Reviewed, UniProtKB/Swiss-Prot Q5E9H7 (DHB12_BOVIN)

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

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	312 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.

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	binding Inferred from electronic annotation. Source: InterPro 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_0000248367
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

Sequences

	Sequence		Length	Mass (Da)
	Q5E9H7-1 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 3A10BB92B7F6B1D1	FASTA	312	34,495
	10 20 30 40 50 60 METALPAAGF LYWVGASTVA YLALRISCWF FTALRVWGLG HEAGVGPWLG EWAVVTGGTD 70 80 90 100 110 120 GIGKSYAEEL AKRGMKIVLI SRSQDKLDQV SSEISEKFKV ETKTIAVDFT SEDIYDKIKA 130 140 150 160 170 180 SLAGLNIGVL VNNVGMSYEY PEYFLDVPDL DNTIKKLITV NALSVCKMTR LVLPGMVERS 190 200 210 220 230 240 KGAILNISSA SGMYPVPLLT IYSATKAFVD FFSQCLHEEY KSKGVIVQSV LPYYVATKLA 250 260 270 280 290 300 KIKRPTWDKP SPETFVKSAM KTIGVQSRTN GYPIHSLVAS VSASLPSWLY FKIAMYSGNS 310 IRVRYLKKMK MN

References

[1]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BT020943 mRNA. Translation: AAX08960.1.
IPI	IPI00691343.
RefSeq	NP_001074384.1.
UniGene	Bt.89260
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	616219.
KEGG	bta:616219.
Organism-specific databases
CTD	616219.
Phylogenomic databases
HOVERGEN	Q5E9H7.
Enzyme and pathway databases
BRENDA	1.1.1.62. 251.
Family and domain databases
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [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...

Entry information

Entry name

DHB12_BOVIN

Accession

Primary (citable) accession number: Q5E9H7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	March 15, 2005
Last modified:	October 13, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)