ID   DHB12_MOUSE             Reviewed;         312 AA.
AC   O70503; Q3TID1; Q3U7V9; Q542N3; Q8CI39;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 74.
DE   RecName: Full=Estradiol 17-beta-dehydrogenase 12;
DE            EC=1.1.1.62;
DE   AltName: Full=17-beta-hydroxysteroid dehydrogenase 12;
DE            Short=17-beta-HSD 12;
DE   AltName: Full=3-ketoacyl-CoA reductase;
DE            Short=KAR;
DE            EC=1.3.1.-;
DE   AltName: Full=KIK-I;
GN   Name=Hsd17b12; Synonyms=Kik1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Liver;
RA   Gambotto A., Pagliano O., Robbins P., Deleo A.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c, C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Cerebellum, Colon, Head, Lung, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=12482854; DOI=10.1074/jbc.M211684200;
RA   Moon Y.-A., Horton J.D.;
RT   "Identification of two mammalian reductases involved in the two-carbon
RT   fatty acyl elongation cascade.";
RL   J. Biol. Chem. 278:7335-7343(2003).
CC   -!- FUNCTION: Catalyzes the transformation of estrone (E1) into
CC       estradiol (E2), suggesting a central role in estrogen formation.
CC       Its strong expression in ovary and mammary gland suggest that it
CC       may constitute the major enzyme responsible for the conversion of
CC       E1 to E2 in females. Also has 3-ketoacyl-CoA reductase activity,
CC       reducing both long chain 3-ketoacyl-CoAs and long chain fatty
CC       acyl-CoAs, suggesting a role in long fatty acid elongation (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Estradiol-17-beta + NAD(P)(+) = estrone +
CC       NAD(P)H.
CC   -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O70503-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O70503-2; Sequence=VSP_020255;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in most tissues tested.
CC   -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum
CC       localization for type I membrane proteins (By similarity).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family. 17-beta-HSD 3 subfamily.
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DR   EMBL; AF064635; AAC16885.1; -; mRNA.
DR   EMBL; AK078841; BAC37418.1; -; mRNA.
DR   EMBL; AK081869; BAC38354.1; -; mRNA.
DR   EMBL; AK082715; BAC38583.1; -; mRNA.
DR   EMBL; AK088521; BAC40401.1; -; mRNA.
DR   EMBL; AK150849; BAE29906.1; -; mRNA.
DR   EMBL; AK152489; BAE31260.1; -; mRNA.
DR   EMBL; AK166027; BAE38530.1; -; mRNA.
DR   EMBL; AK167908; BAE39915.1; -; mRNA.
DR   EMBL; BC037620; AAH37620.1; -; mRNA.
DR   IPI; IPI00119219; -.
DR   IPI; IPI00785470; -.
DR   RefSeq; NP_062631.1; -.
DR   UniGene; Mm.22505; -.
DR   HSSP; P50163; 2AE1.
DR   PhosphoSite; O70503; -.
DR   PRIDE; O70503; -.
DR   Ensembl; ENSMUSG00000027195; Mus musculus.
DR   GeneID; 56348; -.
DR   KEGG; mmu:56348; -.
DR   MGI; MGI:1926967; Hsd17b12.
DR   HOVERGEN; O70503; -.
DR   OMA; O70503; YPEYFLD.
DR   BRENDA; 1.1.1.62; 244.
DR   NextBio; 312340; -.
DR   ArrayExpress; O70503; -.
DR   Bgee; O70503; -.
DR   CleanEx; MM_HSD17B12; -.
DR   GermOnline; ENSMUSG00000027195; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005518; F:collagen binding; IDA:MGI.
DR   GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IEA:EC.
DR   GO; GO:0001968; F:fibronectin binding; IDA:MGI.
DR   GO; GO:0008201; F:heparin binding; IDA:MGI.
DR   GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
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; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Endoplasmic reticulum; Lipid synthesis;
KW   Membrane; NADP; Oxidoreductase; Steroid biosynthesis; Transmembrane.
FT   CHAIN         1    312       Estradiol 17-beta-dehydrogenase 12.
FT                                /FTId=PRO_0000054576.
FT   TRANSMEM      4     24       Potential.
FT   TRANSMEM    182    202       Potential.
FT   TRANSMEM    269    285       Potential.
FT   NP_BIND      50     79       NADP (By similarity).
FT   MOTIF       308    312       Di-lysine motif (By similarity).
FT   ACT_SITE    202    202       Proton acceptor (By similarity).
FT   BINDING     189    189       Substrate (By similarity).
FT   VAR_SEQ       1    135       Missing (in isoform 2).
FT                                /FTId=VSP_020255.
FT   CONFLICT      2      2       E -> V (in Ref. 2; BAE39915).
FT   CONFLICT    256    256       V -> M (in Ref. 2; BAE29906/BAE31260).
SQ   SEQUENCE   312 AA;  34742 MW;  7D255188FA1F8DDB CRC64;
     MECAPPAAGF LYWVGASTIA YLALRASYSL FRAFQVWCVG NEALVGPRLG EWAVVTGGTD
     GIGKAYAEEL AKRGMKIVLI SRSQDKLNQV SNNIKEKFNV ETRTIAVDFS LDDIYDKIKT
     GLSGLEIGVL VNNVGMSYEY PEYFLEIPDL DNTIKKLINI NVLSVCKVTR LVLPGMVERS
     KGVILNISSA SGMLPVPLLT IYSATKAFVD FFSQCLHEEY KSKGIFVQSV MPYLVATKLA
     KIQKPTLDKP SAETFVKSAI KTVGLQTRTT GYVIHSLMGS INSIMPRWMY FKIIMGFSKS
     LRNRYLKKRK KN
//