|
|
1)
|
chain |
A |
residue |
154-168 |
type |
prosite |
sequence |
CPMDLKNFPMDVQTC
|
description |
NEUROTR_ION_CHANNEL Neurotransmitter-gated ion-channels signature. CpMdLknFPmDvqtC
|
source |
prosite : PS00236
|
|
2)
|
chain |
A |
residue |
239-260 |
type |
TRANSMEM |
sequence |
YLIQMYIPSLLIVILSWVSFWI
|
description |
Helical; Name=1 => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
3)
|
chain |
B |
residue |
239-260 |
type |
TRANSMEM |
sequence |
YLIQMYIPSLLIVILSWVSFWI
|
description |
Helical; Name=1 => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
4)
|
chain |
C |
residue |
239-260 |
type |
TRANSMEM |
sequence |
YLIQMYIPSLLIVILSWVSFWI
|
description |
Helical; Name=1 => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
5)
|
chain |
D |
residue |
239-260 |
type |
TRANSMEM |
sequence |
YLIQMYIPSLLIVILSWVSFWI
|
description |
Helical; Name=1 => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
6)
|
chain |
E |
residue |
239-260 |
type |
TRANSMEM |
sequence |
YLIQMYIPSLLIVILSWVSFWI
|
description |
Helical; Name=1 => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
7)
|
chain |
A |
residue |
54 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
8)
|
chain |
B |
residue |
54 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
9)
|
chain |
C |
residue |
54 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
10)
|
chain |
D |
residue |
54 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
11)
|
chain |
E |
residue |
54 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
12)
|
chain |
A |
residue |
261-265 |
type |
TOPO_DOM |
sequence |
NMDAA
|
description |
Cytoplasmic => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
13)
|
chain |
B |
residue |
261-265 |
type |
TOPO_DOM |
sequence |
NMDAA
|
description |
Cytoplasmic => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
14)
|
chain |
C |
residue |
261-265 |
type |
TOPO_DOM |
sequence |
NMDAA
|
description |
Cytoplasmic => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
15)
|
chain |
D |
residue |
261-265 |
type |
TOPO_DOM |
sequence |
NMDAA
|
description |
Cytoplasmic => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
16)
|
chain |
E |
residue |
261-265 |
type |
TOPO_DOM |
sequence |
NMDAA
|
description |
Cytoplasmic => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
17)
|
chain |
A |
residue |
266-286 |
type |
TRANSMEM |
sequence |
PARVGLGITTVLTMTTQSSGS
|
description |
Helical; Name=2 => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
18)
|
chain |
B |
residue |
266-286 |
type |
TRANSMEM |
sequence |
PARVGLGITTVLTMTTQSSGS
|
description |
Helical; Name=2 => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
19)
|
chain |
C |
residue |
266-286 |
type |
TRANSMEM |
sequence |
PARVGLGITTVLTMTTQSSGS
|
description |
Helical; Name=2 => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
20)
|
chain |
D |
residue |
266-286 |
type |
TRANSMEM |
sequence |
PARVGLGITTVLTMTTQSSGS
|
description |
Helical; Name=2 => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
21)
|
chain |
E |
residue |
266-286 |
type |
TRANSMEM |
sequence |
PARVGLGITTVLTMTTQSSGS
|
description |
Helical; Name=2 => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
22)
|
chain |
A |
residue |
287-297 |
type |
TOPO_DOM |
sequence |
RASLPKVSYVK
|
description |
Extracellular => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
23)
|
chain |
B |
residue |
287-297 |
type |
TOPO_DOM |
sequence |
RASLPKVSYVK
|
description |
Extracellular => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
24)
|
chain |
C |
residue |
287-297 |
type |
TOPO_DOM |
sequence |
RASLPKVSYVK
|
description |
Extracellular => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
25)
|
chain |
D |
residue |
287-297 |
type |
TOPO_DOM |
sequence |
RASLPKVSYVK
|
description |
Extracellular => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
26)
|
chain |
E |
residue |
287-297 |
type |
TOPO_DOM |
sequence |
RASLPKVSYVK
|
description |
Extracellular => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
27)
|
chain |
A |
residue |
298-318 |
type |
TRANSMEM |
sequence |
AIDIWMAVCLLFVFSALLEYA
|
description |
Helical; Name=3 => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
28)
|
chain |
B |
residue |
298-318 |
type |
TRANSMEM |
sequence |
AIDIWMAVCLLFVFSALLEYA
|
description |
Helical; Name=3 => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
29)
|
chain |
C |
residue |
298-318 |
type |
TRANSMEM |
sequence |
AIDIWMAVCLLFVFSALLEYA
|
description |
Helical; Name=3 => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
