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	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	0098657	biological_process	import into cell
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	60
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	66
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	23
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"UniProtKB","id":"P43003","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	20
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	27
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"UniProtKB","id":"P43003","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	21
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"UniProtKB","id":"P43003","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	63
Details	Intramembrane: {"description":"Discontinuously helical","evidences":[{"source":"UniProtKB","id":"P43003","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	26
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"UniProtKB","id":"P43003","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	21
Details	Transmembrane: {"description":"Helical; Name=8","evidences":[{"source":"UniProtKB","id":"P43003","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P43003","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"O59010","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---