Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005911 | cellular_component | cell-cell junction |
| A | 0006836 | biological_process | neurotransmitter transport |
| A | 0006874 | biological_process | intracellular calcium ion homeostasis |
| A | 0007268 | biological_process | chemical synaptic transmission |
| A | 0008021 | cellular_component | synaptic vesicle |
| A | 0016020 | cellular_component | membrane |
| A | 0016082 | biological_process | synaptic vesicle priming |
| A | 0019901 | molecular_function | protein kinase binding |
| A | 0022857 | molecular_function | transmembrane transporter activity |
| A | 0030672 | cellular_component | synaptic vesicle membrane |
| A | 0031410 | cellular_component | cytoplasmic vesicle |
| A | 0031594 | cellular_component | neuromuscular junction |
| A | 0042995 | cellular_component | cell projection |
| A | 0043005 | cellular_component | neuron projection |
| A | 0045202 | cellular_component | synapse |
| A | 0048786 | cellular_component | presynaptic active zone |
| A | 0055085 | biological_process | transmembrane transport |
| A | 0098793 | cellular_component | presynapse |
| A | 0098978 | cellular_component | glutamatergic synapse |
| A | 0098982 | cellular_component | GABA-ergic synapse |
| B | 0005576 | cellular_component | extracellular region |
Functional Information from PROSITE/UniProt
| site_id | PS00217 |
| Number of Residues | 26 |
| Details | SUGAR_TRANSPORT_2 Sugar transport proteins signature 2. LsGVGiGGsipivfsYfsEflaqekR |
| Chain | Residue | Details |
| A | LEU264-ARG289 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 240 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 174 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 44 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q02563","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9JIS5","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | Motif: {"description":"Host ganglioside-binding motif","evidences":[{"source":"UniProtKB","id":"P0DPI0","evidenceCode":"ECO:0000250"}]} |
