SitesBLAST

HLN 66:68 (≠ HIN 66:68) binding
Y138 (≠ F129) binding
GFA 199:201 (≠ GYA 190:192) binding
N203 (= N194) binding
R206 (= R197) binding
PL 236:237 (≠ PI 224:225) mutation to FW: No detectable water or glycerol permeability.

1fx8A Crystal structure of the e. Coli glycerol facilitator (glpf) with substrate glycerol (see paper)
38% identity, 96% coverage: 5:244/251 of query aligns to 1:251/254 of 1fx8A

query
sites
1fx8A

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x
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G

binding glycerol: W43 (≠ F47), N63 (= N68), G194 (= G190), F195 (≠ Y191), A196 (= A192), N198 (= N194), R201 (= R197)

Q96PS8 Aquaporin-10; AQP-10; Aquaglyceroporin-10; Small intestine aquaporin from Homo sapiens (Human) (see 2 papers)
37% identity, 94% coverage: 6:240/251 of query aligns to 20:261/301 of Q96PS8

query
sites
Q96PS8

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x
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Q

E27 (= E13) mutation to Q: Abolishes permeability to glycerol.
G73 (≠ A59) mutation to A: Increased permeability to glycerol at acidic pH.; mutation to F: Abolishes permeability to glycerol.
S77 (= S63) mutation S->A,D: Nearly abolishes permeability to glycerol.
H80 (= H66) mutation to A: Abolishes permeability to glycerol.
F85 (≠ V71) mutation to A: Nearly abolishes permeability to glycerol.
R94 (= R80) mutation to A: Abolishes permeability to glycerol.
N133 (≠ D116) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to Q: Abolishes N-glycosylation.

6f7hC Crystal structure of human aqp10 (see paper)
38% identity, 94% coverage: 6:240/251 of query aligns to 5:246/253 of 6f7hC

query
sites
6f7hC

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Q

binding glycerol: I55 (= I57), N199 (= N194)

P37451 Propanediol uptake facilitator PduF from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
34% identity, 98% coverage: 5:250/251 of query aligns to 4:263/264 of P37451

query
sites
P37451

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K

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N

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Q

E

NPA 66:68 (= NPA 68:70) NPA 1
NPA 201:203 (= NPA 194:196) NPA 2

I1CR68 Aquaporin-1 from Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar) (see paper)
36% identity, 91% coverage: 8:235/251 of query aligns to 59:292/306 of I1CR68

query
sites
I1CR68

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A

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x
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G

A

P

P

I

I

I

L

G

G

P

L

L

V

G

G

H275 (≠ E217) mutation to A: Affects pH sensing; when associated with A-85.

8c9hA Aqp7_inhibitor
38% identity, 92% coverage: 8:239/251 of query aligns to 10:247/253 of 8c9hA

