Reviewed, UniProtKB/Swiss-Prot Q6P7R8 (DHB12_RAT)

Names and origin

Protein names

Recommended 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.-

Gene names

Name:

Hsd17b12

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	312 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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.
Sequence caution	The sequence AAD00504.1 differs from that shown. Reason: Frameshift at position 272.

Ontologies

Keywords
Biological process	Lipid synthesis Steroid biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW steroid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	estradiol 17-beta-dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 312	312	Estradiol 17-beta-dehydrogenase 12		PRO_0000248370
Regions
	Transmembrane	4 – 24	21	Potential
	Transmembrane	182 – 202	21	Potential
	Transmembrane	271 – 291	21	Potential
	Nucleotide binding	50 – 79	30	NADP By similarity
	Motif	308 – 312	5	Di-lysine motif By similarity
Sites
	Active site	202	1	Proton acceptor By similarity
	Binding site	189	1	Substrate By similarity
Experimental info
	Sequence conflict	236	1	A → S in AAD00504. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q6P7R8-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 8531943458EFC711	FASTA	312	34,841
	10 20 30 40 50 60 MERALPAAGF LYWVGASTIA YLTLRASYSL FRAFQVWCVG NQAFVGPRLG EWAVVTGGTD 70 80 90 100 110 120 GIGKSYAEEL AKRGMKIVLI SRSQDKLKEV SNNIKEKFNV ETRTIAVDFS LDDIYDKIKT 130 140 150 160 170 180 GLSGLEIGVL VNNVGMSYEY PEYFLEIPDL DNTIKKLINI NVLSICKVTR LVLPGMVERS 190 200 210 220 230 240 KGVILNISSA SGMLPVPLLT VYSATKAFVD FFSQCLHEEY KSKGIFVQSV LPFFVATKLA 250 260 270 280 290 300 KIRKPTLDKP SAETFVKSAI KTVGLQTRTT GYVIHAIMGS INSILPRWIY FKTIMGFNKS 310 LRNRYLKKTK KN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Trzyna W.C., Gabbeta V., McHugh K.M. Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: Pituitary anterior lobe.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U81186 mRNA. Translation: AAD00504.1. Frameshift. BC061543 mRNA. Translation: AAH61543.1.
IPI	IPI00208645.
RefSeq	NP_114455.1.
UniGene	Rn.203283
3D structure databases
HSSP	HSSP built from PDB template 1YB1 based on UniProtKB Q8NBQ5.
SMR	Q6P7R8. Positions 50-283.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6P7R8.
PTM databases
PhosphoSite	Q6P7R8.
Proteomic databases
PRIDE	Q6P7R8.
Genome annotation databases
Ensembl	ENSRNOT00000012806; ENSRNOP00000012806; ENSRNOG00000009630; Rattus norvegicus. [Genome view]
GeneID	84013.
KEGG	rno:84013.
NMPDR	fig|10116.3.peg.19242.
UCSC	BC061543. rat.
Organism-specific databases
CTD	84013.
RGD	708367. Hsd17b12.
Phylogenomic databases
eggNOG	roNOG06538.
HOVERGEN	Q6P7R8.
InParanoid	Q6P7R8.
OMA	YPEYFLD.
OrthoDB	EOG9909VJ.
PhylomeDB	Q6P7R8.
Enzyme and pathway databases
BRENDA	1.1.1.62. 248.
Gene expression databases
ArrayExpress	Q6P7R8.
Genevestigator	Q6P7R8.
GermOnline	ENSRNOG00000009630. Rattus norvegicus.
Family and domain databases
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. IPR020904. Sc_DH/Rdtase_CS. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR19410. ADH_short_C2. 1 hit.
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
PROSITE	PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	616547.

Entry information

Entry name

DHB12_RAT

Accession

Primary (citable) accession number: Q6P7R8
Secondary accession number(s): Q9Z1B9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	July 5, 2004
Last modified:	January 19, 2010
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)