversion of androstenedione to testosterone. 
Sequence information
Length: 312 AA [This is the length of the unprocessed precursor] Molecular weight: 34324 Da [This is the MW of the unprocessed precursor] CRC64: 8518336D7F514E50 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MESALPAAGF LYWVGAGTVA YLALRISYSL FTALRVWGVG NEAGVGPGLG EWAVVTGSTD 

        70         80         90        100        110        120 
GIGKSYAEEL AKHGMKVVLI SRSKDKLDQV SSEIKEKFKV ETRTIAVDFA SEDIYDKIKT 

       130        140        150        160        170        180 
GLAGLEIGIL VNNVGMSYEY PEYFLDVPDL DNVIKKMINI NILSVCKMTQ LVLPGMVERS 

       190        200        210        220        230        240 
KGAILNISSG SGMLPVPLLT IYSATKTFVD FFSQCLHEEY RSKGVFVQSV LPYFVATKLA 

       250        260        270        280        290        300 
KIRKPTLDKP SPETFVKSAI KTVGLQSRTN GYLIHALMGS IISNLPSWIY LKIVMNMNKS 

       310 
TRAHYLKKTK KN 

Q53GQ0 in FASTA format

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