SitesBLAST

C9 (≠ G11) mutation to S: No effect.
C20 (= C22) mutation to S: Loss of oligomerization; no alteration of water permeability.
T183 (= T184) mutation to C: No effect.
R189 (= R190) mutation R->V,S: Loss of function.

2abmA Crystal structure of aquaporin z tetramer reveals both open and closed water-conducting channels (see paper)
69% identity, 97% coverage: 3:227/233 of query aligns to 1:226/227 of 2abmA

query
sites
2abmA

L

M

F

F

K

R

R

K

S

L

I

A

T

A

E

E

G
x
C

L
x
F

G

G

T

T

F
|
F

W

W

L

L

V

V

L

F

G

G

C

C

G

G

S

S

A

A

V

V

L

L

A

A

A

G

F

F

P

P

A

E

V

L

G

G

I

I

G

G

L

F

L

A

G

G

V

V

S

A

L

L

A

A

F

F

G

G

L

L

T

T

V

V

L

L

T

T

M

M

A

A

F

F

A

A

I

V

G

G

H

H

I

I

S

S

G

G

C

G

H

H

L

F

N

N

P

P

A

A

V

V

S

T

V

I

G

G

L

L

V

W

V

A

G

G

R

R

F

F

P

P

A

A

R

K

E

E

L

V

P

V

A

G

Y

Y

I

V

V

I

A

A

Q

Q

V

V

G

G

T

I

I

V

A

A

L
|
L

L

L

Y

Y

F

L

I

I

A

A

S

S

G

G

K

K

P

T

G

G

F

F

E

D

L

A

A

A

-

A

S

S

G

G

L

F

A

A

S

S

N

N

G

G

Y

Y

G

G

E

E

H

H

S

S

P

P

G

G

Y

Y

S

S

M

M

V

L

A

S

G

A

F

L

V

V

C

V

E

E

L

L

V

V

M

L

T

S

A

A

M

G

F

F

V

L

I

V

I

I

L

H

G

G

A

A

T

T

D

D

R

K

R

F

A

A

P

P

P

A

G

G

L

F

A

A

P

P

V

I

A

A

I

I

G

G

L

L

A

A

L

L

T

T

L

L

I

I

H

H

L

L

I

I

S

S

I

I

P

P

V

V

T

T

N

N

T

T

S

S

V

V

N

N

P

P

A

A

R

R

S

S

T

T

G

A

P

V

A

A

L

I

I

F

V

Q

G

G

W

W

A

A

I

L

Q

E

Q

Q

L

L

W

W

M

F

F

F

W

W

L

V

A

V

P

P

I

I

L

V

G

G

A

G

V

I

I

I

G

G

V

L

T

I

Y

Y

R

R

W

T

L

L

binding bis(((3s,4s,5r,6r)-5-(ethyl(phosphoryloxy))-3,4,6-trihydroxy-tetrahydro-2h-pyran-2-yl)methyl) hydrogen phosphate: C9 (≠ G11), F10 (≠ L12), F13 (= F15), L98 (= L100)

2o9eA Crystal structure of aqpz mutant t183c complexed with mercury (see paper)
67% identity, 99% coverage: 2:231/233 of query aligns to 2:232/232 of 2o9eA

query
sites
2o9eA

S

A

L

M

F

F

K

R

R

K

S

L

I

A

T

A

E

E

G

S

L

F

G

G

T

T

F

F

W

W

L

L

V

V

L

F

G

G

C

S

G

G

S

S

A

A

V

V

L

L

A

A

A

G

F

F

P

P

A

E

V

L

G

G

I

I

G

G

L

F

L

A

G

G

V

V

S

A

L

L

A

A

F

F

G

G

L

L

T

T

V

V

L

L

T

T

M

M

A

A

F

F

A

A

I

V

G

G

H

H

I

I

S

S

G

G

C

G

H

H

L

F

N

N

P

P

A

A

V

V

S

T

V

I

G

G

L

L

V

W

V

A

G

G

R

R

F

F

P

P

A

A

R

K

E

E

L

V

P

V

A

G

Y

Y

I

V

V

I

A

A

Q

Q

V

V

G

G

T

I

I

V

A

A

L

L

Y

Y

F

L

I

I

A

A

S

S

G

G

K

K

P

T

G

G

F

F

E

D

L

A

A

A

-

A

S

S

G

G

L

F

A

A

S

S

N

N

G

G

Y

Y

G

G

E

E

H

H

S

S

P

P

G

G

Y

Y

S

S

M

M

V

L

A

S

G

A

F

L

V

V

C

V

E
|
E

L

L

V

V

M

L

T

S

A

A

M

G

F

F

V

L

I

V

I

I

L

H

G

G

A

A

T

T

D

D

R

K

R

F

A

A

P

P

P

A

G

G

L

F

A

A

P

P

V

I

A

A

I

I

G

G

L

L

A

A

L

L

T

T

L

L

I

I

H

H

L

L

I

I

S
|
S

I

I

P

P

V

V

T

T

N

N

T

C

S

S

V

V

N

N

P

P

A

A

R

R

S

S

T

T

G

A

P

V

A

A

L

I

I

F

V

Q

G

G

W

W

A

A

I

L

Q

E

Q

Q

L

L

W

W

M

F

F

F

W

W

L

V

A

V

P

P

I

I

L

V

G

G

A

G

V

I

I

I

G

G

V

L

T

I

Y

Y

R

R

W

T

L

L

G

L

K

E

E

K

E

R

binding mercury (ii) ion: E140 (= E139), S179 (= S178)

