SitesBLAST

HLN 66:68 (= HLN 64:66) binding
Y138 (= Y136) binding
GFA 199:201 (= GFA 197:199) binding
N203 (= N201) binding
R206 (= R204) binding
PL 236:237 (≠ PI 234:235) mutation to FW: No detectable water or glycerol permeability.

1fx8A Crystal structure of the e. Coli glycerol facilitator (glpf) with substrate glycerol (see paper)
69% identity, 95% coverage: 4:257/266 of query aligns to 1:254/254 of 1fx8A

query
sites
1fx8A

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L

binding glycerol: W43 (= W46), N63 (= N66), G194 (= G197), F195 (= F198), A196 (= A199), N198 (= N201), R201 (= R204)

O14520 Aquaporin-7; AQP-7; Aquaglyceroporin-7; Aquaporin adipose; AQPap; Aquaporin-7-like from Homo sapiens (Human) (see 4 papers)
35% identity, 100% coverage: 1:266/266 of query aligns to 29:289/342 of O14520

query
sites
O14520

M
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x
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x
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D

V59 (vs. gap) to L: in dbSNP:rs4008659
Y135 (≠ S107) Important for permeability to glycerol; mutation to A: Strongly decreased permeability to glycerol. Mildly decreased water permeability.
H165 (≠ S140) mutation to A: Decreased permeability to glycerol. Mildly decreased water permeability.
G264 (= G241) 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

Q96PS8 Aquaporin-10; AQP-10; Aquaglyceroporin-10; Small intestine aquaporin from Homo sapiens (Human) (see 2 papers)
36% identity, 98% coverage: 5:266/266 of query aligns to 20:277/301 of Q96PS8

query
sites
Q96PS8

L

L

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E

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D

E27 (= E12) mutation to Q: Abolishes permeability to glycerol.
G73 (≠ T57) mutation to A: Increased permeability to glycerol at acidic pH.; mutation to F: Abolishes permeability to glycerol.
S77 (= S61) mutation S->A,D: Nearly abolishes permeability to glycerol.
H80 (= H64) mutation to A: Abolishes permeability to glycerol.
F85 (≠ V69) mutation to A: Nearly abolishes permeability to glycerol.
R94 (≠ C78) mutation to A: Abolishes permeability to glycerol.
N133 (≠ H117) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to Q: Abolishes N-glycosylation.

6f7hC Crystal structure of human aqp10 (see paper)
37% identity, 94% coverage: 5:253/266 of query aligns to 5:249/253 of 6f7hC

query
sites
6f7hC

L

L

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Y

Y

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A

A

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M

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M

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A

A

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L

D

D

D

R

G

R

N

N

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K

G

G

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A

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L

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A

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N

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C

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I

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M

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N
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N

P

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A

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R

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D

F

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R

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F

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A

A

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D

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W

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W

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A

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G

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Y

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Y

L

L

L

I

V

binding glycerol: I55 (≠ V54), N199 (= N201)

8c9hA Aqp7_inhibitor
34% identity, 96% coverage: 1:255/266 of query aligns to 4:253/253 of 8c9hA

query
sites
8c9hA

M

L

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Q

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M

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K

A

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G

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G

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N

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x
F

G

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A

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x
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H
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H

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M

N

N

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A

A

A

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F

A

A

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Y

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Q

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F

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F

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G

A

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L

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A

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F

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H

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Q

-

L

-

A

A

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I

I

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F

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Y

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A

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W

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L

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x
Q

G

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C

I

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M
x
F

A

A

L

I

T

T

D

D

D

Q

G

E

N

N

G

N

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I
|
I

G

G

L

I

L

L

V

V

A

V

V

I

I

I

G

G

A

V

S

S

T

L

G

G

P

M

L

N

T

T

G

G

F

Y

A

A

M

I

N

N

P

P

A

S

R

R

D

D

F

L

G

P

P

P

K

R

L

I

F

F

T

T

W

F

M

I

A

A

G

G

W

W

G

G

D

K

I

Q

A

V

M

F

T

S

G

N

G

G

R

E

D

N

I

-

P

-

Y

W

F

W

I

W

V

V

P

P

I

V

A

A

P

P

L

L

I

L

G

G

A

A

C

Y

L

L

G

G

A

G

A

I

I

I

Y

Y

R

L

Y

V

L

F

I

I

G

G

N

S

binding ethyl 4-[(4-pyrazol-1-ylphenyl)methylcarbamoylamino]benzoate: F49 (≠ W46), A66 (≠ G63), H67 (= H64), L157 (= L157), Q158 (≠ M158), F162 (≠ M162), I181 (= I181)