query
sites
8c9hA

K

R

E

E

M

F

L

L

S

A

E

E

F

F

M

M

G

S

T

T

M

Y

V

V

L

M

I

M

I

V

F

F

G

G

A

L

G

G

N

S

V

V

A

A

M

H

T

M

V

V

L

L

F

N

G

K

K

K

T

Y

L

G

N

S

I

Y

T

L

W

G

D

V

N

N

I

L

T

G

F
|
F

G

G

W

F

G

G

L

-

A

-

V

V

L

T

L

M

G

G

I

V

-

H

M

V

A

A

G

G

L

R

P

I

S

S

G

G

A
|
A

H
|
H

I

M

N

N

P

A

A

A

V

V

S

T

L

F

A

A

L

N

A

C

A

A

T

L

G

G

R

R

F

V

P

P

W

W

R

R

K

K

V

F

L

P

P

V

Y

Y

S

V

V

L

A

G

Q

Q

V

F

A

L

G

G

G

S

F

F

A

L

G

A

A

A

I

T

V

I

F

Y

-

S

-

L

-

F

-

Y

-

T

-

A

-

I

L

L

D

H

F

F

K

S

A

G

K

G

W

Q

L

L

G

M

V

V

D

T

P

G

Q

P

L

V

A

A

S

-

T

T

A

A

G

G

I

I

F

F

C

A

T

T

F

Y

P

L

A

P

I

D

T

H

T

M

S

T

Y

L

L

W

P

R

G

G

F

F

I

L

D

N

Q

E

I

A

I

W

G

L

T

T

A

G

V

M

L
|
L

M
x
Q

F

L

G

C

I

L

L
x
F

A

A

I

I

G

T

D

D

F

Q

A

E

G

N

K

N

N

P

N

A

V

L

G

P

W

G

M

T

G

E

P

A

V

L

L

V

V
x
I

A

G

A

I

L

L

I

V

V

V

A

I

I

I

G

G

M

V

S

S

L

L

G

G

A

M

M

N

H

T

G

G

Y

Y

A

A

I

I

N

N

P

P

A

S

R

R

D

D

F

L

G

P

P

P

R

R

F

I

F

F

A

T

L

F

V

I

A

A

G

G

F

W

T

G

Q

K

P

Q

N

V

L

F

M

S

E

N

-

G

P

E

G

N

I

W

V

W

L

W

V

V

P

P

I

V

V

V

G

A

P

P

I

L

G

G

G

A

P

Y

L

L

G

G

A

G

F

I

I

I

Y

Y

binding ethyl 4-[(4-pyrazol-1-ylphenyl)methylcarbamoylamino]benzoate: F49 (= F47), A66 (= A65), H67 (= H66), L157 (= L150), Q158 (≠ M151), F162 (≠ L155), I181 (≠ V174)

O14520 Aquaporin-7; AQP-7; Aquaglyceroporin-7; Aquaporin adipose; AQPap; Aquaporin-7-like from Homo sapiens (Human) (see 4 papers)
38% identity, 92% coverage: 8:239/251 of query aligns to 35:272/342 of O14520

query
sites
O14520

K

R

E

E

M

F

L

L

S

A

E

E

F

F

M

M

G

S

T

T

M

Y

V

V

L

M

I

M

I

V

F

F

G

G

A

L

G

G

N

S

V

V

A

A

M

H

T

M

V
|
V

L

L

F

N

G

K

K

K

T

Y

L

G

N

S

I

Y

T

L

W

G

D

V

N

N

I

L

T

G

F

F

G

G

W

F

G

G

L

-

A

-

V

V

L

T

L

M

G

G

I

V

-

H

M

V

A

A

G

G

L

R

P

I

S

S

G

G

A

A

H

H

I

M

N

N

P

A

A

A

V

V

S

T

L

F

A

A

L

N

A

C

A

A

T

L

G

G

R

R

F

V

P

P

W

W

R

R

K

K

V

F

L

P

P

V

Y

Y

S

V

V

L

A

G

Q

Q

V

F

A

L

G

G

G

S

F

F

A

L

G

A

A

A

I

T

V

I

F

Y

-

S

-

L

-

F

-
x
Y

-

T

-

A

-

I

L

L

D

H

F

F

K

S

A

G

K

G

W

Q

L

L

G

M

V

V

D

T

P

G

Q

P

L

V

A

A

S

-

T

T

A

A

G

G

I

I

F

F

C

A

T

T

F

Y

P

L

A

P

I

D

T
x
H

T

M

S

T

Y

L

L

W

P

R

G

G

F

F

I

L

D

N

Q

E

I

A

I

W

G

L

T

T

A

G

V

M

L

L

M

Q

F

L

G

C

I

L

L

F

A

A

I

I

G

T

D

D

F

Q

A

E

G

N

K

N

N

P

N

A

V

L

G

P

W

G

M

T

G

E

P

A

V

L

L

V

V

I

A

G

A

I

L

L

I

V

V

V

A

I

I

I

G

G

M

V

S

S

L

L

G

G

A

M

M

N

H

T

G

G

Y

Y

A

A

I

I

N

N

P

P

A

S

R

R

D

D

F

L

G

P

P

P

R

R

F

I

F

F

A

T

L

F

V

I

A

A

G

G

F

W

T

G

Q

K

P

Q

N

V

L

F

M

S

E

N

-

G

P

E

G

N

I

W

V

W

L

W

V

V

P

P

I

V

V

V

G

A

P

P

I

L

G
|
G

G

A

P

Y

L

L

G

G

A

G

F

I

I

I

Y

Y

V59 (= V32) to L: in dbSNP:rs4008659
Y135 (vs. gap) Important for permeability to glycerol; mutation to A: Strongly decreased permeability to glycerol. Mildly decreased water permeability.
H165 (≠ T133) mutation to A: Decreased permeability to glycerol. Mildly decreased water permeability.
G264 (= G231) to V: affects water and glycerol transport; dbSNP:rs62542743

