Q8TC12 · RDH11_HUMAN
- ProteinRetinol dehydrogenase 11
- GeneRDH11
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids318 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Retinol dehydrogenase with a clear preference for NADP. Displays high activity towards 9-cis, 11-cis and all-trans-retinol, and to a lesser extent on 13-cis-retinol (PubMed:12036956, PubMed:12226107, PubMed:29410696).
Exhibits a low reductive activity towards unsaturated medium-chain aldehydes such as cis -6-nonenal and no activity toward nonanal or 4-hydroxy-nonenal (PubMed:15865448).
Has no dehydrogenase activity towards steroid (PubMed:12036956, PubMed:12226107).
Exhibits a low reductive activity towards unsaturated medium-chain aldehydes such as cis -6-nonenal and no activity toward nonanal or 4-hydroxy-nonenal (PubMed:15865448).
Has no dehydrogenase activity towards steroid (PubMed:12036956, PubMed:12226107).
Miscellaneous
Shows clear specificity for the pro-S hydrogen on C4 of NADPH and the pro-R hydrogen on C15 of retinols.
Catalytic activity
- all-trans-retinol + NADP+ = all-trans-retinal + H+ + NADPH
- 11-cis-retinol + NADP+ = 11-cis-retinal + H+ + NADPH
- 9-cis-retinol + NADP+ = 9-cis-retinal + H+ + NADPH
- 13-cis-retinol + NADP+ = 13-cis-retinal + H+ + NADPH
Activity regulation
SELENOF decreases the retinol dehydrogenase activity.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.23 μM | NADPH | |||||
0.8 μM | NADP | |||||
0.5 μM | all-trans-retinal | |||||
0.62 μM | 13-cis-retinal | |||||
0.19 μM | 9-cis-retinal | |||||
1.3 μM | all-trans-retinol | |||||
5 μM | (Z)-non-6-enol |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
18 nmol/min/mg | with all-trans-retinal as substrate | ||||
7 nmol/min/mg | with 13-cis-retinal as substrate | ||||
1.6 nmol/min/mg | with 9-cis-retinal as substrate | ||||
0.95 nmol/min/mg | with all-trans-retinol as substrate | ||||
19 nmol/min/mg | with (Z)-non-6-enol |
Vmax is measured per mg microsomal protein.
Pathway
Cofactor metabolism; retinol metabolism.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | photoreceptor inner segment | |
Molecular Function | 11-cis-retinol dehydrogenase activity | |
Molecular Function | aldehyde dehydrogenase (NADP+) activity | |
Molecular Function | all-trans-retinol dehydrogenase (NAD+) activity | |
Molecular Function | all-trans-retinol dehydrogenase (NADP+) activity | |
Molecular Function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor | |
Biological Process | cellular detoxification of aldehyde | |
Biological Process | retinal metabolic process | |
Biological Process | retinoid metabolic process | |
Biological Process | retinol metabolic process | |
Biological Process | visual perception |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameRetinol dehydrogenase 11
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8TC12
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Single-pass type II membrane protein
Features
Showing features for transmembrane, topological domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 1-21 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: MVELMFPLLLLLLPFLLYMAA | ||||||
Topological domain | 22-318 | Cytoplasmic | ||||
Sequence: PQIRKMLSSGVCTSTVQLPGKVVVVTGANTGIGKETAKELAQRGARVYLACRDVEKGELVAKEIQTTTGNQQVLVRKLDLSDTKSIRAFAKGFLAEEKHLHVLINNAGVMMCPYSKTADGFEMHIGVNHLGHFLLTHLLLEKLKESAPSRIVNVSSLAHHLGRIHFHNLQGEKFYNAGLAYCHSKLANILFTQELARRLKGSGVTTYSVHPGTVQSELVRHSSFMRWMWWLFSFFIKTPQQGAQTSLHCALTEGLEILSGNHFSDCHVAWVSAQARNETIARRLWDVSCDLLGLPID |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Retinal dystrophy, juvenile cataracts, and short stature syndrome (RDJCSS)
- Note
- DescriptionA disorder characterized by retinal dystrophy resulting in progressive decrease in visual acuity and difficulties with night vision in the first decade of life, development of juvenile cataracts, facial dysmorphism, psychomotor developmental delays, learning disabilities and short stature. Ophthalmological findings include salt-and-pepper retinopathy, attenuation of the arterioles, generalized rod-cone dysfunction, mottled macula at an early age, and peripapillary sparing of the retinal pigment epithelium.