6n1gA Crystal structure of aquaglyceroporin aqp7 (see paper)
35% identity, 95% coverage: 4:257/266 of query aligns to 1:249/249 of 6n1gA

query
sites
6n1gA

S

K

L

M

K

V

A

R

Q

E

C

F

T

L

A

A

E

E

F

F

L

M

G

S

T

T

G

Y

L

V

F

M

L

M

F

V

F

F

G

G

I

L

G

G

C

S

L

V

S

A

A

H

L

M

-

V

-

L

-

N

K

K

V

K

A

Y

G

G

A

S

S

Y

L

L

G

G

L

-

W

-

E

-

I

V

C

N

I

L

I

G

W

F

G

G

L

F

G

G

I

V

S

T

L

M

A

G

V

V

Y

H

L

V

T

A

S

G

G

R

I

I

S

S

G

G

G

A

H

H

L

M

N

N

P

A

A

A

V

V

T

T

V

F

A

A

L

N

W

C

L

A

F
x
L

A

G

C
x
R

F

V

P

P

G

W

R

R

K

K

V

F

F

P

P

V

Y

Y

I

V

V

L

S

G

Q

Q

V

F

A

L

G

G

A

S

F

F

G

L

G

A

A

A

V

A

L

T

A

I

Y

Y

V

S

L

L

Y

F

S

Y

T

T

M

A

F

I

T

L

E

H

F

F

E

S

S

G

A

G

H

Q

H

L

I

M

A

V

R

T

G

G

S

P

V

V

E

A

S

T

L

-

Q

-

L

-

A

A

S

G

I

I

F

F

S

A

T

T

Y

Y

P

L

A

P

A

D

S

H

L

M

S

T

I

L

W

W

H

R

A

G

A

F

L

L

V

N

E

E

V

A

V

W

I

L

T

T

S

G

M

M

L

L

M

Q

G

L

M

C

I

L

M

F

A

A

L

I

T

T

D

D

D

Q

G

E

N

N

G

N

V

P

P

A

K

L

G

P

P

G

L

T

A

E

P

A

L

L

L

V

I

I

G

G

L

I

L

L

V

V

A

V

V

I

I

I

G

G

A

V

S

S

T

L

G

G

P

M

L

N

T

T

G

G

F

Y

A

A

M

I

N

N

P

P

A

S

R

R

D

D

F

L

G

P

P

P

K

R

L

I

F

F

T

T

W

F

M

I

A

A

G

G

W

W

G

G

D

K

I

Q

A

V

M

F

T

S

G

N

G

G

R

E

D

N

I

-

P

-

Y

W

F

W

I

W

V

V

P

P

I

V

A

A

P

P

L

L

I

L

G

G

A

A

C

Y

L

L

G

G

A

G

A

I

I

I

Y

Y

R

L

Y

V

L

F

I

I

G

G

N

S

N

T

L

I

binding glycerol: L73 (≠ F76), R75 (≠ C78)

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)
35% identity, 88% coverage: 11:245/266 of query aligns to 63:292/306 of I1CR68

query
sites
I1CR68

A

A

E

E

F

F

L

I

G

G

T

T

G

V

L

I

F

L

L

V

F

L

G

T

I

C

G

G

C

F

L

C

S

A

A

E

L

Q

K

T

V

L

A

H

G

I

A

E

S

E

L

S

G

K

L

S

W

W

E

L

I

T

C

S

I

S

I

F

-

G

W

S

G

G

L

L

G

S

I

V

S

L

L

I

A

G

V

I

Y

C

L

V

T

S

S

G

G

H

I

V

S

S

G

G

G

A

H

H

L

L

N

N

P

P

A

A

V

V

T

T

V

I

A

A

L

F

W

C

L

I

F

F

A

S

C

G

F

F

P

P

G

I

R

R

K

K

V

V

F

P

P

S

Y

Y

I

I

V

T

S

A

Q

Q

V

L

A

L

G

G

A

A

F

F

G

A

G

G

A

A

V

A

L

L

A

L

Y

Y

V

I

L

I

Y

I

S

E

T

P

M

A

F

I

T

V

E

Q

F

F

E

D

S

G

A

G

H

Q

H

R

I

Y

A

I

R

L

G

G

S

E

V

K

E

S

S

T

L

-

Q

-

L

-

A

A

S

G

I

I

F

F

S

G

T

T

Y

Y

P

P

A

P

A

L

S

Y

L

V

S

G

I

I

W

G

H

S

A

A

A

I

L

A

V

S

E

E

V

I

V

M

I

G

T

T

S

A

M

M

L

L

M

L

G

L

M

V

I

I

M

M

A

-

L

V

T

T

D

G

D

H

G

P

N

N

G

N

V

L

P

P

K

Y

G

K

P

S

L

A

A

Q

P

G

L

A

L

M

I

I

G

A

L

L

L

G

V

I

A

T

V

T

I

I

G

S

A

L

S

C

T

I

G

G

P

Y

L

T

T

S

G

G

F

F

A

S

M

L

N

N

P

P

A

A

R

R

D

D

F

F

G

G

P

P

K

R

L

L

F

F

T

T

W

A

M

I

A

A

G

G

W

W

G

G

-

F

D

D

I

V

A

F

M

K

T

V

G

Y

G
x
H

R

Y

D

-

I

-

P

-

Y

Y

F

A

I

L

V

V

P

P

I

M

I

F

A

A

P

P

L

I

I

L

G

G

A

G

C

L

L

V

G

G

H275 (≠ G225) mutation to A: Affects pH sensing; when associated with A-85.

