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Protein

Testosterone 17-beta-dehydrogenase 3

Gene

Hsd17b3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Favors the reduction of androstenedione to testosterone. Uses NADPH while the two other EDH17B enzymes use NADH.By similarity

Catalytic activityi

Testosterone + NADP+ = androst-4-ene-3,17-dione + NADPH.

Pathwayi: testosterone biosynthesis

This protein is involved in the pathway testosterone biosynthesis, which is part of Hormone biosynthesis.
View all proteins of this organism that are known to be involved in the pathway testosterone biosynthesis and in Hormone biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei181 – 1811SubstrateBy similarity
Active sitei194 – 1941Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi44 – 7330NADPBy similarityAdd
BLAST

GO - Molecular functioni

  • estradiol 17-beta-dehydrogenase activity Source: RGD
  • testosterone 17-beta-dehydrogenase (NADP+) activity Source: UniProtKB
  • testosterone dehydrogenase (NAD+) activity Source: RGD

GO - Biological processi

  • biphenyl metabolic process Source: RGD
  • cellular response to antibiotic Source: RGD
  • cellular response to gonadotropin stimulus Source: RGD
  • cellular response to hormone stimulus Source: RGD
  • hippocampus development Source: RGD
  • insecticide metabolic process Source: RGD
  • Leydig cell differentiation Source: RGD
  • organic acid metabolic process Source: RGD
  • phenol-containing compound metabolic process Source: RGD
  • response to activity Source: RGD
  • response to arsenic-containing substance Source: RGD
  • response to cadmium ion Source: RGD
  • response to corticosterone Source: RGD
  • response to estrogen Source: RGD
  • response to ethanol Source: RGD
  • response to fatty acid Source: RGD
  • response to fungicide Source: RGD
  • response to herbicide Source: RGD
  • response to insecticide Source: RGD
  • response to L-ascorbic acid Source: RGD
  • response to lead ion Source: RGD
  • response to metal ion Source: RGD
  • response to nutrient levels Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to steroid hormone Source: RGD
  • response to vitamin E Source: RGD
  • steroid biosynthetic process Source: RGD
  • testosterone biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.1.1.64. 5301.
UniPathwayiUPA00367.

Names & Taxonomyi

Protein namesi
Recommended name:
Testosterone 17-beta-dehydrogenase 3 (EC:1.1.1.64)
Alternative name(s):
17-beta-hydroxysteroid dehydrogenase type 3
Short name:
17-beta-HSD 3
Testicular 17-beta-hydroxysteroid dehydrogenase
Gene namesi
Name:Hsd17b3
Synonyms:Edh17b3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621805. Hsd17b3.

Subcellular locationi

  • Endoplasmic reticulum By similarity

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • intracellular membrane-bounded organelle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1075158.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 306306Testosterone 17-beta-dehydrogenase 3PRO_0000054575Add
BLAST

Proteomic databases

PaxDbiO54939.
PRIDEiO54939.

PTM databases

iPTMnetiO54939.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025850.

Chemistry

BindingDBiO54939.

Structurei

3D structure databases

ProteinModelPortaliO54939.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1014. Eukaryota.
COG0300. LUCA.
HOGENOMiHOG000039237.
HOVERGENiHBG005478.
InParanoidiO54939.
KOiK10207.
PhylomeDBiO54939.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR033281. HSD17B3.
IPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PTHR24322:SF621. PTHR24322:SF621. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PIRSFiPIRSF000126. 11-beta-HSD1. 1 hit.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

O54939-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQFLLSVGL LVCLVCLVKC VRFSRYLFLS FCKALPGSFL RSMGQWAVIT
60 70 80 90 100
GAGDGIGKAY SFELARHGLN VVLISRTLEK LQVISEEIER TTGSRVKVVQ
110 120 130 140 150
ADFTREDIYD HIEEQLKGLE IGVLVNNVGM LPNLLPSHFL STSGESQSVI
160 170 180 190 200
HCNITSVVKM TQLVLKHMES RRRGLILNIS SGVGVRPWPL YSLYSASKAF
210 220 230 240 250
VCTFSKALNV EYRDKGIIIQ VLTPYSVSTP MTKYLNTSRV TKTADEFVKE
260 270 280 290 300
SLKYVTIGAE TCGCLAHEIL AIILNLIPSR IFYSSTTQRF LLKQFSDYLK

SNISNR
Length:306
Mass (Da):34,223
Last modified:June 1, 1998 - v1
Checksum:i8B88584047614B53
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF035156 mRNA. Translation: AAB99739.1.
RefSeqiNP_446459.1. NM_054007.1.
UniGeneiRn.10895.

Genome annotation databases

GeneIDi117182.
KEGGirno:117182.
UCSCiRGD:621805. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF035156 mRNA. Translation: AAB99739.1.
RefSeqiNP_446459.1. NM_054007.1.
UniGeneiRn.10895.

3D structure databases

ProteinModelPortaliO54939.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025850.

Chemistry

BindingDBiO54939.
ChEMBLiCHEMBL1075158.

PTM databases

iPTMnetiO54939.

Proteomic databases

PaxDbiO54939.
PRIDEiO54939.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi117182.
KEGGirno:117182.
UCSCiRGD:621805. rat.

Organism-specific databases

CTDi3293.
RGDi621805. Hsd17b3.

Phylogenomic databases

eggNOGiKOG1014. Eukaryota.
COG0300. LUCA.
HOGENOMiHOG000039237.
HOVERGENiHBG005478.
InParanoidiO54939.
KOiK10207.
PhylomeDBiO54939.

Enzyme and pathway databases

UniPathwayiUPA00367.
BRENDAi1.1.1.64. 5301.

Miscellaneous databases

NextBioi620038.
PROiO54939.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR033281. HSD17B3.
IPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PTHR24322:SF621. PTHR24322:SF621. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PIRSFiPIRSF000126. 11-beta-HSD1. 1 hit.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Khanum A., Tsai-Morris C.-H., Dufau M.L.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiDHB3_RAT
AccessioniPrimary (citable) accession number: O54939
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: May 11, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.