3nkaB Crystal structure of aqpz h174g,t183f (see paper)
67% identity, 99% coverage: 3:232/233 of query aligns to 3:233/233 of 3nkaB

query
sites
3nkaB

L

M

F

F

K

R

R

K

S

L

I

A

T

A

E

E

G

C

L

F

G

G

T

T

F

F

W

W

L

L

V

V

L

F

G

G

C

C

G

G

S

S

A
|
A

V

V

L

L

A

A

A
|
A

A

G

F

F

P

P

A

E

V

L

G

G

I

I

G

G

L
x
F

L

A

G

G

V

V

S

A

L

L

A

A

F

F

G

G

L

L

T

T

V

V

L

L

T

T

M

M

A

A

F

F

A

A

I

V

G

G

H

H

I

I

S

S

G

G

C

G

H

H

L

F

N

N

P

P

A

A

V

V

S

T

V

I

G

G

L

L

V

W

V

A

G

G

R

R

F

F

P

P

A

A

R

K

E

E

L

V

P

V

A

G

Y

Y

I

V

V

I

A

A

Q

Q

V

V

G

G

T

I

I

V

A

A

L

L

Y

Y

F

L

I

I

A

A

S

S

G

G

K

K

P

T

G

G

F

F

E

D

-

A

L

A

A

A

S

S

G

G

L

F

A

A

S

S

N

N

G

G

Y

Y

G

G

E

E

H

H

S

S

P

P

G

G

Y

Y

S

S

M

M

V

L

A

S

G

A

F

L

V

V

C

V

E

E

L

L

V

V

M

L

T

S

A

A

M

G

F

F

V

L

I

V

I

I

L

H

G

G

A

A

T

T

D

D

R

K

R

F

A

A

P

P

P

A

G

G

L

F

A

A

P

P

V

I

A

A

I

I

G

G

L

L

A

A

L

L

T

T

L

L

I

I

H

G

L

L

I

I

S

S

I

I

P

P

V

V

T

T

N

N

T

F

S

S

V

V

N

N

P

P

A

A

R

R

S

S

T

T

G

A

P

V

A

A

L

I

I

F

V

Q

G

G

W

W

A

A

I

L

Q

E

Q

Q

L

L

W

W

M

F

F

F

W

W

L

V

A

V

P

P

I

I

L

V

G

G

A

G

V

I

I

I

G

G

V

L

T

I

Y

Y

R

R

W

T

L

L

G

L

K

E

E

K

E

R

P

D

binding glycerol: A25 (= A25), A29 (= A29), F38 (≠ L38)

P08995 Nodulin-26; N-26 from Glycine max (Soybean) (Glycine hispida) (see paper)
35% identity, 97% coverage: 3:229/233 of query aligns to 36:252/271 of P08995

query
sites
P08995

L

F

F

L

K

Q

R

K

S

L

I

V

T

A

E

E

G

A

L

V

G

G

T

T

F

Y

W

F

L

L

V

I

L

F

G

A

G

G

C

C

G

A

S

S

A

L

V

V

L

V

A

N

A

E

A

N

F

Y

P

Y

A

N

V

M

G

-

I

I

G

T

L

F

L

P

G

G

V

I

S

A

L

I

A

V

F

W

G

G

L

L

T

V

V

L

L

T

T

V

M

L

A

V

F

Y

A

T

I

V

G

G

H

H

I

I

S

S

G

G

C

G

H

H

L

F

N

N

P

P

A

A

V

V

S

T

V

I

G

A

L

F

V

A

V

S

G

T

G

R

R

R

F

F

P

P

A

L

R

I

E

Q

L

V

P

P

A

A

Y

Y

I

V

V

V

A

A

Q

Q

V

L

G

G

G

S

T

I

I

L

A

A

A

S

A

G

L

T

L

L

Y

R

F

L

I

L

A

F

S

M

G

G

K

N

P

-

G

-

F

H

E

D

L

Q

A

F

S

S

G

G

L

T

A

V

S

P

N

N

G

G

Y

-

G

-

E

-

H

-

S

-

P

-

G

-

Y

-

S

T

M

N

V

L

A

Q

G

A

F

F

V

V

C

F

E

E

L

F

V

I

M

M

T

T

A

F

M

F

F

L

V

M

V

F

I

V

I

I

L

C

G

G

-

V

A

A

T

T

D

D

R

N

R

R

A

A

P

V

P

G

G

E

L

F

A

A

P

G

V

I

A

A

I

I

G

G

L

S

A

T

L

L

T

L

L

L

I

N

H

V

L

I

I

I

S

G

I

G

P

P

V

V

T

T

N

G

T

A

S

S

V

M

N

N

P

P

A

A

R

R

S

S

T

L

G

G

P

P

A

A

L

F

I

V

V

H

G

G

G

E

W

Y

A

-

I

-

Q

E

Q

G

L

I

W

W

M

I

F

Y

W

L

L

L

A

A

P

P

I

V

L

V

G

G

A

A

V

I

I

A

G

G

G

A

V

W

T

V

Y

Y

-

N

-

I

-

V

R

R

W

Y

L

T

G

D

K

K

Sites not aligning to the query:

262 modified: Phosphoserine; by CPK

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)
36% identity, 96% coverage: 4:227/233 of query aligns to 9:222/271 of P56402

query
sites
P56402

F

F

K

S

R

R

S

A

I

V

-

L

T

A

E

E

G

F

L

L

G

A

T

T

F

L

W

L

L

F

V

V

L

F

G

F

G

G

C

L

G

G

S

S

A

A

V

L

L

Q

A

W

A

A

A

S

F

S

P

P

A

P

V

-

G

-

I

-

G

S

L

V

L

L

G

Q

V

I

S

A

L

V

A

A

F

F

G

G

L

L

T

G

V

I

L

G

T

T

M

L

A

V

F

Q

A

A

I

L

G

G

H

H

I

V

S

S

G

G

C

A

H

H

L

I

N

N

P

P

A

A

V

V

S

T

V

V

G

A

L

C

V

L

V

V

G

G

G

C

R

H

F

V

P

S

A

F

R

L

E

R

L

A

P

A

A

F

Y

Y

I

V

V

A

A

A

Q

Q

V

L

G

G

G

A

T

V

I

A

A

G

A

A

L

I

L

L

Y

H

F

E

I

I

A

T

S

P

G

-

K

-

P

-

G

-

F

V

E

E

L

I

A

R

S

G

G

D

L

L

A

A

S

V

N

N

G

A

Y

L

G

H

E

N

H

N

S

A

P
x
T

G

A

G

G

Y

Q

S

A

M

V

V

-

A

-

G

-

F

-

V

T

C

V

E

E

L

L

V

F

M

L

T

T

A

M

M

Q

F

L

V

V

V

L

I

C

I

I

L

F

G

A

A

S

T

T

D

D

R

E

R

R

A

R

P

S

P

D

G

N

L

L

A

G

P

S

-

P

-

A

V

L

A

S

I

I

G

G

L

F

A

S

L

V

T

T

L

L

I

G

H

H

L

L

I

L

S

G

I

I

P

Y

V

F

T

T

N

G

T

C

S

S

V

M

N

N

P

P

A

A

R

R

S

S

T

L

G

A

P

P

A

A

L

V

I

V

V

T

G

G

G

K

W

F

A

-

I

-

Q

D

L

H

W

W

M

V

F

F

W

W

L

I

A

G

P

P

I

L

L

V

G

G

A

A

V

V

I

I

G

G

G

S

V

L

T

L

Y

Y

R

N

W

Y

L

L

T126 (≠ P127) 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

4nefA X-ray structure of human aquaporin 2 (see paper)
34% identity, 96% coverage: 4:227/233 of query aligns to 8:221/239 of 4nefA