2evuA Crystal structure of aquaporin aqpm at 2.3a resolution (see paper)
36% identity, 94% coverage: 4:252/266 of query aligns to 3:243/245 of 2evuA

query
sites
2evuA

S

S

L

L

K

T

A

K

Q

R

C

C

T

I

A

A

E

E

F

F

L

I

G

G

T

T

G

F

L

I

F

L

L

V

F

F

G

G

I

A

G

G

C

S

L

-

S

A

A

A

L

V

K

T

V

L

A

M

G

I

A

A

S

S

L

G

G

G

L

T

-

S

-

P

-

N

-

P

-

F

-

N

-
x
I

-

G

-

I

-

G

-

L

-

G

-

L

-

G

-

D

W
|
W

-

V

E

A

I

I

C

G

I

L

I

A

W

F

G

G

L

F

G

A

I
|
I

S

A

L

A

A

S

V

I

Y

Y

L

A

T

L

S

G

G

N

I

I

S

S

G

G

G

C

H

H

L
x
I

N
|
N

P

P

A

A

V

V

T

T

V

I

A

G

L

L

W

W

L

S

F

V

A

K

C

K

F

F

P

P

G

G

R

R

K

E

V

V

F

V

P

P

Y

Y

I

I

V

I

S

A

Q

Q

V

L

A

L

G

G

A

A

F

A

G

F

G

G

A

S

V

F

L

I

A

-

Y

-

V

-

L

-

Y

-

S

-

T

-

M

-

F

-

T

-

E

-

F

F

E

L

S

Q

A

C

H

A

H

G

I

I

A

G

R

A

G

A

S

T

V

V

E

G

S

G

L

L

Q
x
G

L

-

A

-

S

-

I

-

F

-

S
x
A

T

T

Y
x
A

P
|
P

A
x
F

A

P

S

G

L

I

S

S

I

Y

W

W

H

Q

A

A

A

M

L

L

V

A

E

E

V

V

I

G

T

T

S

F

M

L

L

L

M

M

G

I

M

T

I

I

M

M

A

G

L

I

T

A

D

V

D

D

G

E

N

R

G

-

V

A

P

P

K

K

G

G

P

-

L

F

A

A

P

G

L

I

I

I

G

G

L

L

L

T

V

V

A

A

V

G

I

I

G

I

A

T

S

T

T

L

G

G

P

N

L

I

T

S

G

G

F

S

A

S

M

L

N

N

P

P

A

A

R

R

D

T

F

F

G

G

P

P

K

Y

L

L

F

-

T

-

W

-

M

-

A

-

G

-

W

-

G

N

D

D

I

M

A

I

M

F

T

A

G

G

G

T

R

D

D

L

I

W

P

N

Y

Y

F

Y

I

S

V

I

P

Y

I

V

I

I

A

G

P

P

L

I

I

V

G

G

A

A

C

V

L

L

G

A

A

A

A

L

I

T

Y

Y

R

Q

Y

Y

L

L

binding glycerol: I44 (vs. gap), W55 (= W40), I66 (= I50), I81 (≠ L65), N82 (= N66), G133 (≠ Q128), A134 (≠ S134), A136 (≠ Y136), P137 (= P137), F138 (≠ A138)

3c02A X-ray structure of the aquaglyceroporin from plasmodium falciparum (see paper)
31% identity, 94% coverage: 4:253/266 of query aligns to 1:235/242 of 3c02A

query
sites
3c02A

S

S

L

Y

K

V

A

R

Q

E

C

F

T

I

A

G

E

E

F

F

L

L

G

G

T

T

G

F

L

V

F

L

L

M

F

F

F

L

G

G

I

E

G

G

C

A

L

T

S

A

A

N

L

F

K

H

V

T

A

T

G

G

A

L

S

S

L

G

G

D

L

W

W

Y

E

K

I

L

C

C

I

L

I

G

W
|
W

G

G

L

L

G

A

I

V

S

F

L

F

A

G

V

I

Y

L

L

V

T

S

S

A

G

K

I

L

S

S

G

G

G

A

H

H

L

L

N

N

P

L

A

A

V

V

T

S

V

I

A

G

L

L

W

S

L

S

F

I

A

N

C

K

F

F

P

D

G

L

R

K

K

K

V

I

F

P

P

V

Y

Y

I

F

V

F

S

A

Q

Q

V

L

A

L

G

G

A

A

F

F

G

V

G

G

A

T

V

S

L

T

A

V

Y

Y

V

G

L

L

Y

Y

S

H

T

G

M

-

F

-

T

-

E

-

F

F

E

I

S

S

A

N

H

S

H

K

I

I

A

P

R

Q

G

F

S

A

V

W

E

E

S

T

L

-

Q

-

L

-

A

-

S

-

I

-

F

-

S

S

T

R

Y

N

P

P

A

S

A

I

S

S

L

L

S

T

I

-

W

-

H

G

A

A

A

F

L

F

V

N

E

E

V

L

V

I

I

L

T

T

S

G

M

I

L

L

M

L

G

L

M

V

I

I

M

L

A

V

L

V

T

V

D

D

D

E

G

-

N

N

G

I

V

C

P

G

K

K

G

F

P

H

L

I

A

L

P

K

L

L

-

S

L

V

I

V

G

G

L

L

L

I

V

I

A

L

V

C

I

I

G

G

A

I

S

T

T

F

G

G

P

G

L

N

T

T

G
|
G

F
|
F

A

A

M

L

N

N

P

P

A

S

R
|
R

D

D

F

L

G

G

P

S

K

R

L

F

F

L

T

S

W

L

M

I

A

A

G

-

W

Y

G

G

D

K

I

D

A

T

M

F

T

T

G

-

R

K

D

D

I

N

P

F

Y

Y

F

F

I

W

V

V

P

P

I

L

I

V

A

A

P

P

L

C

I

V

G

G

A

S

C

V

L

V

G

F

A

C

A

Q

I

F

Y

Y

R

D

Y

K

L

V

I

I

binding glycerol: W43 (= W46), G182 (= G197), F183 (= F198), R189 (= R204)

