Primary Information |
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BoMiProt ID | Bomi9021 |
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Protein Name | Septin-1 |
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Organism | Bos taurus |
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Uniprot ID | A5PJU9 |
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Milk Fraction | Whey |
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Ref Sequence ID | NP_001092417.1 |
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Aminoacid Length | 367 |
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Molecular Weight | 41983 |
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FASTA Sequence |
Download |
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Gene Name | SEPTIN1/SEPT1 |
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Gene ID | 512478 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | Septin 1 is a member of an evolutionarily conserved family of GTP-binding and filament-forming proteins named septins, which function in diverse processes including cytokinasis, vesicle trafficking, apoptosis, remodelling of the cytoskeleton, infection, neurodegeneration and neoplasia. |
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Biochemical Properties | Septins are an evolutionarily conserved group of GTP-binding and filament-forming proteins that belong to the large superclass of P-loop GTPases. The septins were first recognized in Saccharomyces cerevisiae as a set of homologous proteins (the products of the CDC3, CDC10, CDC11 and CDC12 genes) associated with the 10 nm filaments found at the cytoplasmic face of the plasma membrane in the mother-bud neck |
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PTMs | Phosphorylation at Ser/Thr |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|A5PJU9|SEPT1_BOVIN Septin-1 OS=Bos taurus OX=9913 GN=SEPTIN1 PE=2 SV=1
MDKEYVGFAALPNQLHRKSVKKGFDFTLMVAGESGLGKSTLINSLFLTNLYEDRQIPEAS
ARLTQTLTIERRGVEIEEGGIKVKLTVVDTPGFGDSVDCSDCWLPVVRFIEEQFEQYLRD
ESGLNRKNIQDSRVHCCLYFISPFGRGLRPLDVAFLRAVHEKVNIIPVIGKADALMPKET
QALKQKIREQLKEEEINIYQFPECDS*206DEDEDFKRQDAEMKESIPFAVVGSCEVVRDGGPR
PVRGRHYS*248WGT*251VEVENPHHCDFLNLRRMLVQTHLQDLKEVTHDLLYEGYRARCLQSLARP
GARDRAS*307RSKLSRQS*315ATEIPLPMLPLADTEKLIREKDEELRRMQEMLEKMQAQMQLSQAQ
GEQSDAL
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Predicted Disorder Regions | 202-211, 298-367 |
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DisProt Annotation | |
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TM Helix Prediction | no TM helices |
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Additional Comments | Septin 1 with site-directed mutations of five serine residues (Ser19, Ser206, Ser307, Ser312 and Ser315) has a much lower degree of aggregation and better structural homogeneity and that the mutations cause only slight perturbations in the secondary structure of septin 1. |
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Bibliography | 1.Hu H, Yu WB, Li SX, Ding XM, Yu L, Bi RC. Crystallization and preliminary crystallographic studies of human septin 1 with site-directed mutations. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Feb 1;62(Pt 2):128-32. doi: 10.1107/S1744309105043228. Epub 2006 Jan 27. PMID: 16511282; PMCID: PMC2150944. |