query
sites
4nefA

F

F

K

S

R

R

S

A

I

V

-

F

T

A

E

E

G

F

L

L

G

A

T

T

F

L

W

L

L

F

V

V

L

F

G

F

G

G

C

L

G

G

S

S

A

A

V

L

L

-

A

-

A

N

F

W

P

P

A

Q

V

A

G

L

I

P

G

S

L

V

L

L

G

Q

V

I

S

A

L

M

A

A

F

F

G

G

L

L

T

G

V

I

L

G

T

T

M

L

A

V

F

Q

A

A

I

L

G

G

H

H

I

I

S

S

G

G

C

A

H

H

L

I

N

N

P

P

A

A

V

V

S

T

V

V

G

A

L
x
C

V

L

V

V

G

G

G

C

R
x
H

F

V

P

S

A

V

R

L

E

R

L

A

P

A

A

F

Y

Y

I

V

V

A

A

A

Q

Q

V

L

G

G

G

A

T

V

I

A

A

G

A

A

L

L

Y

H

F

E

I

I

A

T

S

P

G

A

K

-

P

-

G

-

F

-

E

D

L

I

A

R

S

G

G

D

L

L

A

A

S

V

N

N

G

A

Y

L

G

S

E

N

H

S

S

T

P

T

G

A

G

G

Y

Q

S

A

M

V

V

T

A

V

G

-

F

-

V

-

C

-

E

E

L

L

V

F

M

L

T

T

A

L

M

Q

F

L

V

V

V

L

I

C

I

I

L

F

G

A

A

S

T

T

D

D

R

E

R

R

-

R

-

G

A

E

P

N

P

P

G

G

L

T

A

P

P

A

V

L

A

S

I

I

G

G

L

F

A

S

L

V

T

A

L

L

I

G

H

H

L

L

I

L

S

G

I

I

P

H

V

Y

T

T

N

G

T

C

S

S

V

M

N

N

P

P

A

A

R

R

S

S

T

L

G

A

P

P

A

A

L

V

I

V

V

T

G

G

G

K

W

F

A

-

I

-

Q

D

L

H

W

W

M

V

F

F

W

W

L

I

A

G

P

P

I

L

L

V

G

G

A

A

V

I

I

L

G

G

G

S

V

L

T

L

Y

Y

R

N

W

Y

L

V

binding zinc ion: C74 (≠ L72), H79 (≠ R77)

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 11 papers)
34% identity, 96% coverage: 4:227/233 of query aligns to 9:222/271 of P41181

query
sites
P41181

F

F

K

S

R

R

S

A

I

V

-

F

T

A

E

E

G

F

L

L

G

A

T

T

F

L

W

L

L

F

V

V

L

F

G

F

G

G

C

L

G

G

S

S

A

A

V

L

L

-

A

-

A

N

F

W

P

P

A

Q

V

A

G

L

I

P

G

S

L

V

L

L

G

Q

V

I

S

A

L

M

A

A

F

F

G

G

L

L

T

G

V

I

L

G

T

T

M

L

A

V

F

Q

A

A

I

L

G

G

H

H

I

I

S

S

G
|
G

C

A

H

H

L

I

N

N

P

P

A

A

V

V

S

T

V

V

G

A

L

C

V

L

V

V

G

G

G

C

R

H

F

V

P

S

A

V

R

L

E

R

L

A

P

A

A

F

Y

Y

I

V

V

A

A

A

Q

Q

V

L

G

G

G

A

T

V

I

A

A

G

A

A

L

L

Y

H

F

E

I

I

A

T

S

P

G

A

K

-

P

-

G

-

F

-

E

D

L

I

A

R

S

G

G

D

L

L

A

A

S

V

N

N

G

A

Y

L

G

S

E

N

H

S

S

T

P

T

G

A

G

G

Y

Q

S

A

M

V

V

-

A

-

G

-

F

-

V

T

C

V

E

E

L

L

V

F

M

L

T

T

A

L

M

Q

F

L

V

V

V

L

I

C

I

I

L

F

G

A

A
x
S

T

T

D

D

R

E

R

R

-

R

-

G

A

E

P

N

P

P

G

G

L

T

A

P

P

A

V

L

A

S

I

I

G

G

L

F

A

S

L

V

T

A

L

L

I

G

H

H

L

L

I

L

S

G

I

I

P

H

V

Y

T

T

N

G

T

C

S

S

V

M

N

N

P

P

A

A

R
|
R

S

S

T

L

G
x
A

P

P

A

A

L

V

I
x
V

V

T

G

G

G

K

W

F

A

-

I

-

Q

D

L

H

W

W

M

V

F

F

W

W

L

I

A

G

P

P

I

L

L

V

G

G

A

A

V

I

I

L

G

G

G
x
S

V

L

T

L

Y

Y

R

N

W

Y

L

V

G64 (= G61) to R: in NDI2; loss of water channel activity; dbSNP:rs104894326
S148 (≠ A153) 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 (= R190) to C: in NDI2; loss of water channel activity; mutant protein does not fold properly; dbSNP:rs104894328
A190 (≠ G193) to T: in NDI2; mutant protein does not fold properly and is not functional; dbSNP:rs104894341
V194 (≠ I197) to I: in dbSNP:rs772051028
S216 (≠ G221) to P: in NDI2; loss of water channel activity; dbSNP:rs104894329

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.
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.