O94778 Aquaporin-8; AQP-8 from Homo sapiens (Human) (see 4 papers)
36% identity, 75% coverage: 9:208/266 of query aligns to 38:217/261 of O94778

query
sites
O94778

C
|
C

T

L

A

V

E

E

F

L

L

L

G

G

T

S

G

A

L

L

F
|
F

L

I

F

F

F

-

G

-

I

I

G

G

C
|
C

L

L

S

S

A

V

L

I

K

E

V

-

A

N

G

G

A

T

S

D

L

T

G

G

L

L

W

L

E

Q

I

P

C

A

I

L

I

A

W
x
H

G

G

L

L

G

A

I

L

S

G

L

L

A

V

V

I

Y

A

L

T

T

L

S

G

G

N

I

I

S

S

G

G

H

H

L

F

N

N

P

P

A

A

V

V

T

S

V

L

A

A

L

A

W

M

L

L

F

I

A

G

C

G

F

L

P

N

G

L

R

V

K

M

V

L

F

L

P

P

Y

Y

I

W

V

V

S

S

Q

Q

V

L

A

L

G

G

A

G

F

M

G

L

G

G

A

A

V

A

L

L

A

A

Y

K

V

A

L

V

Y

S

S

P

T

E

M

-

F

-

T

E

E

R

F

F

E

W

S

N

A

A

H

S

H

G

I

A

A

A

R

F

G

V

S

T

V

V

-

Q

E

E

S

Q

L

G

Q

Q

L

V

A

A

S

G

I

-

F

-

S

-

T

-

Y

-

P

-

A

-

S

-

L

-

S

-

I

-

W

-

H

-

A

A

A

L

L

V

V

A

E

E

V

I

I

L

T

T

S

T

M

L

L

L

-

A

M

L

G

A

M

V

I
x
C

M

M

A

G

L

A

T

I

D

N

D

E

G

K

N

T

G

-

V

-

P

-

K

K

G

G

P

P

L

L

A

A

P

P

L

F

L

S

I

I

G

G

L

F

L

A

V

V

A

T

V

V

I

D

G

I

A

L

S

A

T

G

G

G

P

P

L

V

T

S

G

G

F

G

A
x
C

M

M

N

N

P

P

A

A

R
|
R

D

A

F

F

G

G

P

P

C38 (= C9) mutation to S: Does not affect loss of hydrogen peroxide transport after stress.
F48 (= F19) mutation to A: Loss of hydrogen peroxide transport activity under stress condition.
C53 (= C26) modified: Cysteine persulfide; modified: Cysteine sulfenic acid (-SOH); mutation to S: Does not affect hydrogen peroxide transport under stress condition.
H72 (≠ W46) mutation to A: Does not affect hydrogen peroxide transport activity under stress condition.
C173 (≠ I161) mutation to A: Loss of hydrogen peroxide transporter activity.; mutation to S: Slightly affect hydrogen peroxide transport after stress.
C208 (≠ A199) mutation to S: Does not affect loss of hydrogen peroxide transport after stress.
R213 (= R204) mutation to A: Does not affect hydrogen peroxide transport activity under stress condition.

Sites not aligning to the query:

8 C→S: Does not affect loss of hydrogen peroxide transport after stress.
229 I → M: in a breast cancer sample; somatic mutation
247 C→S: Does not affect loss of hydrogen peroxide transport after stress.

3nkaA Crystal structure of aqpz h174g,t183f (see paper)
32% identity, 82% coverage: 1:217/266 of query aligns to 3:202/230 of 3nkaA