Sites not aligning to the query:

1:32 mutation Missing: Decreased interaction with PLIN1.
12 R → C: in dbSNP:rs139297434

6n1gA Crystal structure of aquaglyceroporin aqp7 (see paper)
38% identity, 92% coverage: 8:239/251 of query aligns to 4:241/249 of 6n1gA

query
sites
6n1gA

K

R

E

E

M

F

L

L

S

A

E

E

F

F

M

M

G

S

T

T

M

Y

V

V

L

M

I

M

I

V

F

F

G

G

A

L

G

G

N

S

V

V

A

A

M

H

T

M

V

V

L

L

F

N

G

K

K

K

T

Y

L

G

N

S

I

Y

T

L

W

G

D

V

N

N

I

L

T

G

F

F

G

G

W

F

G

G

L

-

A

-

V

V

L

T

L

M

G

G

I

V

-

H

M

V

A

A

G

G

L

R

P

I

S

S

G

G

A

A

H

H

I

M

N

N

P

A

A

A

V

V

S

T

L

F

A

A

L

N

A

C

A

A

T
x
L

G

G

R
|
R

F

V

P

P

W

W

R

R

K

K

V

F

L

P

P

V

Y

Y

S

V

V

L

A

G

Q

Q

V

F

A

L

G

G

G

S

F

F

A

L

G

A

A

A

I

T

V

I

F

Y

-

S

-

L

-

F

-

Y

-

T

-

A

-

I

L

L

D

H

F

F

K

S

A

G

K

G

W

Q

L

L

G

M

V

V

D

T

P

G

Q

P

L

V

A

A

S

-

T

T

A

A

G

G

I

I

F

F

C

A

T

T

F

Y

P

L

A

P

I

D

T

H

T

M

S

T

Y

L

L

W

P

R

G

G

F

F

I

L

D

N

Q

E

I

A

I

W

G

L

T

T

A

G

V

M

L

L

M

Q

F

L

G

C

I

L

L

F

A

A

I

I

G

T

D

D

F

Q

A

E

G

N

K

N

N

P

N

A

V

L

G

P

W

G

M

T

G

E

P

A

V

L

L

V

V

I

A

G

A

I

L

L

I

V

V

V

A

I

I

I

G

G

M

V

S

S

L

L

G

G

A

M

M

N

H

T

G

G

Y

Y

A

A

I

I

N

N

P

P

A

S

R

R

D

D

F

L

G

P

P

P

R

R

F

I

F

F

A

T

L

F

V

I

A

A

G

G

F

W

T

G

Q

K

P

Q

N

V

L

F

M

S

E

N

-

G

P

E

G

N

I

W

V

W

L

W

V

V

P

P

I

V

V

V

G

A

P

P

I

L

G

G

G

A

P

Y

L

L

G

G

A

G

F

I

I

I

Y

Y

binding glycerol: L73 (≠ T78), R75 (= R80)

3c02A X-ray structure of the aquaglyceroporin from plasmodium falciparum (see paper)
33% identity, 93% coverage: 8:240/251 of query aligns to 4:232/242 of 3c02A

