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Reviewed, UniProtKB/Swiss-Prot O70503 (DHB12_MOUSE)

Last modified June 16, 2009. Version 74. 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 · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Estradiol 17-beta-dehydrogenase 12
    EC=1.1.1.62
Alternative name(s):
    17-beta-hydroxysteroid dehydrogenase 12
      Short name=17-beta-HSD 12
    3-ketoacyl-CoA reductase
      Short name=KAR
    EC=1.3.1.-
    KIK-I
Gene names
Name: Hsd17b12
Synonyms: Kik1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Catalyzes the transformation of estrone (E1) into estradiol (E2), suggesting a central role in estrogen formation. Its strong expression in ovary and mammary gland suggest that it may constitute the major enzyme responsible for the conversion of E1 to E2 in females. Also has 3-ketoacyl-CoA reductase activity, reducing both long chain 3-ketoacyl-CoAs and long chain fatty acyl-CoAs, suggesting a role in long fatty acid elongation By similarity.

Catalytic activity

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

Pathway

Steroid biosynthesis; estrogen biosynthesis.

Lipid metabolism; fatty acid biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Tissue specificity

Expressed in most tissues tested. Ref.4

Domain

The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins By similarity.

Sequence similarities

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O70503-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O70503-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-135: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Estradiol 17-beta-dehydrogenase 12
PRO_0000054576

Regions

Transmembrane4 – 2421 Potential
Transmembrane182 – 20221 Potential
Transmembrane269 – 28517 Potential
Nucleotide binding50 – 7930NADP By similarity
Motif308 – 3125Di-lysine motif By similarity

Sites

Active site2021Proton acceptor By similarity
Binding site1891Substrate By similarity

Natural variations

Alternative sequence1 – 135135Missing in isoform 2.
VSP_020255

Experimental info

Sequence conflict21E → V in BAE39915. Ref.2
Sequence conflict2561V → M in BAE29906. Ref.2
Sequence conflict2561V → M in BAE31260. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 7D255188FA1F8DDB

FASTA31234,742
        10         20         30         40         50         60 
MECAPPAAGF LYWVGASTIA YLALRASYSL FRAFQVWCVG NEALVGPRLG EWAVVTGGTD 

        70         80         90        100        110        120 
GIGKAYAEEL AKRGMKIVLI SRSQDKLNQV SNNIKEKFNV ETRTIAVDFS LDDIYDKIKT 

       130        140        150        160        170        180 
GLSGLEIGVL VNNVGMSYEY PEYFLEIPDL DNTIKKLINI NVLSVCKVTR LVLPGMVERS 

       190        200        210        220        230        240 
KGVILNISSA SGMLPVPLLT IYSATKAFVD FFSQCLHEEY KSKGIFVQSV MPYLVATKLA 

       250        260        270        280        290        300 
KIQKPTLDKP SAETFVKSAI KTVGLQTRTT GYVIHSLMGS INSIMPRWMY FKIIMGFSKS 

       310 
LRNRYLKKRK KN 

« Hide

Isoform 2.

Checksum: CAC34046DDAE3A0D
Show »

FASTA17720,127

References

« Hide 'large scale' references
[1]Gambotto A., Pagliano O., Robbins P., Deleo A.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: BALB/c.
Tissue: Liver.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: BALB/c, C57BL/6J and NOD.
Tissue: Bone marrow, Cerebellum, Colon, Head, Lung and Thymus.
[3]"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] (ISOFORM 2).
Strain: FVB/N-3.
Tissue: Mammary tumor.
[4]"Identification of two mammalian reductases involved in the two-carbon fatty acyl elongation cascade."
Moon Y.-A., Horton J.D.
J. Biol. Chem. 278:7335-7343(2003) [PubMed: 12482854] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF064635 mRNA. Translation: AAC16885.1.
AK078841 mRNA. Translation: BAC37418.1.
AK081869 mRNA. Translation: BAC38354.1.
AK082715 mRNA. Translation: BAC38583.1.
AK088521 mRNA. Translation: BAC40401.1.
AK150849 mRNA. Translation: BAE29906.1.
AK152489 mRNA. Translation: BAE31260.1.
AK166027 mRNA. Translation: BAE38530.1.
AK167908 mRNA. Translation: BAE39915.1.
BC037620 mRNA. Translation: AAH37620.1.
IPIIPI00119219.
IPI00785470.
RefSeqNP_062631.1.
UniGeneMm.22505

3D structure databases

HSSPHSSP built from PDB template 2AE1 based on UniProtKB P50163.
ModBaseSearch...

PTM databases

PhosphoSiteO70503.

Proteomic databases

PRIDEO70503.

Genome annotation databases

EnsemblENSMUSG00000027195. Mus musculus. [Contig view]
GeneID56348.
KEGGmmu:56348.

Organism-specific databases

MGIMGI:1926967. Hsd17b12.

Phylogenomic databases

HOVERGENO70503.
OMAO70503. YPEYFLD.

Enzyme and pathway databases

BRENDA1.1.1.62. 244.

Gene expression databases

ArrayExpressO70503.
BgeeO70503.
CleanExMM_HSD17B12.
GermOnlineENSMUSG00000027195. Mus musculus.

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. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio312340.
SOURCESearch...

Entry information

Entry nameDHB12_MOUSE
AccessionPrimary (citable) accession number: O70503
Secondary accession number(s): Q3TID1 expand/collapse secondary AC list , Q3U7V9, Q542N3, Q8CI39
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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