query
sites
3nkaA

M

M

N

F

D

R

S

K

L

L

K

A

A

A

Q

E

C

C

T

F

A

G

E

T

F

F

L

-

G

-

T

-

G

-

L

-

F

W

L

L

F

V

F

F

G

G

I

-

G

G

C

C

L

G

S

S

A
|
A

L

V

K

L

V

A

A

A

G

G

-

F

-

P

-

E

A

L

S

G

L

I

G

G

L

F

W

A

E

G

I
x
V

C

A

I

L

I

A

W

F

G

G

L

L

G

T

I

V

S

L

L

T

A

M

V

A

Y

F

L

A

T

V

S

G

G

H

I

I

S

S

G

G

H

H

L

F

N

N

P

P

A

A

V

V

T

T

V

I

A

G

L

L

W

W

L

A

F

G

A

G

C

R

F

F

P

P

G

A

R

K

K

E

V

V

F

V

P

G

Y

Y

I

V

V

I

S

A

Q

Q

V

V

A

V

G

G

A

G

F

I

G

V

G

A

A

A

V

A

L

L

A

L

Y

Y

V

L

L

I

Y

A

S

S

T

G

M

K

F

-

T

T

E

G

F

F

E

D

S

A

A

A

H

-

I

-

A

-

R

-

G

-

S

-

V

-

E

A

S

S

L

G

Q

F

L

A

A

S

S

N

I

G

F

Y

S

G

T

E

Y

H

P

S

A

P

A

G

S

G

L

Y

S

S

I

M

W

L

H

S

A

A

A

L

L

V

V

V

E

E

V

L

V

V

I

L

T

S

S

A

M

G

L

F

M

L

G

L

M

V

I

I

M

H

A

G

L

A

T

T

D

D

D

-

G

-

N

K

G

F

V

A

P

P

K

A

G

G

P

-

L

F

A

A

P

P

L

I

L

A

I

I

G

G

L

L

L

A

V

L

A

T

V

L

I

I

G

G

A

L

S

I

T

S

G
x
I

P

P

L

V

T

T

G
x
N

F

F

A

S

M

V

N

N

P

P

A

A

R

R

D

S

F

T

G

A

P

V

K

A

L

I

F

F

T

-

W

-

M

Q

A

G

G

G

W

W

binding glycerol: A25 (= A29), V41 (≠ I42), I180 (≠ G193), N184 (≠ G197)

P55064 Aquaporin-5; AQP-5 from Homo sapiens (Human) (see 2 papers)
33% identity, 92% coverage: 11:256/266 of query aligns to 16:228/265 of P55064

query
sites
P55064

A

A

E

E

F

F

L

L

G

A

T

T

G

L

L

I

F

F

L

V

F

F

G

G

I

L

G

G

C

-

L

-

S

S

A

A

L

L

K

K

V

W

A

P

G

S

A
|
A

S

L

L

P

G

T

L

I

W

L

E

Q

I
|
I

C

A

I

L

I

A

W

F

G

G

L

L

G

A

I

I

S

G

L

T

A

L

V

A

Y

Q

L

A

T

L

S

G

G

P

I

V

S

S

G

G

H

H

L

I

N

N

P

P

A

A

V

I

T

T

V

L

A

A

L

L

W

L

L

V

F

G

A

N

C

Q

F

I

P

S

G

L

R

L

K

R

V

A

F

F

P

F

Y

Y

I

V

V

A

S

A

Q

Q

V

L

A

V

G

G

A

A

F

I

G

A

G

G

A

A

V

G

L

I

A

L

Y

Y

V

G

L

V

Y

-

S

-

T

-

M

-

F

-

T

-

E

-

F

-

E

-

S

-

A

A

H

P

H

L

I

N

A

A

R

R

G

G

S

N

V

L

E

A

S

V

L

N

Q

A

L

L

A
x
N

S

N

I

N

F

T

S

T

T

Q

Y

-

P

-

A

-

S

-

L

-

S

-

I

-

W

G

H

Q

A

A

A

M

L

V

V

V

E

E

V

L

V

I

I

L

T

T

S

F

M

Q

L

L

M

A

G

L

M

C

I

I

M

F

A

A

L

S

T

T

D

D

D

S

G

R

N

R

G

T

V
x
S

P

P

K

V

G

G

P

S

L

P

A

A

P

-

L

L

L

S

I

I

G

G

L

L

L

S

V

V

A

T

V

L

I

G

G

H

A

L

S

V

T

G

G
x
I

P

Y

L

F

T

T

G

G

F

C

A

S

M

M

N

N

P

P

A

A

R
|
R

D

S

F

F

G

G

P

P

K

-

L

-

F

-

T

-

W

-

M

-

A

-

G

-

W

-

G

-

D

-

I

-

A

A

M

V

T

V

G

M

G

N

R

R

D

F

I

S

P

P

Y

A

F

H

I

W

V

V

P

F

I

W

I

V

A

G

P

P

L

I

I

V

G

G

A

A

C

V

L

L

G

A

A

A

A

I

I

L

Y

Y

R

F

Y

Y

L

L

I

L

G

F

N

P

N

N

A38 (= A35) to E: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123054
I45 (= I42) to S: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123055
N123 (≠ A130) to D: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123057
S156 (≠ V171) mutation to A: No effect on location at the cell membrane.; mutation to E: Increased location at the cell membrane.
I177 (≠ G193) to F: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123056
R188 (= R204) to C: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs368292687

5dyeD Crystal structure of the full length s156e mutant of human aquaporin 5 (see paper)
33% identity, 92% coverage: 11:256/266 of query aligns to 15:227/253 of 5dyeD