30)
|
chain |
D |
residue |
298-318 |
type |
TRANSMEM |
sequence |
AIDIWMAVCLLFVFSALLEYA
|
description |
Helical; Name=3 => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
31)
|
chain |
E |
residue |
298-318 |
type |
TRANSMEM |
sequence |
AIDIWMAVCLLFVFSALLEYA
|
description |
Helical; Name=3 => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
32)
|
chain |
A |
residue |
208 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000250|UniProtKB:P23415
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
33)
|
chain |
D |
residue |
208 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000250|UniProtKB:P23415
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
34)
|
chain |
D |
residue |
210 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000250|UniProtKB:P23415
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
35)
|
chain |
D |
residue |
231 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000250|UniProtKB:P23415
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
36)
|
chain |
E |
residue |
208 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000250|UniProtKB:P23415
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
37)
|
chain |
E |
residue |
210 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000250|UniProtKB:P23415
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
38)
|
chain |
E |
residue |
231 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000250|UniProtKB:P23415
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
39)
|
chain |
A |
residue |
210 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000250|UniProtKB:P23415
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
40)
|
chain |
A |
residue |
231 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000250|UniProtKB:P23415
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
41)
|
chain |
B |
residue |
208 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000250|UniProtKB:P23415
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
42)
|
chain |
B |
residue |
210 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000250|UniProtKB:P23415
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
43)
|
chain |
B |
residue |
231 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000250|UniProtKB:P23415
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
44)
|
chain |
C |
residue |
208 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000250|UniProtKB:P23415
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
45)
|
chain |
C |
residue |
210 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000250|UniProtKB:P23415
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
46)
|
chain |
C |
residue |
231 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000250|UniProtKB:P23415
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
47)
|
chain |
A |
residue |
218 |
type |
BINDING |
sequence |
Y
|
description |
BINDING => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
48)
|
chain |
B |
residue |
218 |
type |
BINDING |
sequence |
Y
|
description |
BINDING => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
49)
|
chain |
C |
residue |
218 |
type |
BINDING |
sequence |
Y
|
description |
BINDING => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
50)
|
chain |
D |
residue |
218 |
type |
BINDING |
sequence |
Y
|
description |
BINDING => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
51)
|
chain |
E |
residue |
218 |
type |
BINDING |
sequence |
Y
|
description |
BINDING => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
52)
|
chain |
A |
residue |
277 |
type |
SITE |
sequence |
L
|
description |
Important for obstruction of the ion pore in the closed conformation => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
53)
|
chain |
B |
residue |
277 |
type |
SITE |
sequence |
L
|
description |
Important for obstruction of the ion pore in the closed conformation => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
54)
|
chain |
C |
residue |
277 |
type |
SITE |
sequence |
L
|
description |
Important for obstruction of the ion pore in the closed conformation => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
55)
|
chain |
D |
residue |
277 |
type |
SITE |
sequence |
L
|
description |
Important for obstruction of the ion pore in the closed conformation => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
56)
|
chain |
E |
residue |
277 |
type |
SITE |
sequence |
L
|
description |
Important for obstruction of the ion pore in the closed conformation => ECO:0000269|PubMed:26344198
|
source |
Swiss-Prot : SWS_FT_FI9
|
|