Primary Information |
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| BoMiProt ID | Bomi41 |
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| Protein Name | Annexin A1 |
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| Organism | Bos taurus |
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| Uniprot ID | P46193 |
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| Milk Fraction | MFGM, Exosome |
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| Ref Sequence ID | NP_786978.2 |
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| Aminoacid Length | 346 |
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| Molecular Weight | 38952 |
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| FASTA Sequence |
Download |
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| Gene Name | ANXA1 |
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| Gene ID | 327662 |
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| Protein Existence Status | Reviewed: Experimental evidence at protein level |
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Secondary Information |
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| Protein Function | annexin I
aggregates membrane phospholipids; suppress phospholipase A2 activity; inhibits gland differentiation |
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| Biochemical Properties | Cytosolic annexin I
had a molecular mass of 36 kDa which was also found in the
nuclear fraction; A 38-kDa annexin I was
detected in nuclei; The cytosolic
and nuclear 36-kDa annexin I and
the nuclear 38-kDa annexin I showed
different isoelectric points; induced by glucocorticoids |
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| Significance in milk | increased glucocorticoid concentration
induces annexin A1, which is required for
the initiation of lactation |
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| PTMs | phosphorylated by pkc as found in bocine mammary gland; glycosylated as found in human placenta - presence of N-acetyl-D-galactosamine residues, two cc-linked
biantennary mannosyl residues, one site of
asparagine-linked glycosylation which may contain two a-linked biantennary mannosyl
residues; indicates a potential Nlinked
glycosylation site at the 42nd position of its amino terminal region |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Predicted Disorder Regions | (27-42) |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | Phosphorylation by protein kinase C
changes the pI of annexin I; Phosphorylation
by protein kinase C inhibits the
abilities of unphosphorylated annexin I to aggregate
membrane phospholipids and
to suppress phospholipase A2 activity |
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| Additional Comments | Annexin I and annexin II can then be easily
separated from each other by Mono S fast protein liquid chromatography |
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| Bibliography | 1. Katoh, N., Suzuki, T., Yuasa, A., & Miyamoto, T. (1995). Distribution of annexins I, II, and IV in bovine mammary gland. Journal of Dairy Science, 78(11), 2382–2387. https://doi.org/10.3168/jds.S0022-0302(95)76866-7.
2. Goulet, F., Moore, K. G., & Sartorelli, A. C. (1992). Glycosylation of annexin I and annexin II. Biochemical and Biophysical Research Communications, 188(2), 554–558. https://doi.org/10.1016/0006-291x(92)91091-4. |
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