query
sites
5dyeD

A

A

E

E

F

F

L

L

G

A

T

T

G

L

L

I

F

F

L

V

F

F

G

G

I

L

G

G

C

-

L

-

S

S

A

A

L

L

K

K

V

W

A

P

G

S

A

A

S

L

L

P

G

T

L

I

W

L

E

Q

I

I

C

A

I

L

I

A

W

F

G

G

L

L

G

A

I

I

S

G

L

T

A

L

V

A

Y

Q

L

A

T

L

S

G

G

P

I

V

S

S

G

G

H

H

L

I

N

N

P

P

A

A

V

I

T

T

V

L

A

A

L

L

W

L

L

V

F

G

A

N

C

Q

F

I

P

S

G

L

R

L

K

R

V

A

F

F

P

F

Y

Y

I

V

V

A

S

A

Q

Q

V

L

A

V

G

G

A

A

F

I

G

A

G

G

A

A

V

G

L

I

A

L

Y

Y

V

G

L

V

Y

-

S

-

T

-

M

-

F

-

T

-

E

-

F

-

E

-

S

-

A

A

H

P

H

L

I

N

A

A

R

R

G

G

S

N

V

L

E

A

S

V

L

N

Q

A

L

L

A

N

S

N

I

N

F

T

S

T

T

Q

Y

-

P

-

A

-

S

-

L

-

S

-

I

-

W

G

H

Q

A

A

A

M

L

V

V

V

E

E

V

L

V

I

I

L

T

T

S

F

M

Q

L

L

M

A

G

L

M

C

I

I

M

F

A

A

L

S

T

T

D

D

D

S

G

R

N

R

G

T

V

E

P

P

K

V

G
|
G

P
x
S

L

P

A

A

P

-

L

L

L

S

I

I

G

G

L

L

L

S

V

V

A

T

V

L

I

G

G

H

A

L

S

V

T

G

G

I

P

Y

L

F

T

T

G

G

F

C

A

S

M

M

N

N

P

P

A

A

R

R

D

S

F

F

G

G

P

P

K

-

L

-

F

-

T

-

W

-

M

-

A

-

G

-

W

-

G

-

D

-

I

-

A

A

M

V

T

V

G

M

G

N

R

R

D

F

I

S

P

P

Y

A

F

H

I

W

V

V

P

F

I

W

I

V

A

G

P

P

L

I

I

V

G

G

A

A

C

V

L

L

G

A

A

A

A

I

I

L

Y

Y

R

F

Y

Y

L

L

I

L

G

F

N

P

N

N

binding O-[(S)-{[(2S)-2-(hexanoyloxy)-3-(tetradecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-D-serine: G158 (= G174), S159 (≠ P175)

P41181 Aquaporin-2; AQP-2; ADH water channel; Aquaporin-CD; AQP-CD; Collecting duct water channel protein; WCH-CD; Water channel protein for renal collecting duct from Homo sapiens (Human) (see 12 papers)
35% identity, 91% coverage: 11:253/266 of query aligns to 15:223/271 of P41181

query
sites
P41181

A

A

E

E

F

F

L

L

G

A

T

T

G

L

L

L

F

F

L

V

F

F

G

G

I

L

G

G

C

-

L

-

S

S

A

A

L

L

K

N

V

W

A

P

G

Q

A

A

S

L

L

P

G

S

L

V

W

L

E

Q

I

I

C

A

I

M

I

A

W

F

G

G

L

L

G

G

I

I

S

G

L

T

A

L

V

V

Y

Q

L

A

T

L

S

G

G

H

I

I

S

S

G
|
G

G

A

H

H

L

I

N

N

P

P

A

A

V

V

T

T

V

V

A

A

L

C

W

-

L

L

F

V

A
x
G

C
|
C

F

H

P

V

G

S

-

V

-

L

R

R

K

A

V

A

F

F

P

-

Y

Y

I

V

V

A

S

A

Q

Q

V

L

A

L

G

G

A

A

F

V

G

A

G

G

A

A

V

A

L

L

A

-

Y

-

V

-

L

-

Y

-

S

-

T

-

M

-

F

-

T

-

E

-

F

-

E

-

S

-

A

L

H

H

H

E

I

I

A

T

R

P

G

A

S

D

V

I

E

R

S

G

L

D

Q

L

L

A

A

V

S

N

I

A

F

L

S

S

T

N

Y

S

P

T

A

T

A

A

S

G

L

-

S

-

I

-

W

-

H

Q

A

A

A

V

L

T

V

V

E

E

V

L

V

F

I

L

T

T

S

L

M

Q

L

L

M

V

G

L

M

C

I

I

M

F

A

A

L
x
S

T

T

D

D

D

E

G

R

N

R

G

G

V

E

P

N

K

P

G

G

P

T

L

P

A

A

P

-

L

L

L

S

I

I

G

G

L

F

L

S

V

V

A

A

V

L

I

G

G

H

A

L

S

L

T

G

G

I

P

H

L

Y

T

T

G

G

F

C

A

S

M

M

N

N

P

P

A

A

R
|
R

D

S

F

L

G
x
A

P

P

K

A

L

V

F

-

T

-

W

-

M

-

A

-

G

-

W

-

G

-

D

-

I

-

A

-

M
x
V

T

T

G

G

G

K

R

F

D

D

I

D

P

H

Y

W

F

-

I

-

V

V

P

F

I

W

I

I

A

G

P

P

L

L

I

V

G

G

A

A

C

I

L

L

G

G

A
x
S

A
x
L

I

L

Y

Y

R

N

Y
|
Y

L

V

I

L

G64 (= G62) to R: in NDI2; loss of water channel activity; dbSNP:rs104894326
G78 (≠ A77) mutation to A: Does not affect interaction with MIAC; when associated with A-79.
C79 (= C78) mutation to A: Does not affect interaction with MIAC; when associated with A-78.
S148 (≠ L164) mutation to A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; mutation to D: Retained in the endoplasmic reticulum.
R187 (= R204) to C: in NDI2; loss of water channel activity; mutant protein does not fold properly; dbSNP:rs104894328
A190 (≠ G207) to T: in NDI2; mutant protein does not fold properly and is not functional; dbSNP:rs104894341
V194 (≠ M222) to I: in dbSNP:rs772051028
S216 (≠ A246) to P: in NDI2; loss of water channel activity; dbSNP:rs104894329
L217 (≠ A247) mutation to A: Abolishes interaction with MIAC; when associated with A-221.
Y221 (= Y251) mutation to A: Abolishes interaction with MIAC; when associated with A-217.