query
sites
3c02A

K

R

E

E

M

F

L

I

S

G

E

E

F

F

M

L

G

G

T

T

M

F

V

V

L

L

I

M

I

F

F

L

G

G

A

E

G

G

N

A

V

T

A

A

M

N

T

F

V

H

L

T

F

T

G

G

K

-

T

-

L

L

N

S

I

G

T

D

W

W

D

Y

N

K

I

L

T

C

F

L

G

G

W
|
W

G

G

L

L

A

A

V

V

L

F

G

G

I

I

M

L

A

V

G

S

L

A

P

K

-

L

S

S

G

G

A

A

H

H

I

L

N

N

P

L

A

A

V

V

S

S

L

I

A

G

L

L

A

S

T

I

G

N

R

K

F

F

P

D

W

L

R

K

K

K

V

I

L

P

P

V

Y

Y

S

F

V

F

A

A

Q

Q

V

L

A

L

G

G

G

A

F

F

A

V

G

G

A

T

A

S

I

T

V

V

F

Y

L

G

D

L

F

Y

K

H

A

G

K

F

W

I

L

S

G

N

V

S

D

K

-

I

P

P

Q

Q

L

F

A

A

S

W

T

E

A

T

G

S

I

-

F

-

C

-

T

R

F

N

P

P

A

S

I

I

T

S

T

L

S

T

Y

-

L

-

P

G

G

A

F

F

I

F

D

N

Q

E

I

L

I

I

G

L

T

T

A

G

V

I

L

L

M

L

F

L

G

V

I

I

L

L

A

V

I

V

G

V

D

D

-

E

-

N

F

I

A

C

G

G

K

K

N

F

N

H

V

I

G

L

W

K

M

L

G

S

P

S

V

V

L

-

V

V

A

G

A

L

L

I

I

I

V

L

A

C

I

I

G

G

M

I

S

T

L

F

G

G

A

G

M

N

H

T

G
|
G

Y
x
F

A

A

I

L

N

N

P

P

A

S

R
|
R

D

D

F

L

G

G

P

S

R

R

F

F

F

L

A

S

L

L

V

I

A

A

-

Y

-

G

-

K

-

D

G

T

F

F

T

T

Q

K

P

D

N

N

L

F

M

Y

E

-

P

-

G

-

I

-

V

F

L

W

V

V

P

P

I

L

V

V

G

A

P

P

I

C

I

V

G

G

G

S

P

V

L

V

G

F

A

C

F

Q

I

F

Y

Y

D

D

binding glycerol: W43 (= W49), G182 (= G190), F183 (≠ Y191), R189 (= R197)

2evuA Crystal structure of aquaporin aqpm at 2.3a resolution (see paper)
32% identity, 96% coverage: 4:243/251 of query aligns to 2:244/245 of 2evuA

query
sites
2evuA

I

V

S

S

L

L

G

T

K

K

E

R

M

C

L

I

S

A

E

E

F

F

M

I

G

G

T

T

M

F

V

I

L

L

I

V

I

F

F

F

G

G

A

A

G

G

N

S

V

A

A

A

M

V

T

T

V

L

L

M

F

I

-

A

-

S

-

G

G

G

K

T

T

S

L

P

N

N

-

P

-

F

-

N

-
x
I

-

G

-

I

-

G

-

L

-

G

-

L

I

G

T

D

W
|
W

D

V

N

A

I

I

T

G

F

L

G

A

W

F

G

G

L

F

A

A

V
x
I

L

A

G

S

I

I

M

Y

A

A

-

L

G

G

L

N

P

I

S

S

G

G

A

C

H

H

I
|
I

N
|
N

P

P

A

A

V

V

S

T

L

I

A

G

L

L

A

W

A

S

T

V

G

K

R

K

F

F

P

P

W

G

R

R

K

E

V

V

L

V

P

P

Y

Y

S

I

V

I

A

A

Q

Q

V

L

A

L

G

G

G

A

F

A

A

F

G

G

A

S

A

-

I

-

V

-

F

F

L

I

D

F

F

L

K

Q

A

C

K

A

W

G

L

I

G

G

V

A

D

-

P

-

Q

-

L

-

A

A

S

T

T

V

A

G

G

G

I

L

F
x
G

C
x
A

T

T

F
x
A

P
|
P

A
x
F

I

P

T

G

T

I

S

S

Y

Y

L

W

P

Q

G

A

F

M

I

L

D

A

Q

E

I

V

G

G

T

T

A

F

V

L

L

L

M

M

F

I

G

T

I

I

L

M

-

G

-

I

A

A

I

V

G

D

D

E

F

R

A

A

G

P

K

K

N

G

N

F

V

A

G

G

W

I

M

I

G

I

P

G

V

L

L

T

V

V

A

A

A

G

L

I

I

I

V

T

A

-

I

-

G

-

M

-

S

T

L

L

G

G

A

N

M

I

H

S

G

G

Y

S

A

S

I

L

N

N

P

P

A

A

R

R

D

T

F

F

G

G

P

P

R

Y

F

L

F

N

A

D

L

M

V

I

-

F

A

A

G

G

F

T

T

D

Q

L

P

W

N

N

L

Y

M

Y

E

S

P

-

G

-

I

-

V

-

L

-

V

I

P

Y

I

V

V

I

G

G

P

P

I

I

I

V

G

G

G

A

P

V

L

L

G

A

A

A

F

L

I

T

Y

Y

D

Q

W

Y

T

L

T

T

binding glycerol: I44 (vs. gap), W55 (= W42), I66 (≠ V53), I81 (= I67), N82 (= N68), G133 (≠ F126), A134 (≠ C127), A136 (≠ F129), P137 (= P130), F138 (≠ A131)

