Table 1.
Lewis A bearing glycoproteins from stems and siliques of A. thaliana Col-0 and shoots of O. sativa japonica.
| UniProt Accession | Name | Potential N-glycosylation sites | Predicted Localization | Proposed Function |
|---|---|---|---|---|
| A. thaliana stems | ||||
| O80434 | Laccase 4 (IRX12) | 14 | Secreted | Lignin biosynthesis |
| Q9LFW3 | COBRA-like protein 4 (COBL4) | 8 | Secreted (GPI-anchored) | Cellulose biosynthesis |
| Q38890 | Endoglucanase 25 (KORRIGAN) | 8 | Plasma membrane | Cellulose biosynthesis |
| Q8LED3 | Protein trichome birefringence-like 3 (TBL3) | 6 | Golgi apparatus | Deposition of cellulose |
| Q9LE45 | O-fucosyltransferase family protein (SUB1) | 11 | Golgi apparatus | Transfer of glycosyl-residues |
| A. thaliana siliques | ||||
| Q38890 | Endoglucanase 25 (KORRIGAN) | 8 | Plasma membrane | Cellulose biosynthesis |
| O80434 | Laccase 4 (IRX12) | 14 | Secreted | Lignin biosynthesis |
| Q9FJD5 | Laccase 17 (LAC17) | 15 | Secreted | Lignin biosynthesis |
| Q9LFW3 | COBRA-like protein 4 (COBL4) | 8 | Secreted (GPI-anchored) | Cellulose biosynthesis |
| Q9LMG7 | Probable inactive purple acid phosphatase 2 (PAP2) | 8 | Secreted | Protein of unknown function |
| Q8LED3 | Protein trichome birefringence-like 3 (TBL3) | 6 | Golgi apparatus | Secondary cell wall biosynthesis |
| F4IH21 | Protein trichome birefringence-like 33 (TBL33) | 6 | Golgi apparatus | Secondary cell wall biosynthesis |
| O. sativa shoots | ||||
| Q306J3 | Dirigent protein (JAC1) | 5 | Secreted | Biosynthesis of lignans, flavonolignans, and alkaloids |
| Q8H8C7 | Chitin elicitor-binding protein (CEBIP) | 11 | Plasma membrane | Chitin binding |
| Q6K7X0 | Os02g0615800 protein | 21 | Plasma membrane | Receptor kinase |
| Q6F3A5 | Beta-Ig-H3 domain-containing protein | 2 | Secreted | Cell surface adhesion protein |
| Q6ZFH9 | Glycerophosphodiester Phospodiesterase | 12 | Secreted | Lipid metabolism |
| Q6ESF0 | Germin-like protein 2-4 | 2 | Secreted | Plant defense |
Proteins were affinity-purified using the JIM84 antibody and identified via mass spectrometry using peptide mapping. The number of potential N-glycosylation sites is based on predictions using the NetNGlyc 1.0 Server (http://www.cbs.dtu.dk/services/NetNGlyc/). The localization and proposed function are based on information from the UniProt-database (https://www.uniprot.org/) and predictions using TargetP (http://www.cbs.dtu.dk/services/TargetP/).