Sites not aligning to the query:

229 S→A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; S→D: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
231 S→A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; S→D: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
232 E→A: Reduces interaction with MIAC.
244 T→A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; T→E: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
254 R → L: in NDI2; results in the loss of arginine vasopressin-mediated phosphorylation at S-256; R → Q: in NDI2; exerts a dominant-negative effect on wild-type-AQP2 in that it interferes with its trafficking to the apical membrane; is a loss of function instead of a gain of function mutation on dominant nephrogenic diabetes insipidus
256 modified: Phosphoserine; by PKA; S→A: Retained in vesicles.; S→D: Expressed in the apical membrane.
258 E → K: in NDI2; retained in the Golgi compartment; dbSNP:rs104894332
262 P → L: in NDI2; mutant protein folds properly and is functional but is retained in intracellular vesicles; able to assemble into tetramers with wild-type AQP2 that properly localize to the apical membrane; dbSNP:rs104894339; P→A: No effect on expression at the apical cell membrane.

4nefA X-ray structure of human aquaporin 2 (see paper)
35% identity, 91% coverage: 11:253/266 of query aligns to 14:222/239 of 4nefA

query
sites
4nefA

A

A

E

E

F

F

L

L

G

A

T

T

G

L

L

L

F

F

L

V

F

F

G

G

I

L

G

G

C

-

L

-

S

S

A

A

L

L

K

N

V

W

A

P

G

Q

A

A

S

L

L

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G

S

L

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W

L

E

Q

I

I

C

A

I

M

I

A

W

F

G

G

L

L

G

G

I

I

S

G

L

T

A

L

V

V

Y

Q

L

A

T

L

S

G

G

H

I

I

S

S

G

G

G

A

H

H

L

I

N

N

P

P

A

A

V

V

T

T

V

V

A

A

L
x
C

W

-

L

L

F

V

A

G

C

C

F
x
H

P

V

G

S

-

V

-

L

R

R

K

A

V

A

F

F

P

-

Y

Y

I

V

V

A

S

A

Q

Q

V

L

A

L

G

G

A

A

F

V

G

A

G

G

A

A

V

A

L

L

A

-

Y

-

V

-

L

-

Y

-

S

-

T

-

M

-

F

-

T

-

E

-

F

-

E

-

S

-

A

L

H

H

H

E

I

I

A

T

R

P

G

A

S

D

V

I

E

R

S

G

L

D

Q

L

L

A

A

V

S

N

I

A

F

L

S

S

T

N

Y

-

P

-

A

-

S

S

L

T

S

T

I

A

W

G

H

Q

A

A

A

V

L

T

V

V

E

E

V

L

V

F

I

L

T

T

S

L

M

Q

L

L

M

V

G

L

M

C

I

I

M

F

A

A

L

S

T

T

D

D

D

E

G

R

N

R

G

G

V

-

P

-

K

E

G

N

P

P

L

G

A

T

P

P

L

A

L

L

-

S

I

I

G

G

L

F

L

S

V

V

A

A

V

L

I

G

G

H

A

L

S

L

T

G

G

I

P

H

L

Y

T

T

G

G

F

C

A

S

M

M

N

N

P

P

A

A

R

R

D

S

F

L

G

A

P

P

K

A

L

V

F

-

T

-

W

-

M

-

A

-

G

-

W

-

G

-

D

-

I

-

A

-

M

V

T

T

G

G

G

K

R

F

D

D

I

D

P

H

Y

W

F

-

I

-

V

V

P

F

I

W

I

I

A

G

P

P

L

L

I

V

G

G

A

A

C

I

L

L

G

G

A

S

A

L

I

L

Y

Y

R

N

Y

Y

L

V

I

L

binding zinc ion: C74 (≠ L73), H79 (≠ F79)

P60844 Aquaporin Z; Bacterial nodulin-like intrinsic protein; Water channel AqpZ from Escherichia coli (strain K12) (see paper)
31% identity, 82% coverage: 1:217/266 of query aligns to 1:200/231 of P60844