P08995 Nodulin-26; N-26 from Glycine max (Soybean) (Glycine hispida) (see paper)
30% identity, 93% coverage: 8:240/251 of query aligns to 38:245/271 of P08995

query
sites
P08995

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N

Sites not aligning to the query:

262 modified: Phosphoserine; by CPK

Q92R43 Aquaglyceroporin AqpS from Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) (see paper)
39% identity, 43% coverage: 1:109/251 of query aligns to 1:110/233 of Q92R43

query
sites
Q92R43

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T49 (≠ F47) mutation T->F,W: Increases uptake of both methylarsenite and methylarsenate and exhibits higher sensitivity to methylarsenite.

Sites not aligning to the query:

177 V→I: Decreases methylarsenite transport activity and results in higher resistance to methylarsenite. Slight decrease in methylarsenate transport activity.; V→R: Increases methylarsenite transport activity, leading to lower resistance to methylarsenite. Nearly complete loss of methylarsenate transport activity.

P09011 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Rattus norvegicus (Rat) (see 2 papers)
28% identity, 96% coverage: 1:241/251 of query aligns to 2:219/261 of P09011

query
sites
P09011

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Sites not aligning to the query:

233 modified: Phosphoserine
244 N→D: No effects.

P55088 Aquaporin-4; AQP-4; Mercurial-insensitive water channel; MIWC; WCH4 from Mus musculus (Mouse) (see 2 papers)
28% identity, 92% coverage: 8:239/251 of query aligns to 36:252/323 of P55088

query
sites
P55088

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F

S111 (≠ P82) modified: Phosphoserine; by PKG; mutation to A: Loss of phosphorylation by PKG (in vitro). No effect on location at cell membrane.

Sites not aligning to the query:

4 natural variant: G -> R

P30301 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Homo sapiens (Human) (see 10 papers)
28% identity, 96% coverage: 1:241/251 of query aligns to 4:221/263 of P30301

query
sites
P30301

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x
E

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x
G

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Y

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N

-

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-

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x
Y

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x
W

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V

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G

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x
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F

R33 (≠ M30) to C: in CTRCT15; reduces cell-to-cell adhesion, reduces cell-to-cell gap junction coupling, no loss of cell membrane localization, no loss of water channel activity; dbSNP:rs864309693
V107 (≠ D107) to I: in CTRCT15; likely benign; dbSNP:rs74641138
E134 (≠ Q143) to G: in CTRCT15; non-progressive lamellar cataract; loss of activity; dbSNP:rs121917869
T138 (= T147) to R: in CTRCT15; progressive polymorphic and lamellar cataract; loss of activity; dbSNP:rs121917867
D150 (= D159) to H: in CTRCT15; loss of plasma membrane expression; dbSNP:rs778327521
G165 (≠ A180) to D: in CTRCT15; uncertain significance; loss of plasma membrane expression
Y177 (vs. gap) to C: in CTRCT15; uncertain significance

Sites not aligning to the query:

204:263 natural variant: Missing (in CTRCT15; uncertain significance)
211:263 natural variant: Missing (in CTRCT15; uncertain significance)
235 modified: Phosphoserine
246 modified: Deamidated asparagine; by deterioration
259 modified: Deamidated asparagine; by deterioration

P06624 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Bos taurus (Bovine) (see 4 papers)
28% identity, 96% coverage: 1:241/251 of query aligns to 4:221/263 of P06624

