Primary Information |
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| BoMiProt ID | Bomi9134 |
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| Protein Name | Shadow of prion protein/Protein shadoo |
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| Organism | Bos taurus |
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| Uniprot ID | A0RZB4 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001073790.1 |
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| Aminoacid Length | 143 |
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| Molecular Weight | 13982 |
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| FASTA Sequence |
Download |
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| Gene Name | SPRN |
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| Gene ID | 616266 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | involved in prion pathogenesis. mutations in SPRN and the incidence of variant and sporadic Creutzfeldt-Jakob disease. Sho may play a role in the physiological function of PrP(C) and prion pathogenesis. |
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| Biochemical Properties | interaction between Sho 61-77 and PrP(C) 108-126 domains. Sho resembles the N-terminal domain of PrPC but lacks the C-terminal α-helices and β-sheet regions of the latter.Sho has a series of N-terminal charged tetrarepeats rich in glycine, serine, alanine and arginine. Sho contains a GPI anchor, N-glycosylation at one or two sites and a cleavage event likely positions the N-terminal to the hydrophobic tract. |
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| Significance in milk | accelerates the progression of prion diseases |
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| PTMs | N-glycosylated. |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|A0RZB4|SPRN_BOVIN Shadow of prion protein OS=Bos taurus OX=9913 GN=SPRN PE=2 SV=1
MNWAAAVCWALLLAATFLCDGSAAKGGRGGARGSARGGRGAARVRVRPAPRYAGSSMRVA
AGAAAGAAAGAAAGLAAGSSWRRAAGPAELGPEDAEDGAPGSN*163GTGRGVYSYWAWTSGTG
PTGHRHLCPLLGGALGALRLLRP |
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| Predicted Disorder Regions | 2 disordered segments; (26-42), (85-105) |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Bibliography | Jiayu W, Zhu H, Ming X, Xiong W, Songbo W, Bocui S, Wensen L, Jiping L, Keying M, Zhongyi L, Hongwei G. Mapping the interaction site of prion protein and Sho. Mol Biol Rep. 2010 Jun;37(5):2295-300. doi: 10.1007/s11033-009-9722-0. Epub 2009 Aug 15. PMID: 19685161. |
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