query
sites
P60844

M

M

N

F

D

R

S

K

L

L

K

A

A

A

Q

E

C
|
C

T

F

A

G

E

T

F

F

L

-

G

-

T

-

G

-

L

-

F

W

L

L

F

V

F

F

G

G

I

-

G

G

C
|
C

L

G

S

S

A

A

L

V

K

L

V

A

A

A

G

G

-

F

-

P

-

E

A

L

S

G

L

I

G

G

L

F

W

A

E

G

I

V

C

A

I

L

I

A

W

F

G

G

L

L

G

T

I

V

S

L

L

T

A

M

V

A

Y

F

L

A

T

V

S

G

G

H

I

I

S

S

G

G

H

H

L

F

N

N

P

P

A

A

V

V

T

T

V

I

A

G

L

L

W

W

L

A

F

G

A

G

C

R

F

F

P

P

G

A

R

K

K

E

V

V

F

V

P

G

Y

Y

I

V

V

I

S

A

Q

Q

V

V

A

V

G

G

A

G

F

I

G

V

G

A

A

A

V

A

L

L

A

L

Y

Y

V

L

L

I

Y

A

S

S

T

G

M

K

F

-

T

T

E

G

F

F

E

D

S

A

A

A

H

-

I

-

A

-

R

-

G

-

S

-

V

-

E

A

S

S

L

G

Q

F

L

A

A

S

S

N

I

G

F

Y

S

G

T

E

Y

H

P

S

A

P

A

G

S

G

L

Y

S

S

I

M

W

L

H

S

A

A

A

L

L

V

V

V

E

E

V

L

V

V

I

L

T

S

S

A

M

G

L

F

M

L

G

L

M

V

I

I

M

H

A

G

L

A

T

T

D

D

D

-

G

-

N

K

G

F

V

A

P

P

K

A

G

G

P

-

L

F

A

A

P

P

L

I

L

A

I

I

G

G

L

L

L

A

V

L

A

T

V

L

I

I

G

H

A

L

S

I

T

S

G

I

P

P

L

V

T

T

G

N

F
x
T

A

S

M

V

N

N

P

P

A

A

R
|
R

D

S

F

T

G

A

P

V

K

A

L

I

F

F

T

-

W

-

M

Q

A

G

G

G

W

W

C9 (= C9) mutation to S: No effect.
C20 (= C26) mutation to S: Loss of oligomerization; no alteration of water permeability.
T183 (≠ F198) mutation to C: No effect.
R189 (= R204) mutation R->V,S: Loss of function.

P56402 Aquaporin-2; AQP-2; ADH water channel; Aquaporin-CD; AQP-CD; Collecting duct water channel protein; WCH-CD; Water channel protein for renal collecting duct from Mus musculus (Mouse) (see 2 papers)
34% identity, 91% coverage: 11:253/266 of query aligns to 15:223/271 of P56402

query
sites
P56402

A

A

E

E

F

F

L

L

G

A

T

T

G

L

L

L

F

F

L

V

F

F

G

G

I

L

G

G

C

-

L

-

S

S

A

A

L

L

K

Q

V

W

A

A

G

S

A

S

S

P

L

P

G

S

L

V

W

L

E

Q

I

I

C

A

I

V

I

A

W

F

G

G

L

L

G

G

I

I

S

G

L

T

A

L

V

V

Y

Q

L

A

T

L

S

G

G

H

I

V

S

S

G

G

G

A

H

H

L

I

N

N

P

P

A

A

V

V

T

T

V

V

A

A

L

C

W

-

L

L

F

V

A

G

C

C

F

H

P

V

G

S

-

F

-

L

R

R

K

A

V

A

F

F

P

-

Y

Y

I

V

V

A

S

A

Q

Q

V

L

A

L

G

G

A

A

F

V

G

A

G

G

A

A

V

A

L

-

A

-

Y

-

V

I

L

L

Y

H

S

E

T

I

M

T

F

P

T

V

E

E

F

I

E

-

S

-

A

-

H

-

I

-

A

-

R

R

G

G

S

-

V

-

E

-

S

D

L

L

Q

A

L

V

A

N

S

A

I

L

F

H

S

N

T

N

Y

A

P
x
T

A

A

A

G

S

-

L

-

S

-

I

-

W

-

H

Q

A

A

A

V

L

T

V

V

E

E

V

L

V

F

I

L

T

T

S

M

M

Q

L

L

M

V

G

L

M

C

I

I

M

F

A

A

L

S

T

T

D

D

D

E

G

R

N

R

G

S

V

D

P

N

K

L

G

G

P

S

L

P

A

A

P

-

L

L

L

S

I

I

G

G

L

F

L

S

V

V

A

T

V

L

I

G

G

H

A

L

S

L

T

G

G

I

P

Y

L

F

T

T

G

G

F

C

A

S

M

M

N

N

P

P

A

A

R

R

D

S

F

L

G

A

P

P

K

A

L

V

F

-

T

-

W

-

M

-

A

-

G

-

W

-

G

-

D

-

I

-

A

-

M

V

T

T

G

G

G

K

R

F

D

D

I

D

P

H

Y

W

F

-

I

-

V

V

P

F

I

W

I

I

A

G

P

P

L

L

I

V

G

G

A

A

C

V

L

I

G

G

A

S

A

L

I

L

Y

Y

R

N

Y

Y

L

L

I

L

T126 (≠ P137) mutation to M: Does not cause loss of water channel activity, but impairs trafficking from cytoplasmic vesicles to the cell membrane.

Sites not aligning to the query:

256 modified: Phosphoserine; S → L: in cph; loss of a phosphorylation site and loss of trafficking to the apical cell membrane; causes aberrant location at the basolateral cell membrane

Query Sequence

>BWI76_RS23100 BWI76_RS23100 aquaporin
MNDSLKAQCTAEFLGTGLFLFFGIGCLSALKVAGASLGLWEICIIWGLGISLAVYLTSGI
SGGHLNPAVTVALWLFACFPGRKVFPYIVSQVAGAFGGAVLAYVLYSTMFTEFESAHHIA
RGSVESLQLASIFSTYPAASLSIWHAALVEVVITSMLMGMIMALTDDGNGVPKGPLAPLL
IGLLVAVIGASTGPLTGFAMNPARDFGPKLFTWMAGWGDIAMTGGRDIPYFIVPIIAPLI
GACLGAAIYRYLIGNNLPCNTCKLED

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