7VR8
Inward-facing structure of human EAAT2 in the substrate-free state
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005313 | molecular_function | L-glutamate transmembrane transporter activity |
A | 0005314 | molecular_function | high-affinity L-glutamate transmembrane transporter activity |
A | 0005515 | molecular_function | protein binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0006750 | biological_process | glutathione biosynthetic process |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0006836 | biological_process | neurotransmitter transport |
A | 0006865 | biological_process | amino acid transport |
A | 0007268 | biological_process | chemical synaptic transmission |
A | 0007399 | biological_process | nervous system development |
A | 0007632 | biological_process | visual behavior |
A | 0008509 | molecular_function | monoatomic anion transmembrane transporter activity |
A | 0009410 | biological_process | response to xenobiotic stimulus |
A | 0009416 | biological_process | response to light stimulus |
A | 0009611 | biological_process | response to wounding |
A | 0009986 | cellular_component | cell surface |
A | 0015175 | molecular_function | neutral L-amino acid transmembrane transporter activity |
A | 0015179 | molecular_function | L-amino acid transmembrane transporter activity |
A | 0015293 | molecular_function | symporter activity |
A | 0015501 | molecular_function | glutamate:sodium symporter activity |
A | 0015804 | biological_process | neutral amino acid transport |
A | 0015813 | biological_process | L-glutamate transmembrane transport |
A | 0016020 | cellular_component | membrane |
A | 0021537 | biological_process | telencephalon development |
A | 0030424 | cellular_component | axon |
A | 0030534 | biological_process | adult behavior |
A | 0030673 | cellular_component | axolemma |
A | 0031982 | cellular_component | vesicle |
A | 0033229 | molecular_function | cysteine transmembrane transporter activity |
A | 0035264 | biological_process | multicellular organism growth |
A | 0042734 | cellular_component | presynaptic membrane |
A | 0043200 | biological_process | response to amino acid |
A | 0044297 | cellular_component | cell body |
A | 0044306 | cellular_component | neuron projection terminus |
A | 0045121 | cellular_component | membrane raft |
A | 0045202 | cellular_component | synapse |
A | 0046326 | biological_process | positive regulation of D-glucose import |
A | 0046872 | molecular_function | metal ion binding |
A | 0070207 | biological_process | protein homotrimerization |
A | 0070633 | biological_process | transepithelial transport |
A | 0070778 | biological_process | L-aspartate transmembrane transport |
A | 0070779 | biological_process | D-aspartate import across plasma membrane |
A | 0071314 | biological_process | cellular response to cocaine |
A | 0097449 | cellular_component | astrocyte projection |
A | 0098656 | biological_process | monoatomic anion transmembrane transport |
A | 0098712 | biological_process | L-glutamate import across plasma membrane |
A | 0098796 | cellular_component | membrane protein complex |
A | 0098810 | biological_process | neurotransmitter reuptake |
A | 0098978 | cellular_component | glutamatergic synapse |
A | 0140009 | biological_process | L-aspartate import across plasma membrane |
A | 0150104 | biological_process | transport across blood-brain barrier |
A | 1903712 | biological_process | cysteine transmembrane transport |
Functional Information from PROSITE/UniProt
site_id | PS00713 |
Number of Residues | 15 |
Details | NA_DICARBOXYL_SYMP_1 Sodium:dicarboxylate symporter family signature 1. P.GDiLMrMLKMLIlP |
Chain | Residue | Details |
A | PRO81-PRO95 |
site_id | PS00714 |
Number of Residues | 24 |
Details | NA_DICARBOXYL_SYMP_2 Sodium:dicarboxylate symporter family signature 2. PvGaTiNMDGTaLYeaVaaIFIAQ |
Chain | Residue | Details |
A | PRO391-GLN414 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 154 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
Chain | Residue | Details |
A | MET1-ASN44 | |
A | ASP109-ALA120 | |
A | GLY260-ASP268 | |
A | THR340-PRO344 | |
A | GLU376-ARG384 | |
A | TYR494-LYS574 |
site_id | SWS_FT_FI2 |
Number of Residues | 60 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
A | LEU45-LEU64 | |
A | MET88-LEU108 | |
A | MET121-ILE142 |
site_id | SWS_FT_FI3 |
Number of Residues | 158 |
Details | TOPO_DOM: Extracellular => ECO:0000305 |
Chain | Residue | Details |
A | ARG65-ARG87 | |
A | HIS143-GLU235 | |
A | CYS297-MET317 | |
A | ILE412-GLN424 | |
A | LEU459-ASP471 |
site_id | SWS_FT_FI4 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000250|UniProtKB:P43003 |
Chain | Residue | Details |
A | PHE236-MET259 |
site_id | SWS_FT_FI5 |
Number of Residues | 27 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000250|UniProtKB:P43003 |
Chain | Residue | Details |
A | PHE269-ILE296 |
site_id | SWS_FT_FI6 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000250|UniProtKB:P43003 |
Chain | Residue | Details |
A | VAL318-VAL339 |
site_id | SWS_FT_FI7 |
Number of Residues | 63 |
Details | INTRAMEM: Discontinuously helical => ECO:0000250|UniProtKB:P43003 |
Chain | Residue | Details |
A | PHE345-LEU375 | |
A | ILE425-GLY458 |
site_id | SWS_FT_FI8 |
Number of Residues | 26 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000250|UniProtKB:P43003 |
Chain | Residue | Details |
A | VAL385-PHE411 |
site_id | SWS_FT_FI9 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=8 => ECO:0000250|UniProtKB:P43003 |
Chain | Residue | Details |
A | TRP472-VAL493 |
site_id | SWS_FT_FI10 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P43003 |
Chain | Residue | Details |
A | ALA362 | |
A | THR395 | |
A | THR401 | |
A | ILE442 | |
A | ASP475 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:O59010 |
Chain | Residue | Details |
A | GLY393 | |
A | ASN397 | |
A | ASN482 | |
A | ASP486 |
site_id | SWS_FT_FI12 |
Number of Residues | 3 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P31596 |
Chain | Residue | Details |
A | SER3 | |
A | SER21 | |
A | SER25 |
site_id | SWS_FT_FI13 |
Number of Residues | 7 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P43006 |
Chain | Residue | Details |
A | SER506 | |
A | SER521 | |
A | SER532 | |
A | SER534 | |
A | SER544 | |
A | SER560 | |
A | SER564 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P43006 |
Chain | Residue | Details |
A | TYR539 |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P43006 |
Chain | Residue | Details |
A | CYS38 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN206 | |
A | ASN216 |