Primary Information |
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| BoMiProt ID | Bomi8735 |
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| Protein Name | Retinol dehydrogenase 10 |
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| Organism | Bos taurus |
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| Uniprot ID | Q8HZT6 |
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| Milk Fraction | Whey,MFGM |
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| Ref Sequence ID | NP_777159.1 |
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| Aminoacid Length | 341 |
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| Molecular Weight | 38087 |
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| FASTA Sequence |
Download |
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| Gene Name | RDH10 |
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| Gene ID | 282852 |
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| Protein Existence Status | Reviewed |
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Secondary Information |
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| Protein Function | Participate in visual cycle. involved in the pathway retinol metabolism, which is part of Cofactor metabolism.Converts all-trans-retinol to all-trans-retinal.Involved in specification of the dorsoventral and anteroposterior body axes, as well as in pattern formation of the CNS. |
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| Biochemical Properties | It has retinoid oxidoreductase activity.Requires NADP+ as cofactor.all-trans-retinol + NADP+ = all-trans-retinal + H+ + NADPH.it contains cofactor binding motif(Gly-Xaa(3)-Gly-Xaa-Gly).The amino acid sequence homologies among RDH10 from different species are exceptionally high, with a 100% identity between bovine and human RDH10 and a 99% identity between mouse and human RDH10 at the amino acid level.Hydrophobic domains of RDH10 contribute to its membrane-anchoring. |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| NA |
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | 1TMH; (7-25) |
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| Additional Comments | Present in retinal pigment epithelium and retinal Müller cells.RDH10 deficiency causes embryonic lethality in the mouse, suggesting that other RDH members cannot substitute the function of RDH10 during the embryonic development. An important difference between RDH10 and other RDHs is its extremely high sequence homology across evolution, which support that RDH10 is functionally more significant than other RDH enzymes. RDH10 is likely to play an essential role in producing atRAL which is the substrate for synthesis of RA at early developmental stages. |
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| Bibliography | 1.Takahashi Y, Moiseyev G, Farjo K, Ma JX. Characterization of key residues and membrane association domains in retinol dehydrogenase 10. Biochem J. 2009 Apr 1;419(1):113-22, 1 p following 122. doi: 10.1042/BJ20080812. PMID: 19102727; PMCID: PMC2728083. 2.Strate I, Min TH, Iliev D, Pera EM. Retinol dehydrogenase 10 is a feedback regulator of retinoic acid signalling during axis formation and patterning of the central nervous system. Development. 2009 Feb;136(3):461-72. doi: 10.1242/dev.024901. PMID: 19141675. |
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