Q9H2F3 · 3BHS7_HUMAN
- Protein3 beta-hydroxysteroid dehydrogenase type 7
- GeneHSD3B7
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids369 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids. HSD VII is active against four 7-alpha-hydroxylated sterols. Does not metabolize several different C(19/21) steroids as substrates. Involved in bile acid synthesis (PubMed:11067870).
Plays a key role in cell positioning and movement in lymphoid tissues by mediating degradation of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC): 7-alpha,25-OHC acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor for a number of lymphoid cells (By similarity).
Plays a key role in cell positioning and movement in lymphoid tissues by mediating degradation of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC): 7-alpha,25-OHC acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor for a number of lymphoid cells (By similarity).
Catalytic activity
- 7alpha-hydroxycholesterol + NAD+ = 7alpha-hydroxycholest-4-en-3-one + H+ + NADHThis reaction proceeds in the forward direction.
- 7alpha,25-dihydroxycholesterol + NAD+ = 7alpha,25-dihydroxy-4-cholesten-3-one + H+ + NADHThis reaction proceeds in the forward direction.
- (25R)-cholest-5-en-3beta,7alpha,26-triol + NAD+ = (25R)-7alpha,26-dihydroxycholest-4-en-3-one + H+ + NADHThis reaction proceeds in the forward direction.
- (24S)-7alpha-dihydroxycholesterol + NAD+ = (24S)-7alpha,24-dihydroxycholest-4-en-3-one + H+ + NADHThis reaction proceeds in the forward direction.
Pathway
Lipid metabolism; steroid biosynthesis.
Features
Showing features for active site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | lipid droplet | |
Molecular Function | 3-beta-hydroxy-delta5-steroid dehydrogenase (NAD+) activity | |
Molecular Function | cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase activity | |
Molecular Function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor | |
Biological Process | B cell chemotaxis | |
Biological Process | bile acid biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended name3 beta-hydroxysteroid dehydrogenase type 7
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9H2F3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 289-309 | Helical | ||||
Sequence: LLPYWLLVFLAALNALLQWLL | ||||||
Transmembrane | 311-331 | Helical | ||||
Sequence: PLVLYAPLLNPYTLAVANTTF |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Congenital bile acid synthesis defect 1 (CBAS1)
- Note
- DescriptionA primary defect in bile synthesis leading to progressive liver disease. Clinical features include neonatal jaundice, severe intrahepatic cholestasis, cirrhosis.
- See alsoMIM:607765
Natural variants in CBAS1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_054775 | 19 | G>S | in CBAS1 | |
VAR_054776 | 147 | E>K | in CBAS1; loss of activity; dbSNP:rs104894518 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_054775 | 19 | in CBAS1 | |||
Sequence: G → S | ||||||
Natural variant | VAR_054776 | 147 | in CBAS1; loss of activity; dbSNP:rs104894518 | |||
Sequence: E → K | ||||||
Natural variant | VAR_031040 | 250 | in dbSNP:rs9938550 | |||
Sequence: T → A | ||||||
Natural variant | VAR_048100 | 347 | in dbSNP:rs34212827 | |||
Sequence: L → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 460 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000087791 | 1-369 | 3 beta-hydroxysteroid dehydrogenase type 7 | |||
Sequence: MADSAQAQKLVYLVTGGCGFLGEHVVRMLLQREPRLGELRVFDQHLGPWLEELKTGPVRVTAIQGDVTQAHEVAAAVAGAHVVIHTAGLVDVFGRASPKTIHEVNVQGTRNVIEACVQTGTRFLVYTSSMEVVGPNTKGHPFYRGNEDTPYEAVHRHPYPCSKALAEWLVLEANGRKVRGGLPLVTCALRPTGIYGEGHQIMRDFYRQGLRLGGWLFRAIPASVEHGRVYVGNVAWMHVLAARELEQRATLMGGQVYFCYDGSPYRSYEDFNMEFLGPCGLRLVGARPLLPYWLLVFLAALNALLQWLLRPLVLYAPLLNPYTLAVANTTFTVSTDKAQRHFGYEPLFSWEDSRTRTILWVQAATGSAQ |
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9H2F3-1
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.
- Name1
- Length369
- Mass (Da)41,016
- Last updated2004-05-24 v2
- Checksum7254A5DAAFAC23E7
Q9H2F3-2
- Name2
- Differences from canonical
- 178-369: VRGGLPLVTCALRPTGIYGEGHQIMRDFYRQGLRLGGWLFRAIPASVEHGRVYVGNVAWMHVLAARELEQRATLMGGQVYFCYDGSPYRSYEDFNMEFLGPCGLRLVGARPLLPYWLLVFLAALNALLQWLLRPLVLYAPLLNPYTLAVANTTFTVSTDKAQRHFGYEPLFSWEDSRTRTILWVQAATGSAQ → AMLPGCTCWQPGSWSSGQP
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_042658 | 178-369 | in isoform 2 | |||
Sequence: VRGGLPLVTCALRPTGIYGEGHQIMRDFYRQGLRLGGWLFRAIPASVEHGRVYVGNVAWMHVLAARELEQRATLMGGQVYFCYDGSPYRSYEDFNMEFLGPCGLRLVGARPLLPYWLLVFLAALNALLQWLLRPLVLYAPLLNPYTLAVANTTFTVSTDKAQRHFGYEPLFSWEDSRTRTILWVQAATGSAQ → AMLPGCTCWQPGSWSSGQP | ||||||
Sequence conflict | 265 | in Ref. 1; AAG37824 | ||||
Sequence: Y → H | ||||||
Sequence conflict | 329 | in Ref. 1; AAG37824 | ||||
Sequence: T → A |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF277719 EMBL· GenBank· DDBJ | AAG37824.1 EMBL· GenBank· DDBJ | mRNA | ||
AK057436 EMBL· GenBank· DDBJ | BAB71486.1 EMBL· GenBank· DDBJ | mRNA | ||
AK290950 EMBL· GenBank· DDBJ | BAF83639.1 EMBL· GenBank· DDBJ | mRNA | ||
AK292068 EMBL· GenBank· DDBJ | BAF84757.1 EMBL· GenBank· DDBJ | mRNA | ||
AC135048 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471192 EMBL· GenBank· DDBJ | EAW52183.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC004929 EMBL· GenBank· DDBJ | AAH04929.1 EMBL· GenBank· DDBJ | mRNA |