query
sites
P06624

M

L

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R

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S

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G

G

A

A

I

V

V

L

F

Y

L

S

D

V

F

-

K

-

A

-

K

-

W

-

L

-

G

-

V

T

D

P

P

P

Q

A

L

V

A

R

S

G

T

N

A

L

G

A

I

L

F

N

C

T

T

L

F

H

P

P

A

G

I

V

T

S

T

V

S

G

Y

-

L

-

P

Q

G

A

F

T

I

I

D

V

Q

E

I

I

I

F

G

L

T

T

A

L

V

Q

L

F

M

V

F

L

G

C

I

I

L

F

A

A

I

T

G
x
Y

D

D

F

-

A

-

G

-

K

E

N

R

V

N

G

G

W

R

M

L

G

G

P

S

V

V

L

-

V

-

A

-

A

A

L

L

I

A

V

V

A

G

I

F

G

S

M

L

S

T

L

L

G

G

A

H

M

L

H

F

G

G

Y

M

-

Y

-

T

-

G

-

A

A

G

I

M

N

N

P

P

A

A

R

R

D

S

F

F

G

A

P

P

R

A

F

I

F

-

A

-

L

L

V

T

A

R

G

N

F

F

T

T

Q

N

P

H

N

-

L

-

M

-

E

-

P

-

G

-

I

-

V

-

L

W

V

V

P

Y

I

W

V

V

G

G

P

P

I

V

I

I

G

G

G

A

P

G

L

L

G

G

A

S

F

L

I

L

Y

Y

D

D

W

F

Y149 (≠ G158) mutation to G: Increases constitutive water permeability. Abolishes regulation by cytoplasmic calcium levels.; mutation to L: Strongly decreases water permeability. Abolishes regulation by cytoplasmic calcium levels.; mutation to S: Slightly decreases water permeability, but has a minor effect on the regulation by cytoplasmic calcium levels.

Sites not aligning to the query:

227 L→A: Strongly reduced CALM binding.
227:237 Interaction with CALM
230 V→A: Strongly reduced CALM binding.
235 modified: Phosphoserine
243 modified: Phosphoserine; by PKA
245 modified: Phosphoserine
246 Interaction with BFSP1; modified: Deamidated asparagine
250 interaction with BFSP1

P55064 Aquaporin-5; AQP-5 from Homo sapiens (Human) (see 2 papers)
31% identity, 92% coverage: 8:239/251 of query aligns to 12:221/265 of P55064

query
sites
P55064

K

K

E

A

M

V

L

F

S

A

E

E

F

F

M

L

G

A

T

T

M

L

V

I

L

F

I

V

I

F

F

F

G

G

A

L

G

G

N

-

V

-

A

-

M

-

T

S

V

A

L

L

F

K

G

W

K

P

T

S

L
x
A

N

L

I

P

T

T

W

I

D

L

N

Q

I
|
I

T

A

F

L

G

A

W

F

G

G

L

L

A

A

V

I

-

G

L

T

L

L

G

A

I

Q

M

A

A

L

G

G

L

P

P

V

S

S

G

G

A

G

H

H

I

I

N

N

P

P

A

A

V

I

S

T

L

L

A

A

L

L

A

L

A

V

T

G

G

N

R

Q

F

I

P

S

W

L

R

L

K

R

V

A

L

F

P

F

Y

Y

S

V

V

A

A

A

Q

Q

V

L

A

V

G

G

G

A

F

I

A

A

G

G

A

A

A

G

I

I

V

L

F

Y

L

-

D

-

F

-

K

-

A

-

K

-

W

-

L

-

G

G

V

V

D

A

P

P

Q

-

L

L

A

N

S

A

T

R

A

G

G

N

I

L

F

A

C

V

T

N

F

A

P

L

A
x
N

I

N

T

N

T

T

S

T

Y

Q

L

G

P

Q

G

A

F

M

I

V

D

V

Q

E

I

L

I

I

G

L

T

T

A

F

V

Q

L

L

M

A

F

L

G

C

I

I

L

F

A

A

I

S

G

T

D

D

F

S

A

R

G

R

K

T

N
x
S

N

P

V

V

G

G

W

-

M

-

G

S

P

P

V

A

L

L

V

S

A

I

A

G

L

L

I

S

V

V

A

T

I

L

G

G

M

H

S

L

L

V

G

G

-
x
I

A

Y

M

F

H

T

G

G

Y

C

A

S

I

M

N

N

P

P

A

A

R
|
R

D

S

F

F

G

G

P

P

R

-

F

-

A

A

L

V

V

V

A

M

G

N

F

R

T

F

Q

S

P

P

N

A

L

H

M

W

E

-

P

-

G

-

I

-

V

-

L

-

V

V

P

F

I

W

V

V

G

G

P

P

I

I

I

V

G

G

G

A

P

V

L

L

G

A

A

A

F

I

I

L

Y

Y

A38 (≠ L38) to E: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123054
I45 (= I45) to S: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123055
N123 (≠ A131) to D: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123057
S156 (≠ N164) mutation to A: No effect on location at the cell membrane.; mutation to E: Increased location at the cell membrane.
I177 (vs. gap) to F: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123056
R188 (= R197) to C: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs368292687