- See alsoMIM:616108
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 334 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000054763 | 1-318 | Retinol dehydrogenase 11 | |||
Sequence: MVELMFPLLLLLLPFLLYMAAPQIRKMLSSGVCTSTVQLPGKVVVVTGANTGIGKETAKELAQRGARVYLACRDVEKGELVAKEIQTTTGNQQVLVRKLDLSDTKSIRAFAKGFLAEEKHLHVLINNAGVMMCPYSKTADGFEMHIGVNHLGHFLLTHLLLEKLKESAPSRIVNVSSLAHHLGRIHFHNLQGEKFYNAGLAYCHSKLANILFTQELARRLKGSGVTTYSVHPGTVQSELVRHSSFMRWMWWLFSFFIKTPQQGAQTSLHCALTEGLEILSGNHFSDCHVAWVSAQARNETIARRLWDVSCDLLGLPID | ||||||
Modified residue | 112 | N6-acetyllysine | ||||
Sequence: K |
Post-translational modification
Not glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Predominantly expressed in the epithelial cells of prostate, in both basal and luminal secretory cell populations. Expressed at low levels in spleen, thymus, testis, ovary, small intestine, colon, peripherical blood leukocytes, kidney, adrenal gland and fetal liver. Not detected in prostatic fibromuscular stromal cells, endothelial cells, or infiltrating lymphocytes.
Induction
By androgens in prostate cancer cells.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with SELENOF.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8TC12 | SELENOF O60613 | 5 | EBI-2823756, EBI-1052797 | |
BINARY | Q8TC12 | UBAC1 Q9BSL1 | 2 | EBI-2823756, EBI-749370 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q8TC12-1
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
- Length318
- Mass (Da)35,386
- Last updated2003-08-29 v2
- Checksum5B0C366552774835
Q8TC12-2
- Name2
- Differences from canonical
- 52-64: Missing
Q8TC12-3
- Name3
- Differences from canonical
- 152-221: Missing
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_008159 | 52-64 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_046403 | 152-221 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 176 | in Ref. 9; AAH51291 | ||||
Sequence: S → F | ||||||
Sequence conflict | 294 | in Ref. 1; AAF89632 | ||||
Sequence: A → V | ||||||
Sequence conflict | 316 | in Ref. 9; AAH26274 | ||||
Sequence: P → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF167438 EMBL· GenBank· DDBJ | AAF89632.1 EMBL· GenBank· DDBJ | mRNA | ||
AF395068 EMBL· GenBank· DDBJ | AAK72049.1 EMBL· GenBank· DDBJ | mRNA | ||
AF151840 EMBL· GenBank· DDBJ | AAD34077.1 EMBL· GenBank· DDBJ | mRNA | ||
CR457180 EMBL· GenBank· DDBJ | CAG33461.1 EMBL· GenBank· DDBJ | mRNA | ||
AK289427 EMBL· GenBank· DDBJ | BAF82116.1 EMBL· GenBank· DDBJ | mRNA | ||
AK293355 EMBL· GenBank· DDBJ | BAG56871.1 EMBL· GenBank· DDBJ | mRNA | ||
AK314465 EMBL· GenBank· DDBJ | BAG37073.1 EMBL· GenBank· DDBJ | mRNA | ||
AK074749 EMBL· GenBank· DDBJ | BAG51997.1 EMBL· GenBank· DDBJ | mRNA | ||
AL049779 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471061 EMBL· GenBank· DDBJ | EAW80950.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000112 EMBL· GenBank· DDBJ | AAH00112.1 EMBL· GenBank· DDBJ | mRNA | ||
BC011727 EMBL· GenBank· DDBJ | AAH11727.1 EMBL· GenBank· DDBJ | mRNA | ||
BC026274 EMBL· GenBank· DDBJ | AAH26274.1 EMBL· GenBank· DDBJ | mRNA | ||
BC037302 EMBL· GenBank· DDBJ | AAH37302.1 EMBL· GenBank· DDBJ | mRNA | ||
BC051291 EMBL· GenBank· DDBJ | AAH51291.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ426886 EMBL· GenBank· DDBJ | ABD90542.1 EMBL· GenBank· DDBJ | mRNA |