8ct2D Local refinement of aqp1 tetramer (c1; refinement mask included d1 of protein 4.2 and ankyrin-1 ar1-5) in class 2 of erythrocyte ankyrin-1 complex (see paper)
38% identity, 80% coverage: 41:227/233 of query aligns to 50:228/247 of 8ct2D

query
sites
8ct2D

V

V

S

S

L

L

A

A

F

F

G

G

L

L

T

S

V

I

L

A

T

T

M

L

A

A

F

Q

A

S

I

V

G

G

H

H

I

I

S

S

G

G

C

A

H

H

L

L

N

N

P

P

A

A

V

V

S

T

V

L

G

G

L

L

V

L

G

S

G

C

R

Q

F

I

P

S

A

I

R

F

E

R

L

A

P

L

A

M

Y

Y

I

I

V

I

A

A

Q

Q

V

C

V

V

G

G

G

A

T

I

I

V

A

A

A

T

A

A

L
x
I

L

L

Y

S

F
x
G

I
|
I

A

T

S

S

G

S

K

L

P

T

G

G

F

N

E

S

L

L

A

G

S

R

G

N

L

D

A

L

S

A

N

D

G

G

Y

V

G
x
N

E

S

H
x
G

S
x
Q

P

-

G

-

Y

-

S

-

M

-

V

-

A

-

G

G

F

L

V
x
G

C

I

E

E

L
x
I

V

I

M

G

T

T

A

L

M

Q

F

L

V

V

V

L

I

C

I

V

L

L

G

A

A

T

T

T

D

D

R

R

A

R

P

R

P

D

-

L

-

G

G

G

L

S

A

A

P

P

V

L

A

A

I

I

G

G

L

L

A

S

L

V

T

A

L

L

I

G

H

H

L

L

I

L

S

A

I

I

P

D

V

Y

T

T

N

G

T

C

S

G

V

I

N

N

P

P

A

A

R

R

S

S

T

F

G

G

P

S

A

A

L

V

I

I

V

T

G

H

G

N

W

F

A

S

I

N

Q

H

Q

-

L

-

W

W

M

I

F

F

W

W

L

V

A

G

P

P

I

F

L

I

G

G

A

G

V

A

I

L

G

A

G

V

V

L

T

I

Y

Y

R

D

W

F

L

I

binding cholesterol: I109 (≠ L100), G112 (≠ F103), I113 (= I104), N132 (≠ G123), G134 (≠ H125), Q135 (≠ S126), G138 (≠ V137), I141 (≠ L140)

P55088 Aquaporin-4; AQP-4; Mercurial-insensitive water channel; MIWC; WCH4 from Mus musculus (Mouse) (see 2 papers)
34% identity, 97% coverage: 1:227/233 of query aligns to 32:251/323 of P55088

query
sites
P55088

M

Q

S

A

L

F

F

W

K

K

R

A

S

V

I

S

T

A

E

E

G

F

L

L

G

A

T

T

F

L

W

I

L

F

V

V

L

L

G

L

G

G

C

V

G

G

S

S

A

T

V

I

-

N

L

W

A

G

A

S

F

E

P

N

A

P

V

L

G

P

I

V

G

D

L

M

L

V

G

L

V

I

S

S

L

L

A

C

F

F

G

G

L

L

T

S

V

I

L

A

T

T

M

M

A

V

F

Q

A

C

I

F

G

G

H

H

I

I

S

S

G

G

C

G

H

H

L

I

N

N

P

P

A

A

V

V

S

T

V

V

G

A

L

M

V

V

V

C

G

T

G

R

R

K

F

I

P
x
S

A

I

R

A

E

K

L

S

P

V

A

F

Y

Y

I

I

V

I

A

A

Q

Q

V

C

V

L

G

G

G

A

T

I

I

I

A

G

A

A

A

G

L

I

L

L

Y

Y

F

L

I

V

A

T

S

P

-

P

-

S

-

V

G

G

K

G

P

L

G

G

F

V

E

T

L

T

A

V

S

H

G

G

L

N

A

L

S

T

N

A

G

G

Y

H

G

-

E

-

H

-

S

-

P

-

G

-

Y

-

S

-

M

-

V

-

A

-

G

G

F

L

V

L

C

V

E

E

L

L

V

I

M

I

T

T

A

F

M

Q

F

L

V

V

V

F

I

T

I

I

L

F

G

A

A

S

T

C

D

D

-

S

-

K

R

R

R

T

A

D

P

V

P

T

G

G

L

S

A

I

P

A

V

L

A

A

I

I

G

G

L

F

A

S

L

V

T

A

L

I

I

G

H

H

L

L

I

F

S

A

I

I

P

N

V

Y

T

T

N

G

T

A

S

S

V

M

N

N

P

P

A

A

R

R

S

S

T

F

G

G

P

P

A

A

L

V

I

I

V

M

G

G

G

N

W

W

A

A

I

-

Q

-

Q

N

L

H

W

W

M

I

F

Y

W

W

L

V

A

G

P

P

I

I

L

M

G

G

A

A

V

V

I

L

G

A

G

G

V

A

T

L

Y

Y

R

E

W

Y

L

V

S111 (≠ P79) 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

P47863 Aquaporin-4; AQP-4; Mercurial-insensitive water channel; MIWC; WCH4 from Rattus norvegicus (Rat) (see 4 papers)
35% identity, 82% coverage: 36:227/233 of query aligns to 68:251/323 of P47863

query
sites
P47863

I

V

G

D

L

M

L

V

G

L

V

I

S

S

L

L

A

C

F

F

G

G

L

L

T

S

V

I

L

A

T

T

M

M

A

V

F

Q

A

C

I

F

G

G

H

H

I

I

S

S

G

G

C

G

H

H

L

I

N

N

P

P

A

A

V

V

S

T

V

V

G

A

L

M

V

V

V

C

G

T

G

R

R

K

F

I

P

S

A

I

R

A

E

K

L

S

P

V

A

F

Y

Y

I

I

V

T

A

A

Q

Q

V

C

V

L

G

G

G

A

T

I

I

I

A

G

A

A

A

G

L

I

L

L

Y

Y

F

L

I

V

A

T

S

P

-

P

-

S

-

V

G

G

K

G

P

L

G

G

F

V

E

T

L

T

A

V

S

H

G

G

L

N

A

L

S

T

N

A

G

G

Y

H

G

-

E

-

H

-

S

-

P

-

G

-

Y

-

S

-

M

-

V

-

A

-

G

G

F

L

V

L

C

V

E

E

L

L

V

I

M

I

T

T

A

F

M

Q

F

L

V

V

V

F

I

T

I

I

L

F

G

A

A

S

T

C

D

D

-
x
S

-

K

R

R

R

T

A

D

P

V

P

T

G

G

L

S

A

V

P

A

V

L

A

A

I

I

G

G

L

F

A

S

L

V

T

A

L

I

I

G

H
|
H

L

L

I

F

S

A

I

I

P

N

V

Y

T

T

N

G

T

A

S

S

V

M

N

N

P

P

A

A

R

R

S

S

T

F

G

G

P

P

A

A

L

V

I

I

V

M

G

G

G

N

W

W

A

-

I

-

Q

E

Q

N

L

H

W

W

M

I

F

Y

W

W

L

V

A

G

P

P

I

I

L

I

G

G

A

A

V

V

I

L

G

A

G

G

V

A

T

L

Y

Y

R

E

W

Y

L

V

S180 (vs. gap) modified: Phosphoserine; by PKC; mutation to A: Decreases internalization from the cell membrane in response to PKC activation.
H201 (= H175) 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

