Q7Z5P4 · DHB13_HUMAN
- Protein17-beta-hydroxysteroid dehydrogenase 13
- GeneHSD17B13
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids300 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a pivotal role in hepatic lipid metabolism (PubMed:29562163).
In vitro, it catalyzes the oxidation of a variety of lipid substrates, including 17beta-estradiol, retinol, retinal, and leukotriene B4 (PubMed:29562163, PubMed:30415504, PubMed:32973038).
In vitro, it catalyzes the oxidation of a variety of lipid substrates, including 17beta-estradiol, retinol, retinal, and leukotriene B4 (PubMed:29562163, PubMed:30415504, PubMed:32973038).
Isoform 2
Has retinol/retinal dehydrogenase activity in vitro.
Isoform 1
Does not have retinol/retinal dehydrogenase activity in vitro.
Catalytic activity
- 17beta-estradiol + NAD+ = estrone + H+ + NADH
Isoform 2
all-trans-retinal + H2O + NAD+ = all-trans-retinoate + 2 H+ + NADH
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
6.08 μM | 17beta-estradiol |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
0.94 nmol/min/mg | with 17beta-estradiol as substrate |
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | lipid droplet | |
Molecular Function | all-trans-retinol dehydrogenase (NAD+) activity | |
Molecular Function | estradiol 17-beta-dehydrogenase [NAD(P)+] activity | |
Molecular Function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor | |
Molecular Function | steroid dehydrogenase activity | |
Biological Process | lipid metabolic process | |
Biological Process | positive regulation of lipid biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name17-beta-hydroxysteroid dehydrogenase 13
- EC number
- Short names17-beta-HSD 13
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ7Z5P4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Isoform 2
Note: Redistributed from the endoplasmic reticulum to lipids droplets in the cell upon induction of lipids droplet formation.
Isoform 1
Note: Does not localize to lipid droplets.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 22-28 | Does not localize to lipid droplets. | ||||
Sequence: Missing | ||||||
Mutagenesis | 47-49 | Loss of retinol/retinal dehydrogenase activity. | ||||
Sequence: GIG → AIA | ||||||
Mutagenesis | 69-84 | Does not localize to lipid droplets. | ||||
Sequence: Missing | ||||||
Mutagenesis | 85-93 | Does not localize to lipid droplets. | ||||
Sequence: Missing | ||||||
Mutagenesis | 94-106 | Does not localize to lipid droplets. | ||||
Sequence: Missing | ||||||
Mutagenesis | 97 | Decreased retinol/retinal dehydrogenase activity; when associated with A-101. | ||||
Sequence: R → A | ||||||
Mutagenesis | 101 | Decreased retinol/retinal dehydrogenase activity; when associated with A-97. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 144 | Loss of retinol/retinal dehydrogenase activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 153 | Loss of retinol/retinal dehydrogenase activity; when associated with A-156. | ||||
Sequence: K → A | ||||||
Mutagenesis | 156 | Loss of retinol/retinal dehydrogenase activity; when associated with A-153. | ||||
Sequence: L → A | ||||||
Mutagenesis | 172 | Loss of retinol/retinal dehydrogenase activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 185 | Loss of retinol/retinal dehydrogenase activity; when associated with A-189. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 189 | Loss of retinol/retinal dehydrogenase activity; when associated with A-185. | ||||
Sequence: K → A | ||||||
Mutagenesis | 199 | Loss of retinol/retinal dehydrogenase activity; when associated with A-202. | ||||
Sequence: L → A | ||||||
Mutagenesis | 202 | Loss of retinol/retinal dehydrogenase activity; when associated with A-199. | ||||
Sequence: E → A | ||||||
Mutagenesis | 208 | Decreased retinol/retinal dehydrogenase activity. | ||||
Sequence: K → A | ||||||
Natural variant | VAR_087865 | 260 | loss of retinol/retinal dehydrogenase activity; does not affect localization to lipid droplets; dbSNP:rs62305723 | |||
Sequence: P → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 341 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-19 | UniProt | |||||
Sequence: MNIILEILLLLITIIYSYL | |||||||
Chain | PRO_0000042583 | 20-300 | UniProt | 17-beta-hydroxysteroid dehydrogenase 13 | |||
Sequence: ESLVKFFIPQRRKSVAGEIVLITGAGHGIGRQTTYEFAKRQSILVLWDINKRGVEETAAECRKLGVTAHAYVVDCSNREEIYRSLNQVKKEVGDVTIVVNNAGTVYPADLLSTKDEEITKTFEVNILGHFWITKALLPSMMERNHGHIVTVASVCGHEGIPYLIPYCSSKFAAVGFHRGLTSELQALGKTGIKTSCLCPVFVNTGFTKNPSTRLWPVLETDEVVRSLIDGILTNKKMIFVPSYINIFLRLQKFLPERASAILNRMQNIQFEAVVGHKIKMK | |||||||
Modified residue | 33 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 138 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q7Z5P4-1
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.
- Name2
- SynonymsIsoform A
- Length300
- Mass (Da)33,655
- Last updated2003-10-01 v1
- Checksum5B85778554265DFE
Q7Z5P4-2
- Name1
- SynonymsIsoform B
- Differences from canonical
- 71-106: Missing
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_015860 | 71-106 | in isoform 1 | |||
Sequence: Missing |
Polymorphism
The insertion of an adenine adjacent to the donor splice site of exon 6 (dbSNP:rs72613567) is associated with reduced risk of non-alcoholic fatty liver disease and protection from chronic liver disease [MIM:620116]. It is also associated with reduced risk of hepatocellular carcinoma (PubMed:29562163, PubMed:34930143).
Variant rs72613567 alters mRNA splicing and results in the synthesis of a truncated, unstable protein. Liver samples from variant carriers contain reduced levels of isoform 1 and isoform 2 transcripts (PubMed:29562163).
Variant rs72613567 alters mRNA splicing and results in the synthesis of a truncated, unstable protein. Liver samples from variant carriers contain reduced levels of isoform 1 and isoform 2 transcripts (PubMed:29562163).
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY186249 EMBL· GenBank· DDBJ | AAO72313.1 EMBL· GenBank· DDBJ | mRNA | ||
AY186250 EMBL· GenBank· DDBJ | AAO72314.1 EMBL· GenBank· DDBJ | mRNA | ||
AY268355 EMBL· GenBank· DDBJ | AAP42289.1 EMBL· GenBank· DDBJ | mRNA | ||
AY358575 EMBL· GenBank· DDBJ | AAQ88938.1 EMBL· GenBank· DDBJ | mRNA | ||
AB073347 EMBL· GenBank· DDBJ | BAD38632.1 EMBL· GenBank· DDBJ | mRNA | ||
AK292784 EMBL· GenBank· DDBJ | BAF85473.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471057 EMBL· GenBank· DDBJ | EAX05986.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC112303 EMBL· GenBank· DDBJ | AAI12304.1 EMBL· GenBank· DDBJ | mRNA | ||
BC112305 EMBL· GenBank· DDBJ | AAI12306.1 EMBL· GenBank· DDBJ | mRNA |