Primary Information |
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| BoMiProt ID | Bomi9019 |
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| Protein Name | Sepiapterin reductase |
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| Organism | Bos taurus |
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| Uniprot ID | Q17QK8 |
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| Milk Fraction | Exosomes |
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| Ref Sequence ID | NP_001069471.1 |
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| Aminoacid Length | 267 |
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| Molecular Weight | 28939 |
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| FASTA Sequence |
Download |
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| Gene Name | SPR |
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| Gene ID | 533836 |
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| Protein Existence Status | Reviewed |
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Secondary Information |
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| Protein Function | Sepiapterin reductase, a homodimer composed of two subunits, plays an important role in the biosynthesis of tetrahydrobiopterin. |
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| Biochemical Properties | This protein has 261 amino acids of each monomer fold into a single domain with an α/β‐structure. A seven‐stranded anti‐parallel oriented β‐sheet in the centre of the molecule is sandwiched by two arrays of three α‐helices. Six of these strands could form a classic nicotinamide‐binding motif composed of βαβ units. The association of two monomers into the active homodimeric SPR leads to the formation of a four‐helix bundle (helices αE and αF of each monomer). |
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| PTMs | N-acetylation at Meth,Phosphorylation at Ser |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q17QK8|SPRE_BOVIN Sepiapterin reductase OS=Bos taurus OX=9913 GN=SPR PE=2 SV=1
MEGSVGKVGGLGRTLCVLTGASRGFGRTLAQVLAPLMS*38PRSVLVLSARNDEALRQLETEL
GAEWPGLRIVRVPADLGAETGLQQLVGALCDLPRPEGLQRVLLINNAGTLGDVSKRWVDL
TDPTEVNNYWTLNLTSTLCLTSSILQAFPDSPGLSRTVVNISSICALQPFKGWGLYCAGK
AARNMMFQVLAAEEPSVRVLS*201YGPGPLDTDMQQLARETS*219VDPDLRKSLQELKRKGELVDC
KISAQKLLSLLQNDKFESGAHIDFYDE
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Additional Comments | Sepiapterin reductase exhibits a wide distribution in different tissues and is associated with many diseases, including brain dysfunction, chronic pain, cardiovascular disease and cancer. |
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| Bibliography | 1.Wu Y, Chen P, Sun L, Yuan S, Cheng Z, Lu L, Du H, Zhan M. Sepiapterin reductase: Characteristics and role in diseases. J Cell Mol Med. 2020 Sep;24(17):9495-9506. doi: 10.1111/jcmm.15608. Epub 2020 Jul 30. PMID: 32734666; PMCID: PMC7520308. 2.Auerbach G, Herrmann A, Gütlich M, et al. The 1.25 Å crystal structure of sepiapterin reductase reveals its binding mode to pterins and brain neurotransmitters. EMBO J. 1997;16:7219‐7230. 3.Supangat S, Seo KH, Choi YK, et al. Structure of chlorobium tepidum sepiapterin reductase complex reveals the novel substrate binding mode for stereospecific production of L‐threo‐tetrahydrobiopterin. J Biol Chem. 2006;281:2245‐2256. |
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