2evuA Crystal structure of aquaporin aqpm at 2.3a resolution (see paper)
35% identity, 97% coverage: 1:227/233 of query aligns to 2:243/245 of 2evuA

query
sites
2evuA

M

V

S

S

L

L

F

T

K

K

R

R

S

C

I

I

T

A

E

E

G

F

L

I

G

G

T

T

F

F

W

I

L
|
L

V

V

L

F

G

F

G

G

C

A

G

G

S

S

A
|
A

V

A

L

V

A

T

A

L

A

M

F

I

P
x
A

A
x
S

V

G

G
|
G

I

T

-
x
S

-

P

-

N

-

P

-

F

-
x
N

-
x
I

-
x
G

-
x
I

-

G

-

L

-

G

-

L

-

G

G

D

L
x
W

L

V

G

A

V

I

S

G

L

L

A

A

F

F

G

G

L

F

T

A

V
x
I

L

A

T

A

M

S

A

I

F

Y

A

A

I

L

G

G

H

N

I

I

S

S

G
|
G

C
|
C

H
|
H

L
x
I

N
|
N

P

P

A

A

V

V

S

T

V

I

G

G

L
|
L

V

W

V

S

G

V

G

K

R

K

F

F

P

P

A

G

R

R

E

E

L

V

P

V

A

P

Y

Y

I

I

V

I

A

A

Q

Q

V

L

G

G

G

-

T

-

I

-

A

-

A

A

L

F

L

G

Y

S

F

F

I

I

A

F

S

L

G

Q

K

C

P

A

G

G

F

I

E

G

L

A

A

A

S
x
T

G

-

L

-

A

-

S

V

N

G

G
|
G

Y

L

G
|
G

E
x
A

H
x
T

S
x
A

P
|
P

-
x
F

G
x
P

G

G

Y

I

S

S

M

Y

V

W

A

Q

G

A

F

M

V

L

C

A

E

E

L

V

V

V

M

G

T

T

A

F

M

L

F
x
L

V

M

V

I

I

T

I
|
I

L

M

G

G

-

I

A
|
A

T

V

D

D

R

E

R

R

A

A

P

P

P

K

G

G

L

F

A

A

P

G

V

I

A

I

I
|
I

G

G

L

L

A

T

L

V

T

A

L

G

I

I

H

I

L

T

I

T

S

L

I

G

P

N

V

I

T

S

N
x
G

T

S

S

S

V

L

N
|
N

P

P

A

A

R
|
R

S

T

T

F

G

G

P

P

A

Y

L

L

I

N

V

D

G

M

G

I

W

F

A

A

I

G

Q

T

Q

D

L

L

W

W

M

N

F

Y

W

Y

-

S

-

I

-

Y

-

V

L

I

A

G

P

P

I

I

L

V

G

G

A

A

V

V

I

L

G

A

V

L

T

T

Y

Y

R

Q

W

Y

L

L

binding glycerol: L18 (= L17), A26 (= A25), A33 (≠ P32), S34 (≠ A33), G36 (= G35), S38 (vs. gap), N43 (vs. gap), I44 (vs. gap), I44 (vs. gap), G45 (vs. gap), I46 (vs. gap), W55 (≠ L38), I66 (≠ V49), G78 (= G61), C79 (= C62), H80 (= H63), I81 (≠ L64), N82 (= N65), L89 (= L72), T128 (≠ S115), G131 (= G121), G133 (= G123), A134 (≠ E124), T135 (≠ H125), A136 (≠ S126), P137 (= P127), F138 (vs. gap), P139 (≠ G128), L157 (≠ F146), I161 (= I150), A165 (= A153), I179 (= I167), G195 (≠ N183), N199 (= N187), R202 (= R190)

P55064 Aquaporin-5; AQP-5 from Homo sapiens (Human) (see 2 papers)
34% identity, 97% coverage: 1:227/233 of query aligns to 8:224/265 of P55064

query
sites
P55064

M

V

S

A

L

F

F

L

K

K

R

A

S

V

I

F

T

A

E

E

G

F

L

L

G

A

T

T

F

L

W

I

L

F

V

V

L

F

G

F

G

G

C

L

G

G

S

S

A

A

V

L

L

-

A

-

A

K

F

W

P

P

A

S

V
x
A

G

L

I

P

G

T

L

I

L

L

G

Q

V
x
I

S

A

L

L

A

A

F

F

G

G

L

L

T

A

V

I

L

G

T

T

M

L

A

A

F

Q

A

A

I

L

G

G

H

P

I

V

S

S

G

G

C

G

H

H

L

I

N

N

P

P

A

A

V

I

S

T

V

L

G

A

L

L

V

L

V

V

G

G

G

N

R

Q

F

I

P

S

A

L

R

L

E

R

L

A

P

F

A

F

Y

Y

I

V

V

A

A

A

Q

Q

V

L

V

V

G

G

G

A

T

I

I

A

A

G

A

A

A

G

L

I

L

L

Y

Y

F

G

I

V

A

A

S

P

G

-

K

-

P

-

G

-

F

-

E

-

L

-

A

-

S

-

G

-

L

L

A

N

S

A

N

R

G

G

Y

N

G

L

E

A

H

V

S

N

P

A

G

L

G
x
N

Y

N

S

N

M

T

V

T

A

Q

G

G

-

Q

-

A

F

M

V

V

C

V

E

E

L

L

V

I

M

L

T

T

A

F

M

Q

F

L

V

A

V

L

I

C

I

I

L

F

G

A

A

S

T

T

D

D

R

S

R

R

-

R

-

T

A
x
S

P

P

P

V

G

G

L

S

A

P

P

A

V

L

A

S

I

I

G

G

L

L

A

S

L

V

T

T

L

L

I

G

H

H

L

L

I

V

S

G

I
|
I

P

Y

V

F

T

T

N

G

T

C

S

S

V

M

N

N

P

P

A

A

R
|
R

S

S

T

F

G

G

P

P

A

A

L

V

I

V

V

M

G

N

G

R

W

F

A

S

I

P

Q

A

Q

H

L

-

W

W

M

V

F

F

W

W

L

V

A

G

P

P

I

I

L

V

G

G

A

A

V

V

I

L

G

A

V

I

T

L

Y

Y

R

F

W

Y

L

L

A38 (≠ V34) to E: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123054
I45 (≠ V41) to S: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123055
N123 (≠ G129) to D: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123057
S156 (≠ A158) mutation to A: No effect on location at the cell membrane.; mutation to E: Increased location at the cell membrane.
I177 (= I179) to F: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123056
R188 (= R190) 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)
34% identity, 97% coverage: 1:227/233 of query aligns to 7:223/253 of 5dyeD

query
sites
5dyeD

M

V

S

A

L

F

F

L

K

K

R

A

S

V

I

F

T

A

E

E

G

F

L

L

G

A

T

T

F

L

W

I

L

F

V

V

L

F

G

F

G

G

C

L

G

G

S

S

A

A

V

L

L

-

A

-

A

K

F

W

P

P

A

S

V

A

G

L

I

P

G

T

L

I

L

L

G

Q

V

I

S

A

L

L

A

A

F

F

G

G

L

L

T

A

V

I

L

G

T

T

M

L

A

A

F

Q

A

A

I

L

G

G

H

P

I

V

S

S

G

G

C

G

H

H

L

I

N

N

P

P

A

A

V

I

S

T

V

L

G

A

L

L

V

L

V

V

G

G

G

N

R

Q

F

I

P

S

A

L

R

L

E

R

L

A

P

F

A

F

Y

Y

I

V

V

A

A

A

Q

Q

V

L

V

V

G

G

G

A

T

I

I

A

A

G

A

A

A

G

L

I

L

L

Y

Y

F

G

I

V

A

A

S

P

G

-

K

-

P

-

G

-

F

-

E

-

L

-

A

-

S

-

G

-

L

L

A

N

S

A

N

R

G

G

Y

N

G

L

E

A

H

V

S

N

P

A

G

L

G

N

Y

N

S

N

M

T

V

T

A

Q

G

G

-

Q

-

A

F

M

V

V

C

V

E

E

L

L

V

I

M

L

T

T

A

F

M

Q

F

L

V

A

V

L

I

C

I

I

L

F

G

A

A

S

T

T

D

D

R

S

R

R

-

R

-

T

A

E

P

P

P

V

G
|
G

L
x
S

A

P

P

A

V

L

A

S

I

I

G

G

L

L

A

S

L

V

T

T

L

L

I

G

H

H

L

L

I

V

S

G

I

I

P

Y

V

F

T

T

N

G

T

C

S

S

V

M

N

N

P

P

A

A

R

R

S

S

T

F

G

G

P

P

A

A

L

V

I

V

V

M

G

N

G

R

W

F

A

S

I

P

Q

A

Q

H

L

-

W

W

M

V

F

F

W

W

L

V

A

G

P

P

I

I

L

V

G

G

A

A

V

V

I

L

G

A

V

I

T

L

Y

Y

R

F

W

Y

L

L

binding O-[(S)-{[(2S)-2-(hexanoyloxy)-3-(tetradecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-D-serine: G158 (= G161), S159 (≠ L162)

Q9XF58 Aquaporin PIP2-5; Plasma membrane intrinsic protein 2-5; ZmPIP2-5; ZmPIP2;5; ZmPIP2a from Zea mays (Maize) (see paper)
34% identity, 83% coverage: 35:227/233 of query aligns to 77:269/285 of Q9XF58

query
sites
Q9XF58

G

G

I

V

G

G

L

V

L

L

G

G

V

I

S

A

L

W

A

A

F

F

G

G

L

G

T

M

V

I

L

F

T

I

M

L

A

V

F

Y

A

C

I

T

G

A

H

G

I

V

S

S

G

G

C
x
G

H

H

L

I

N

N

P

P

A

A

V

V

S

T

V

F

G

G

L

L

V

F

V

L

G

A

G

R

R

K

F

V

P

S

A

L

R

V

E

R

L

A

P

L

A

L

Y

Y

I

I

V

V

A

A

Q

Q

V

C

V

L

G

G

G

A

T

I

I

C

A

G

A

V

A

G

L

L

L

V

Y

-

F

-

I

-

A

-

S

-

G

-

K

-

P

K

G

G

F

F

E

Q

L

S

A

A

S

F

G

Y

L

V

A

R

S

Y

N

G

G

G

Y

G

G

A

E

N

H

E

S

L

P

S

G

A

G

G

Y

Y

S

S

M

K

V

G

A

T

G

G

F

L

V

A

C

A

E

E

L

I

V

I

M

G

T

T

A

F

M

V

F

L

V

V

V

Y

I

T

I

V

L

F

G

S

A

A

T

T

D

D

-

P

-

K

R

R

R

N

A

A

P

R

-

D

-

S

-

H

-

V

P

P

G

V

L

L

A

A

P

P

V

L

A

P

I

I

G

G

L

F

A

A

L

V

T

F

L

M

I

V

H

H

L

L

I

A

S

T

I

I

P

P

V

I

T

T

N

G

T

T

S

G

V

I

N

N

P

P

A

A

R

R

S

S

T

L

G

G

P

A

A

A

L

V

I

I

V

Y

G

N

-

D

W

K

A

A

I

W

Q

D

L

H

W

W

M

I

F

F

W

W

L

V

A

G

P

P

I

F

L

I

G

G

A

A

V

A

I

I

G

A

V

A

T

Y

Y

H

R

Q

W

Y

L

V

G104 (≠ C62) mutation to W: Loss of water transport.

Q6Z2T3 Aquaporin NIP2-1; Low silicon protein 1; NOD26-like intrinsic protein 2-1; OsNIP2;1; Silicon influx transporter LSI1 from Oryza sativa subsp. japonica (Rice) (see paper)
33% identity, 98% coverage: 3:231/233 of query aligns to 47:261/298 of Q6Z2T3

query
sites
Q6Z2T3

L

L

F

L

K

K

R

K

S

V

I

V

T

S

E

E

G

V

L

V

G

A

T

T

F

F

W

L

L

L

V

V

L

F

G

M

G

T

C

C

G

G

S

A

A

A

V

G

L

I

A

S

A

G

A

S

F

-

P

D

A

L

V

S

G

R

I

I

G

S

L

Q

L

L

G

G

V

Q

S

S

L

I

A

A

F

G

G

G

L

L

T

I

V

V

L

T

T

V

M

M

A

I

F

Y

A

A

I

V

G

G

H

H

I

I

S

S

G

G

C

A

H

H

L

M

N

N

P

P

A

A

V

V

S

T

V

L

G

A

L

F

V

A

V

V

G

F

G

R

R

H

F

F

P

P

A

W

R

I

E

Q

L

V

P

P

A

F

Y

Y

I

W

V

A

A
|
A

Q

Q

V

F

V

T

G

G

G

A

T

I

I

C

A

A

A

S

A

F

L

V

L

L

Y

K

F

A

I

V

A

I

S

H

G

-

K

-

P

-

G

-

F

-

E

-

L

-

A

-

S

-

G

-

L

-

A

P

S

V

N

D

G

V

Y

I

G

G

E

T

H

T

S

T

P

P

G

V

G

G

-

P

-

H

-

W

Y

H

S

S

M

L

V

V

A

V

G

E

F

V

V

I

C

V

E

T

L

F

V

N

M

M

T

-

A

-

M

M

F

F

V

V

V

T

I

L

I

A

L

V

G

-

A

A

T

T

D

D

R

T

R

R

A

A

P

V

P

G

G

E

L

L

A

A

P

G

V

L

A

A

I

V

G

G

L

S

A

A

L

V

T

C

L

I

I

T

H

S

L

I

I

F

S

A

I

G

P

A

V

I

T

S

N

G

T

G

S

S

V

M

N

N

P

P

A

A

R

R

S

T

T

L

G

G

P

P

A

A

L

L

I

A

V

S

G

N

G

K

W

F

A

-

I

-

Q

D

Q

G

L

L

W

W

M

I

F

Y

W

F

L

L

A

G

P

P

I

V

L

M

G

G

A

T

V

L

I

S

G

G

G

A

V

W

T

T

Y

Y

R

T

W

F

L

I

G

R

K

F

E

E

E

D

A132 (= A89) mutation to T: In lsi; impairs silicon uptake. Grain discoloration. Reduces grain yield 10-fold.

P06624 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Bos taurus (Bovine) (see 4 papers)
32% identity, 97% coverage: 2:227/233 of query aligns to 8:222/263 of P06624

query
sites
P06624

S

S

L

F

F

W

K

R

R

A

S

I

I

C

T

A

E

E

G

F

L

F

G

A

T

S

F

L

W

F

L

Y

V

V

L

F

G

F

G

G

C

L

G

G

S

A

A

S

V

L

L

R

A

W

A

A

A

P

F

G

P

P

A

-

V

-

G

-

I

L

G

H

L

V

L

L

G

Q

V

V

S

A

L

L

A

A

F

F

G

G

L

L

T

A

V

L

L

A

T

T

M

L

A

V

F

Q

A

A

I

V

G

G

H

H

I

I

S

S

G

G

C

A

H

H

L

V

N

N

P

P

A

A

V

V

S

T

V

F

G

A

L

F

V

L

V

V

G

G

G

S

R

Q

F

M

P

S

A

L

R

L

E

R

L

A

P

I

A

C

Y

Y

I

M

V

V

A

A

Q

Q

V

L

G

G

G

A

T

V

I

A

A

G

A

A

L

V

L

L

Y

Y

F

S

I

V

A

T

S

P

G

P

K

A

P

-

G

-

F

-

E

-

L

V

A

R

S

G

G

N

L

L

A

A

S

L

N

N

G

T

Y

L

G

H

E

P

H

-

S

-

P

-

G

-

G

G

Y

V

S

S

M

V

V

G

A

Q

G

A

F

T

V

I

C

V

E

E

L

I

V

F

M

L

T

T

A

L

M

Q

F

F

V

V

V

L

I

C

I

I

L

F

G

A

A

T

T
x
Y

D

D

R

E

R

R

A

R

P

N

P

G

G

R

L

L

A

G

P

S

V

V

-

A

-

L

A

A

I

V

G

G

L

F

A

S

L

L

T

T

L

L

I

G

H

H

L

L

I

F

S

G

I

M

P

Y

V

Y

T

T

N

G

T

A

S

G

V

M

N

N

P

P

A

A

R

R

S

S

T

F

G

A

P

P

A

A

L

I

I

L

V

T

G

R

G

N

W

F

A

T

I

N

Q

H

Q

-

L

-

W

W

M

V

F

Y

W

W

L

V

A

G

P

P

I

V

L

I

G

G

A

A

V

G

I

L

G

G

G

S

V

L

T

L

Y

Y

R

D

W

F

L

L

Y149 (≠ T154) 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

P43286 Aquaporin PIP2-1; Plasma membrane intrinsic protein 2-1; AtPIP2;1; Plasma membrane intrinsic protein 2a; PIP2a from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
32% identity, 83% coverage: 35:227/233 of query aligns to 77:269/287 of P43286

query
sites
P43286

G

G

I

V

G

G

L

I

L

L

G

G

V

I

S

A

L

W

A

A

F

F

G

G

L

G

T

M

V

I

L

F

T

I

M

L

A

V

F

Y

A

C

I

T

G

A

H

G

I

I

S

S

G

G

C

G

H

H

L

I

N

N

P

P

A

A

V

V

S

T

V

F

G

G

L

L

V

F

V

L

G

A

G

R

R

K

F

V

P

S

A

L

R

P

E

R

L

A

P

L

A

L

Y

Y

I

I

V

I

A

A

Q

Q

V

C

V

L

G

G

G

A

T

I

I

C

A

G

A

V

A

G

L

-

Y

-

F

F

I

V

A

K

S

A

G

F

K

Q

P

S

G

S

F

Y

E

Y

L

T

A

R

S

Y

G

G

L

G

A

G

S

A

N

N

G

S

Y

L

G

A

E

D

H

-

S

-

P

-

G

-

G

G

Y

Y

S

S

M

T

V

G

A

T

G

G

F

L

V

A

C

A

E

E

L

I

V

I

M

G

T

T

A

F

M

V

F

L

V

V

V

Y

I

T

I

V

L

F

G

S

A

A

T

T

D

D

R

P

R

K

A

R

P

S

-

A

-

R

-

D

-

S

-

H

-

V

P

P

G

V

L

L

A

A

P

P

V

L

A

P

I

I

G

G

L

F

A

A

L

V

T

F

L

M

I

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H

H

L

L

I

A

S

T

I

I

P

P

V

I

T

T

N

G

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T

S

G

V

I

N

N

P

P

A

A

R

R

S

S

T

F

G

G

P

A

A

A

L

V

I

I

V

Y

G

N

G

K

-

S

-

K

-

P

W

W

A

-

I

-

Q

D

L

H

W

W

M

I

F

F

W

W

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G

P

P

I

F

L

I

G

G

A

A

V

A

I

I

G

A

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T

Y

Y

H

R

Q

W

F

L

V

Sites not aligning to the query:

3 modified: N6,N6-dimethyllysine; partial; K→A: 2-fold decrease in water transport activity.; K→R: No effect.
6 E→A: No effect.
280 modified: Phosphoserine; S→A: Normal subcellular localization.
283 modified: Phosphoserine; S→A: Intracellular reticulation pattern, probably corresponding to the endoplasmic reticulum.; S→D: Normal subcellular localization.

P09011 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Rattus norvegicus (Rat) (see 2 papers)
33% identity, 97% coverage: 2:227/233 of query aligns to 6:220/261 of P09011

query
sites
P09011

S

S

L

F

F

W

K

R

R

A

S

I

I

F

T

A

E

E

G

F

L

F

G

A

T

T

F

L

W

F

L

Y

V

V

L

F

G

F

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G

S

S

A

S

V

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L

R

A

W

A

A

A

P

F

G

P

P

A

-

V

-

G

-

I

L

G

H

L

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L

L

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Q

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V

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A

L

L

A

A

F

F

G

G

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L

T

A

V

L

L

A

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M

L

A

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Q

A

T

I

V

G

G

H

H

I

I

S

S

G

G

C

A

H

H

L

V

N

N

P

P

A

A

V

V

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T

V

F

G

A

L

F

V

L

V

V

G

G

G

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R

Q

F

M

P

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A

L

R

L

E

R

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A

P

F

A

C

Y

Y

I

I

V

A

A

A

Q

Q

V

L

G

G

G

A

T

V

I

A

A

G

A

A

L

V

L

L

Y

Y

F

S

I

V

A

T

S

-

G

-

K

P

P

P

G

A

F

-

E

-

L

V

A

R

S

G

G

N

L

L

A

A

S

L

N

N

G

T

Y

L

G

-

E

-

H

-

S

-

P

H

G

A

G

G

Y

V

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M

V

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A

Q

G

A

F

T

V

T

C

V

E

E

L

I

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F

M

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A

L

M

Q

F

F

V

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V

L

I

C

I

I

L

F

G

A

A

T

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Y

D

D

R

E

R

R

A

R

P

N

P

G

G

R

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M

A

G

P

S

V

V

-

A

-

L

A

A

I

V

G

G

L

F

A

S

L

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T

T

L

L

I

G

H

H

L

L

I

F

S

G

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M

P

Y

V

Y

T

T

N

G

T

A

S

G

V

M

N

N

P

P

A

A

R

R

S

S

T

F

G

A

P

P

A

A

L

I

I

L

V

T

G

R

G

N

W

F

A

S

I

N

Q

H

Q

-

L

-

W

W

M

V

F

Y

W

W

L

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A

G

P

P

I

I

L

I

G

G

A

G

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L

G

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S

V

L

T

L

Y

Y

R

D

W

F

L

L

Sites not aligning to the query:

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

Q9SAI4 Aquaporin NIP6-1; NOD26-like intrinsic protein 6-1; AtNIP6;1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
34% identity, 96% coverage: 1:224/233 of query aligns to 76:285/305 of Q9SAI4

query
sites
Q9SAI4

M

V

S

S

L

L

F

Y

K

R

R

K

S

L

I

G

T

A

E

E

G

F

L

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G

G

T

T

F

L

W

I

L

L

V

I

L

F

G

A

G

G

C

T

G

A

S

T

A

A

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I

L

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A

N

A

Q

A

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F

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D

A

G

V

A

G

E

I

T

G

-

L

L

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F
x
A

G

G

L

L

T

A

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M

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M

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A

I

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L

A

S

I

T

G

G

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H

I

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S

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C

A

H

H

L

L

N

N

P

P

A

A

V

V

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T

V

I

G

A

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F

V

A

G

L

G

K

R

H

F

F

P

P

A

W

R

K

E

H

L

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P

P

A

V

Y

Y

I

I

V

G

A

A

Q

Q

V

V

V

M

G

A

G

S

T

V

I

S

A

A

A

F

L

A

L

L

Y

-

F

-

I

-

A

-

S

-

G

-

K

K

P

A

G

V

F

F

E

E

-

P

-

T

L

M

A

S

S

G

G

G

L

V

A

T

S

V

N

P

G

T

Y

V

G

G

E

-

H

-

S

-

P

-

G

-

Y

-

S

-

M

L

V

S

A

Q

G

A

F

F

V

A

C

L

E

E

L

F

V

I

M

I

T

S

-

F

-

N

A

L

M

M

F

F

V

V

I

T

I

A

L

V

G

-

A

A

T

T

D

D

R

T

R

R

A

A

P

V

P

G

G

E

L

L

A

A

P

G

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I

A

A

I

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G

G

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A

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M

L

L

I

N

H

I

L

L

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A

I

G

P

P

V

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T

N

S

T

A

S

S

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M

N

N

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P

A
x
V

R

R

S

T

T

L

G

G

P

P

A

A

L

I

I

A

V

A

G

N

W

Y

A

-

I

-

Q

R

Q

A

L

I

W

W

M

V

F

Y

W

L

L

T

A

A

P

P

I

I

L

L

G

G

A

A

V

L

I

I

G

G

G

A

V

G

T

T

Y

Y

A119 (≠ F45) mutation to W: 6-fold increase in water transport activity, but impaired in urea transport.
V252 (≠ A189) mutation to A: No effect.

Query Sequence

>GFF4011 FitnessBrowser__WCS417:GFF4011
MSLFKRSITEGLGTFWLVLGGCGSAVLAAAFPAVGIGLLGVSLAFGLTVLTMAFAIGHIS
GCHLNPAVSVGLVVGGRFPARELPAYIVAQVVGGTIAAALLYFIASGKPGFELASGLASN
GYGEHSPGGYSMVAGFVCELVMTAMFVVIILGATDRRAPPGLAPVAIGLALTLIHLISIP
VTNTSVNPARSTGPALIVGGWAIQQLWMFWLAPILGAVIGGVTYRWLGKEEPT

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