Q5TJF5 (DHB8_CANFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Estradiol 17-beta-dehydrogenase 8
EC=1.1.1.62

Alternative name(s):
17-beta-hydroxysteroid dehydrogenase 8
Short name=17-beta-HSD 8
3-oxoacyl-[acyl-carrier-protein] reductase
EC=1.1.1.-
Testosterone 17-beta-dehydrogenase 8
EC=1.1.1.239

Gene names

Name:

HSD17B8

Organism

Canis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis › Canis lupus

Protein attributes

Sequence length	259 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	NAD-dependent 17-beta-hydroxysteroid dehydrogenase with highest activity towards estradiol. Has very low activity towards testosterone By similarity. The heteroteramer with CBR4 has NADH-dependent 3-ketoacyl-acyl carrier protein reductase activity. May play a role in biosynthesis of fatty acids in mitochondria By similarity.
Catalytic activity	17-beta-estradiol + NAD(P)+ = estrone + NAD(P)H. Testosterone + NAD+ = androstenedione + NADH.
Pathway	Steroid biosynthesis; estrogen biosynthesis. Lipid metabolism; fatty acid biosynthesis.
Subunit structure	Heterotetramer with CBR4; contains two molecules of HSD17B8 and CBR4 By similarity.
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism Steroid biosynthesis
Cellular component	Mitochondrion
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	estrogen biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	estradiol 17-beta-dehydrogenase activity Inferred from sequence or structural similarity. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro testosterone dehydrogenase (NAD+) 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 – 259	259	Estradiol 17-beta-dehydrogenase 8		PRO_0000054597
Regions
	Nucleotide binding	13 – 21	9	NAD By similarity
	Nucleotide binding	40 – 41	2	NAD By similarity
	Nucleotide binding	72 – 74	3	NAD By similarity
	Nucleotide binding	167 – 171	5	NAD By similarity
	Nucleotide binding	200 – 202	3	NAD By similarity
Sites
	Active site	167	1	Proton acceptor By similarity
	Binding site	154	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5TJF5 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 40AA25885DE5E197	FASTA	259	26,712
	10 20 30 40 50 60 MASPLRLRSA LALVTGAGSG IGRAVSVRLA KEGATVAACD LDRAAACETV WLLGGQGSEK 70 80 90 100 110 120 VAPGGAHTAF QADVSEAGAV RRLLEQVQAC FSRPPSVVVS CAGLTRDEFL LRMSEDDWDR 130 140 150 160 170 180 VIAVNLKGIF LVTQAAAQAL VSSGCRGSII NISSIVGKVG NVGQTNYAAS KAGVIGLTQT 190 200 210 220 230 240 AARELGRHGI RCNSVLPGFI TTPMTQKVPQ KVLDKVIGMI PMGHLGDPED VADAVTFLAS 250 EDSGYITGAS VEVTGGLYM

References

[1]

"Genomic sequence of the class II region of the canine MHC: comparison with the MHC of other mammalian species." Debenham S.L., Hart E.A., Ashurst J.L., Howe K.L., Quail M.A., Ollier W.E.R., Binns M.M. Genomics 85:48-59(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Doberman pinscher.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ630366 Genomic DNA. Translation: CAI11433.1.
3D structure databases
ProteinModelPortal	Q5TJF5.
SMR	Q5TJF5. Positions 6-258.
ModBase	Search...
Protein-protein interaction databases
STRING	9615.ENSCAFP00000001317.
Proteomic databases
PaxDb	Q5TJF5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG1028.
HOVERGEN	HBG002145.
InParanoid	Q5TJF5.
OrthoDB	EOG4NZTTZ.
Enzyme and pathway databases
UniPathway	UPA00094. UPA00769.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. IPR020904. Sc_DH/Rdtase_CS. [Graphical view]
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

DHB8_CANFA

Accession

Primary (citable) accession number: Q5TJF5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 21, 2004
Last modified:	April 3, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program