P47863 Aquaporin-4; AQP-4; Mercurial-insensitive water channel; MIWC; WCH4 from Rattus norvegicus (Rat) (see 4 papers)
27% identity, 93% coverage: 8:241/251 of query aligns to 36:250/323 of P47863

query
sites
P47863

K

K

E

A

M

V

L

T

S

A

E

E

F

F

M

L

G

A

T

M

M

L

V

I

L

F

I

V

I

L

F

L

G

S

A

V

G

G

N

S

V

-

A

-

M

-

T

T

V

I

L

N

F

W

G

G

K

G

T

S

L

E

N

N

-

P

-

L

-

P

-

V

-

D

I

M

T

V

W

L

D

I

N

S

I

L

T

C

F

F

G

G

W

L

G

S

L

I

A

A

V

T

L

M

L

V

G

Q

I

C

M

F

A

-

G

G

L

H

P

I

S

S

G

G

A

G

H

H

I

I

N

N

P

P

A

A

V

V

S

T

L

V

A

A

L

M

A

V

A

C

T

T

G

R

R

K

F

I

P

S

W

I

R

A

K

K

V

S

L

V

P

F

Y

Y

S

I

V

T

A

A

Q

Q

V

C

A

L

G

G

G

A

F

I

A

I

G

G

A

A

A

G

I

I

V

L

F

Y

L

L

D

V

F

-

K

-

A

-

K

-

W

-

L

-

G

-

V

T

D

P

P

P

Q

S

L

V

A

V

S

G

T

G

A

L

G

G

I

V

F

T

C

T

T

V

F

H

P

G

A

N

I

L

T

T

T

A

S

G

Y

H

L

-

P

-

G

G

F

L

I

L

D

V

Q

E

I

L

I

I

G

I

T

T

A

F

V

Q

L

L

M

V

F

F

G

T

I

I

L

F

A

A

I

S

G

C

D

D

F
x
S

A

K

G

R

K

T

N

D

N

V

V

T

G

G

W

-

M

-

G

-

P

-

V

-

L

-

V

-

A

-

A

S

L

V

I

A

V

L

A

A

I

I

G

G

M

F

S

S

L

V

G

A

A

I

M

G

H
|
H

G

L

Y

F

A

A

I

I

-

N

-

Y

-

T

-

G

-

A

-

S

-

M

N

N

P

P

A

A

R

R

D

S

F

F

G

G

P

P

R

-

F

-

A

A

L

V

V

I

A

M

G

G

F

N

T

W

Q

E

P

N

N

H

L

-

M

-

E

-

P

-

G

-

I

-

V

-

L

W

V

I

P

Y

I

W

V

V

G

G

P

P

I

I

G

G

G

A

P

V

L

L

G

A

A

G

F

A

I

L

Y

Y

D

E

W

Y

S180 (≠ F160) modified: Phosphoserine; by PKC; mutation to A: Decreases internalization from the cell membrane in response to PKC activation.
H201 (= H189) mutation to P: Partial loss of transport activity.

Sites not aligning to the query:

13 modified: S-palmitoyl cysteine; C→A: Reduced palmitoylation. Loss of palmitoylation; when associated with A-17.
17 modified: S-palmitoyl cysteine; C→A: Reduced palmitoylation. Loss of palmitoylation; when associated with A-13.
285 modified: Phosphoserine

Query Sequence

>208652 MicrobesOnline__882:208652
MKEISLGKEMLSEFMGTMVLIIFGAGNVAMTVLFGKTLNITWDNITFGWGLAVLLGIMAG
LPSGAHINPAVSLALAATGRFPWRKVLPYSVAQVAGGFAGAAIVFLDFKAKWLGVDPQLA
STAGIFCTFPAITTSYLPGFIDQIIGTAVLMFGILAIGDFAGKNNVGWMGPVLVAALIVA
IGMSLGAMHGYAINPARDFGPRFFALVAGFTQPNLMEPGIVLVPIVGPIIGGPLGAFIYD
WTTGAVNKAQG

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory