SitesBLAST

T49 (= T48) mutation T->F,W: Increases uptake of both methylarsenite and methylarsenate and exhibits higher sensitivity to methylarsenite.
V177 (≠ A173) mutation to I: Decreases methylarsenite transport activity and results in higher resistance to methylarsenite. Slight decrease in methylarsenate transport activity.; mutation to R: Increases methylarsenite transport activity, leading to lower resistance to methylarsenite. Nearly complete loss of methylarsenate transport activity.

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)
30% identity, 73% coverage: 6:180/241 of query aligns to 59:261/306 of I1CR68

query
sites
I1CR68

R

R

Q

E

I

F

A

L

G

A

E

E

V

F

I

I

G

G

T

T

A

V

L

I

L

L

L

-

A

-

V

V

V

L

I

L

G

T

S

C

G

G

I

F

M

C

A

A

E

E

R

Q

L

T

A

L

G

H

G

I

N

E

V

E

A

S

V

K

A

S

L

W

L

L

A

T

N

S

T

S

L

F

A

G

T

S

V

-

G

-

G

G

L

L

Y

S

V

V

L

L

I

I

-

G

-

I

E

C

V

V

F

S

G

G

P

H

I

V

S

S

G

G

A

A

H

H

F

L

N

N

P

P

A

A

V

V

S

T

M

I

V

A

M

F

A

C

V

I

K

F

G

S

E

G

L

F

P

P

R

I

Y

R

A

K

L

V

A

P

P

S

Y

Y

I

I

V

T

A

A

Q

Q

L

L

A

L

G

G

A

A

V

F

L

A

G

G

A

A

W

A

L

L

A

L

H

Y

A

I

M

I

F

I

D

E

V

P

S

A

I

I

L

V

Q

Q

L

F

S

D

A

G

K

G

M

Q

R

R

S

Y

-

I

-

L

-

G

-

E

-

K

-

S

-

T

-

A

-

G

-

I

-

F

-

G

-

T

-

Y

-

P

-

L

-

Y

-

V

G

G

P

I

G

G

Q

S

W

A

I

I

A

A

-

S

E

E

A

I

V

M

A

G

T

T

A

A

G

M

L

L

I

L

L

L

V

V

I

I

L

M

-

V

-

T

-

G

-

H

-

P

-

N

-

L

-

P

-

Y

R

K

A

S

P

A

D

Q

G

G

R

A

A

M

P

I

A

A

M

L

V

G

A

I

S

T

Y

T

I

I

G

S

A

L

A

C

Y

I

W

G

F

Y

T

T

A

S

S

G

T

F

S

S

F

L

A

-

N

N

P

P

A

A

A

R

A

D

F

F

G

G

-

P

R

R

M

L

F

F

S

T

Sites not aligning to the query:

275 H→A: Affects pH sensing; when associated with A-85.

3nkaA Crystal structure of aqpz h174g,t183f (see paper)
31% identity, 60% coverage: 6:150/241 of query aligns to 5:161/230 of 3nkaA

query
sites
3nkaA

R

R

Q

K

I

L

A

A

G

A

E

E

V

C

I

F

G

G

T

T

A

F

L

W

L

L

L

V

A

F

V

G

I

C

G

G

S

S

G
x
A

I

V

M

L

A

A

E

A

R

G

L

F

A

P

G

E

G

L

N

G

V

I

A

G

V

F

A

A

L

G

L
x
V

A

A

N

L

T

A

L

F

A

-

T

-

V

-

G

-

G

G

L

L

Y

T

V

V

L

L

I

T

E

M

V

A

F

F

-

A

-

V

G

G

P

H

I

I

S

S

G

G

A

G

H

H

F

F

N

N

P

P

A

A

V

V

S

T

M

I

V

G

M

L

A

W

V

A

K

G

G

G

E

R

L

F

P

P

R

A

Y

K

A

E

L

V

A

V

P

G

Y

Y

I

V

V

I

A

A

Q

Q

L

V

A

V

G

G

A

G

V

I

L

V

G

A

A

A

W

A

L

L

A

L

H

Y

A

L

M

I

-

A

-

S

-

G

-

K

-

T

-

G

F

F

D

D

V

A

S

A

I

A

L

S

Q

G

L

F

S

A

A

S

K

N

-

G

-

Y

M

G

R

E

S

H

G

S

P

P

G

G

Q

G

W

Y

-

S

-

M

-

L

-

S

-

A

-

L

I

V

A

V

E

E

A

L

V

V

A

L

T

S

A

A

G

G

L

F

I

L

L

L

V

V

I

I

L

H

R

G

A

A

P

T

D

D

G

K

R

F

A

A

P

P

A

A

binding glycerol: A25 (≠ G26), V41 (≠ L42)

Sites not aligning to the query:

binding glycerol: 180, 184

P60844 Aquaporin Z; Bacterial nodulin-like intrinsic protein; Water channel AqpZ from Escherichia coli (strain K12) (see paper)
31% identity, 60% coverage: 6:150/241 of query aligns to 3:159/231 of P60844

query
sites
P60844

R

R

Q

K

I

L

A

A

G

A

E

E

V
x
C

I

F

G

G

T

T

A

F

L

W

L

L

L

V

A

F

V

G

I
x
C

G

G

S

S

G

A

I

V

M

L

A

A

E

A

R

G

L

F

A

P

G

E

G

L

N

G

V

I

A

G

V

F

A

A

L

G

L

V

A

A

N

L

T

A

L

F

A

-

T

-

V

-

G

-

G

G

L

L

Y

T

V

V

L

L

I

T

E

M

V

A

F

F

-

A

-

V

G

G

P

H

I

I

S

S

G

G

A

G

H

H

F

F

N

N

P

P

A

A

V

V

S

T

M

I

V

G

M

L

A

W

V

A

K

G

G

G

E

R

L

F

P

P

R

A

Y

K

A

E

L

V

A

V

P

G

Y

Y

I

V

V

I

A

A

Q

Q

L

V

A

V

G

G

A

G

V

I

L

V

G

A

A

A

W

A

L

L

A

L

H

Y

A

L

M

I

-

A

-

S

-

G

-

K

-

T

-

G

F

F

D

D

V

A

S

A

I

A

L

S

Q

G

L

F

S

A

A

S

K

N

-

G

-

Y

M

G

R

E

S

H

G

S

P

P

G

G

Q

G

W

Y

-

S

-

M

-

L

-

S

-

A

-

L

I

V

A

V

E

E

A

L

V

V

A

L

T

S

A

A

G

G

L

F

I

L

L

L

V

V

I

I

L

H

R

G

A

A

P

T

D

D

G

K

R

F

A

A

P

P

A

A

C9 (≠ V12) mutation to S: No effect.
C20 (≠ I23) mutation to S: Loss of oligomerization; no alteration of water permeability.

Sites not aligning to the query:

183 T→C: No effect.
189 mutation R->V,S: Loss of function.

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)
30% identity, 76% coverage: 4:186/241 of query aligns to 47:236/298 of Q6Z2T3

query
sites
Q6Z2T3

L

L

P

L

R

K

Q

K

I

V

A

V

G

S

E

E

V

V

I

V

G

A

T

T

A

F

L

L

L

V

A

F

V

M

V

T

I

C

G

G

S

A

-

A

G

G

I

I

M

S

A

G

E

S

R

D

L

L

A

S

G

-

N

-

V

-

A

R

V

I

A

S

L

Q

L

L

A

G

N

Q

T

S

L

I

A

A

T

-

V

-

G

G

L

L

Y

I

V

V

L

T

I

V

E

M

V

I

F

Y

-

A

-

V

G

G

P

H

I

I

S

S

G

G

A

A

H

H

F

M

N

N

P

P

A

A

V

V

S

T

M

L

V

A

M

F

A

A

V

V

K

F

G

R

E

H

L

F

P

P

R

W

Y

I

A

Q

L

V

A

P

P

F

Y

Y

I

W

V

A

A
|
A

Q

Q

L

F

A

T

G

G

A

A

V

I

L

C

G

A

A

S

W

F

L

V

A

L

H

K

A

A

M

V

F

I

D

H

-

P

V

V

S

D

I

V

L

I

Q

G

L

T

S

T

A

T

K

P

M

V

R

-

S

-

G

G

P

P

G

-

Q

H

W

W

-

H

-

S

-

L

I

V

A

V

E

E

A

V

V

I

A

V

T

T

A

F

G

N

L

M

I

M

L

F

V

V

I

T

L

L

R

A

-

V

A

A

P

T

D

D

G

T

R

R

A

A

P

V

A

G

M

E

V

L

A

A

S

G

Y

L

-

A

I

V

G

G

A

S

A

A

Y

V

W

C

F

I

T

T

A

S

-

I

-

F

-

A

-

G

-

A

-

I

S

S

T

G

S

G

F

S

A

M

N

N

P

P

A

A

A

R

A

T

F

L

G

G

-

P

R

A

M

L

F

A

S

S

N

N

S

K

F

F

A

D

G

G

I

L

A132 (= A92) mutation to T: In lsi; impairs silicon uptake. Grain discoloration. Reduces grain yield 10-fold.

P37451 Propanediol uptake facilitator PduF from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
33% identity, 44% coverage: 4:109/241 of query aligns to 5:107/264 of P37451

query
sites
P37451

L

L

P

K

R

A

Q

Q

I

C

A

G

G

A

E

E

V

F

I

L

G

G

T

T

A

G

L

L

L

F

L

L

A

F

V

F

V

G

I

I

G

G

S

C

G

-

I

L

M

S

A

A

E

L

R

K

L

V

A

A

G

G

G

A

N

S

V

L

A

G

V

L

A

W

L

-

A

-

N

-

T

E

L

I

A

C

T

I

V

I

G

W

G

G

L

L

Y

G

V

I

L

S

I

L

E

A

V

V

F

Y

-

L

-

T

G

A

P

G

I

I

S

S

G

G

A

G

H

H

F

L

N
|
N

P
|
P

A
|
A

V

V

S

T

M

I

V

A

M

L

A

W

V

L

K

F

G

A

E

C

L

F

P

P

R

K

Y

Q

A

K

L

V

A

L

P

P

Y

Y

I

I

V

I

A

A

Q

Q

L

F

A

A

G

G

A

A

V

F

L

G

G

G

A

A

W

L

L

L

A

A

H

Y

A

V

M

L

F

Y

D

S

NPA 66:68 (= NPA 68:70) NPA 1

Sites not aligning to the query:

201:203 NPA 2

P08995 Nodulin-26; N-26 from Glycine max (Soybean) (Glycine hispida) (see paper)
35% identity, 40% coverage: 52:148/241 of query aligns to 81:180/271 of P08995

query
sites
P08995

L

L

Y

T

V

V

L

L

I

V

E

Y

V

T

F

V

G

G

P

H

I

I

S

S

G

G

A

G

H

H

F

F

N

N

P

P

A

A

V

V

S

T

M

I

V

A

M

F

A

A

V

S

K

T

G

R

E

R

L

F

P

P

R

L

Y

I

A

Q

L

V

A

P

P

A

Y

Y

I

V

V

V

A

A

Q

Q

L

L

A

L

G

G

A

S

V

I

L

L

G

A

A

S

W

G

L

T

A

L

H

R

A

L

M

L

F

F

D

M

V

G

S

N

I

H

L

D

Q

Q

L

F

S

S

A

G

K

T

M

V

R

P

S

N

G

G

P

T

G

N

-

L

-

Q

Q

A

W

F

I

V

A

F

E

E

A

F

V

I

A

M

T

T

A

F

G

F

L

L

I

M

L

F

V

V

I

I

L

C

-

G

R

V

A

A

P

T

D

D

G

N

R

R

A

A

Sites not aligning to the query:

262 modified: Phosphoserine; by CPK

2o9eA Crystal structure of aqpz mutant t183c complexed with mercury (see paper)
31% identity, 60% coverage: 6:150/241 of query aligns to 5:161/232 of 2o9eA

query
sites
2o9eA

R

R

Q

K

I

L

A

A

G

A

E

E

V

S

I

F

G

G

T

T

A

F

L

W

L

L

L

V

A

F

V

G

I

S

G

G

S

S

G

A

I

V

M

L

A

A

E

A

R

G

L

F

A

P

G

E

G

L

N

G

V

I

A

G

V

F

A

A

L

G

L

V

A

A

N

L

T

A

L

F

A

-

T

-

V

-

G

-

G

G

L

L

Y

T

V

V

L

L

I

T

E

M

V

A

F

F

-

A

-

V

G

G

P

H

I

I

S

S

G

G

A

G

H

H

F

F

N

N

P

P

A

A

V

V

S

T

M

I

V

G

M

L

A

W

V

A

K

G

G

G

E

R

L

F

P

P

R

A

Y

K

A

E

L

V

A

V

P

G

Y

Y

I

V

V

I

A

A

Q

Q

L

V

A

V

G

G

A

G

V

I

L

V

G

A

A

A

W

A

L

L

A

L

H

Y

A

L

M

I

-

A

-

S

-

G

-

K

-

T

-

G

F

F

D

D

V

A

S

A

I

A

L

S

Q

G

L

F

S

A

A

S

K

N

-

G

-

Y

M

G

R

E

S

H

G

S

P

P

G

G

Q

G

W

Y

-

S

-

M

-

L

-

S

-

A

-

L

I

V

A

V

E
|
E

A

L

V

V

A

L

T

S

A

A

G

G

L

F

I

L

L

L

V

V

I

I

L

H

R

G

A

A

P

T

D

D

G

K

R

F

A

A

P

P

A

A

binding mercury (ii) ion: E140 (= E129)

Sites not aligning to the query:

binding mercury (ii) ion: 179

O94778 Aquaporin-8; AQP-8 from Homo sapiens (Human) (see 4 papers)
40% identity, 40% coverage: 11:107/241 of query aligns to 41:131/261 of O94778

query
sites
O94778

E

E

V

L

I

L

G

G

T

S

A

A

L

L

L
x
F

L

-

A

-

V

I

V

F

I

I

G

G

S
x
C

G

L

I

S

M

V

A

I

E

E

R

N

L

-

A

-

G

-

N

G

V

T

A

D

V

T

A

G

L

L

A

Q

N

P

T

A

L

L

A

A

T
x
H

V

G

G

L

G

A

L

L

Y

G

V

L

L

V

I

I

E

A

V

T

F

L

G

G

P

N

I

I

S

S

G

G

A

G

H

H

F

F

N

N

P

P

A

A

V

V

S

S

M

L

V

A

M

A

A

M

V

L

K

I

G

G

E

G

L

L

P

N

R

L

Y

V

A

M

L

L

A

L

P

P

Y

Y

I

W

V

V

A

S

Q

Q

L

L

A

L

G

G

A

G

V

M

L

L

G

G

A

A

W

A

L

L

A

A

H

K

A

A

M

V

F48 (≠ L18) mutation to A: Loss of hydrogen peroxide transport activity under stress condition.
C53 (≠ S25) modified: Cysteine persulfide; modified: Cysteine sulfenic acid (-SOH); mutation to S: Does not affect hydrogen peroxide transport under stress condition.
H72 (≠ T48) 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.
38 C→S: Does not affect loss of hydrogen peroxide transport after stress.
173 C→A: Loss of hydrogen peroxide transporter activity.; C→S: Slightly affect hydrogen peroxide transport after stress.
208 C→S: Does not affect loss of hydrogen peroxide transport after stress.
213 R→A: Does not affect hydrogen peroxide transport activity under stress condition.
229 I → M: in a breast cancer sample; somatic mutation
247 C→S: Does not affect loss of hydrogen peroxide transport after stress.

B1VB61 Propanediol uptake facilitator PduF from Citrobacter freundii (see paper)
34% identity, 44% coverage: 4:108/241 of query aligns to 5:106/269 of B1VB61

query
sites
B1VB61

L

L

P

K

R

A

Q

Q

I

C

A

I

G

A

E

E

V

F

I

L

G

G

T

T

A

G

L

L

L

F

L

L

A

F

V

F

V

G

I

I

G

G

S

C

G

-

I

L

M

S

A

A

E

L

R

K

L

V

A

A

G

G

G

A

N

S

V

L

A

G

V

L

A

W

L

-

A

-

N

-

T

E

L

I

A

C

T

I

V

I

G

W

G

G

L

L

Y

G

V

I

L

S

I

L

E

A

V

V

F

Y

-

L

-

T

G

A

P

G

I

I

S

S

G

G

A

A

H

H

F

L

N
|
N

P
|
P

A
|
A

V

I

S

T

M

I

V

A

M

L

A

W

V

L

K

F

G

A

E

C

L

F

P

P

R

G

Y

R

A

K

L

V

A

L

P

P

Y

Y

I

T

V

V

A

A

Q

Q

L

V

A

A

G

G

A

A

V

F

L

G

G

G

A

A

W

L

L

L

A

A

H

Y

A

L

M

L

F

Y

NPA 66:68 (= NPA 68:70) NPA 1

Sites not aligning to the query:

201:203 NPA 2

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)
35% identity, 49% coverage: 6:124/241 of query aligns to 39:157/287 of P43286

query
sites
P43286

R

R

Q

A

I

V

A

I

G

A

E

E

V

F

I

V

G

A

T

T

A

L

L

L

L

F

L

L

A

Y

V

I

-

T

-

V

-

L

-

T

V

V

I

I

G

G

S

Y

G

K

I

I

M

Q

A

S

E

D

R

T

L

D

A

A

G

G

N

V

V

D

A

C

-

G

V

V

A

G

L

I

L

L

A

G

N

I

T

A

L

W

A

A

T

F

V

G

G

G

G

M

L

I

Y

F

V

I

L

L

I

V

E

Y

V

C

F

T

G

A

P

G

I

I

S

S

G

G

A

G

H

H

F

I

N

N

P

P

A

A

V

V

S

T

-

F

-

G

M

L

V

F

M

L

A

A

V

R

K

K

G

V

E

S

L

L

P

P

R

R

Y

A

A

L

L

L

A

-

P

-

Y

Y

I

I

V

I

A

A

Q

Q

L

C

A

L

G

G

A

A

V

I

L

C

G

G

A

V

W

G

L

F

A

V

H

K

A

A

M

-

F

-

D

-

V

-

S

-

I

-

L

F

Q

Q

L

S

S

S

A

Y

K

Y

M

T

R

R

S

Y

G

G

P

G

G

G

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.

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)
32% identity, 68% coverage: 51:213/241 of query aligns to 51:223/271 of P56402

query
sites
P56402

G

G

L

I

Y

G

V

T

L

L

I

V

E

Q

V

A

F

L

G

G

P

H

I

V

S

S

G

G

A

A

H

H

F

I

N

N

P

P

A

A

V

V

S

T

M

V

V

A

M

C

A

L

V

V

K

G

G

C

E

H

L

V

P

S

R

F

Y

L

A

R

L

A

A

A

P

F

Y

Y

I

V

V

A

A

A

Q

Q

L

L

A

L

G

G

A

A

V

V

L

A

G

G

A

A

W

A

L

I

A

L

H

H

A

E

M

I

F

T

D

P

V

V

S

E

I

I

-

R

-

G

-

D

L

L

Q

A

L

V

S

N

A

A

K

L

M

H

R

N

S

N

G

A

P
x
T

-

A

G

G

Q

Q

W

A

I

V

A

T

-

V

E

E

A

L

V

F

A

L

T

T

A

M

G

Q

L

L

I

V

L

L

V

C

I

I

L

F

R

A

A

S

P

T

D

D

G

E

R

R

-

R

-

S

-

D

-

N

-

L

-

G

A

S

P

P

A

A

M

L

V

S

A

I

S

G

Y

F

-

S

-

V

-

T

I

L

G

G

A

H

-

L

A

G

Y

I

W

Y

F

F

T

T

A

G

S

C

T

S

S

-

F

-

A

M

N

N

P

P

A

A

A

R

A

S

F

-

G

-

R

-

M

-

F

-

S

-

N

-

S

-

F

-

A

-

G

-

I

L

A

A

P

P

A

A

S

V

V

V

P

T

G

G

-

K

-

F

-

D

-

H

-

W

-

V

F

F

V

W

L

I

A

G

E

P

L

L

L

V

G

G

A

A

C

V

I

I

G

G

L

S

L

L

H

Y

T

N

A

Y

L

L

T126 (≠ P123) 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)
35% identity, 40% coverage: 51:147/241 of query aligns to 50:151/239 of 4nefA

query
sites
4nefA

G

G

L

I

Y

G

V

T

L

L

I

V

E

Q

V

A

F

L

G

G

P

H

I

I

S

S

G

G

A

A

H

H

F

I

N

N

P

P

A

A

V

V

S

T

M

V

V

A

M
x
C

A

L

V

V

K

G

G

C

E
x
H

L

V

P

S

R

V

Y

L

A

R

L

A

A

A

P

F

Y

Y

I

V

V

A

A

A

Q

Q

L

L

A

L

G

G

A

A

V

V

L

A

G

G

A

A

W

A

L

L

A

L

H

H

A

E

M

I

F

T

-

P

-

A

-

D

-

I

-

R

-

G

D

D

V

L

S

A

I

V

L

N

Q

A

L

L

S

S

A

N

K

S

M

T

R

T

S

A

G

G

P

Q

G

A

Q

V

W

T

I

V

A

-

E

E

A

L

V

F

A

L

T

T

A

L

G

Q

L

L

I

V

L

L

V

C

I

I

L

F

R

A

A

S

P

T

D

D

G

E

R

R

binding zinc ion: C74 (≠ M75), H79 (≠ E80)

Q96PS8 Aquaporin-10; AQP-10; Aquaglyceroporin-10; Small intestine aquaporin from Homo sapiens (Human) (see 2 papers)
36% identity, 39% coverage: 4:97/241 of query aligns to 20:111/301 of Q96PS8

query
sites
Q96PS8

L

L

P

A

R

R

Q

Q

I

C

A

L

G

A

E
|
E

V

F

I

L

G

G

T

V

A

F

L

V

L

L

L

M

A

-

V

-

V

L

I

L

G

T

S

Q

G

G

I

A

M

V

A

A

E

Q

R

A

L

V

A

T

G

S

G

G

-

E

-

T

-

K

-

G

N

N

V

F

A

F

V

T

A

M

L

F

L

L

A

A

N

G

T

S

L

L

A

A

T

V

V

T

G

I

G

A

L

I

Y

Y

V

V

L

-

I

-

E

-

V

-

F
x
G

G

G

P

N

I

V

S
|
S

G

G

A

A

H
|
H

F

L

N

N

P

P

A

A

V
x
F

S

S

M

L

V

A

M

M

A

C

V

I

K

V

G

G

E
x
R

L

L

P

P

R

W

Y

V

A

K

L

L

A

P

P

I

Y

Y

I

I

V

L

A

V

Q

Q

L

L

A

L

G

S

A

A

E27 (= E11) mutation to Q: Abolishes permeability to glycerol.
G73 (≠ F59) 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 (≠ E80) mutation to A: Abolishes permeability to glycerol.

Sites not aligning to the query:

133 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→Q: Abolishes N-glycosylation.

6f7hC Crystal structure of human aqp10 (see paper)
36% identity, 39% coverage: 4:97/241 of query aligns to 5:96/253 of 6f7hC

query
sites
6f7hC

L

L

P

A

R

R

Q

Q

I

C

A

L

G

A

E

E

V

F

I

L

G

G

T

V

A

F

L

V

L

L

L

M

A

-

V

-

V

L

I

L

G

T

S

Q

G

G

I

A

M

V

A

A

E

Q

R

A

L

V

A

T

G

S

G

G

-

E

-

T

-

K

-

G

N

N

V

F

A

F

V

T

A

M

L

F

L

L

A

A

N

G

T

S

L

L

A

A

T

V

V

T

G

I

G

A

L
x
I

Y

Y

V

V

L

-

I

-

E

-

V

-

F

G

G

G

P

N

I

V

S

S

G

G

A

A

H

H

F

L

N

N

P

P

A

A

V

F

S

S

M

L

V

A

M

M

A

C

V

I

K

V

G

G

E

R

L

L

P

P

R

W

Y

V

A

K

L

L

A

P

P

I

Y

Y

I

I

V

L

A

V

Q

Q

L

L

A

L

G

S

A

A

binding glycerol: I55 (≠ L52)

Sites not aligning to the query:

binding glycerol: 199

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)
30% identity, 68% coverage: 51:213/241 of query aligns to 51:223/271 of P41181

query
sites
P41181

G

G

L

I

Y

G

V

T

L

L

I

V

E

Q

V

A

F

L

G

G

P

H

I

I

S

S

G
|
G

A

A

H

H

F

I

N

N

P

P

A

A

V

V

S

T

M

V

V

A

M

C

A

L

V

V

K
x
G

G
x
C

E

H

L

V

P

S

R

V

Y

L

A

R

L

A

A

A

P

F

Y

Y

I

V

V

A

A

A

Q

Q

L

L

A

L

G

G

A

A

V

V

L

A

G

G

A

A

W

A

L

L

A

L

H

H

A

E

M

I

F

T

-

P

-

A

-

D

-

I

-

R

-

G

D

D

V

L

S

A

I

V

L

N

Q

A

L

L

S

S

A

N

K

S

M

T

R

T

S

A

G

G

P

Q

G

A

Q

V

W

T

I

V

A

-

E

E

A

L

V

F

A

L

T

T

A

L

G

Q

L

L

I

V

L

L

V

C

I

I

L

F

R

A

A
x
S

P

T

D

D

-

E

-

R

G

G

R

E

A

N

P

P

A

G

M

T

V

P

A

A

S

L

Y

S

I

I

G

G

A

F

A

-

Y

-

W

-

F

-

T

-

A

-

S

-

T

-

S

-

F

-

A

-

N

-

P

-

A

S

A

V

A

A

F

L

G

G

R

H

M

L

F

L

S

G

N

I

S

H

F

Y

A

T

G

G

-

C

-

S

-

M

-

N

-

P

-

A

-
x
R

-

S

I

L

A
|
A

P

P

A

A

S

V

V
|
V

P

T

G

G

-

K

-

F

-

D

-

H

-

W

-

V

F

F

V

W

L

I

A

G

E

P

L

L

L

V

G

G

A

A

C

I

I

L

G

G

L
x
S

L
|
L

L

L

H

Y

T

N

A
x
Y

L

V

L

L

G64 (= G64) to R: in NDI2; loss of water channel activity; dbSNP:rs104894326
G78 (≠ K78) mutation to A: Does not affect interaction with MIAC; when associated with A-79.
C79 (≠ G79) mutation to A: Does not affect interaction with MIAC; when associated with A-78.
S148 (≠ A143) 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 (vs. gap) to C: in NDI2; loss of water channel activity; mutant protein does not fold properly; dbSNP:rs104894328
A190 (= A187) to T: in NDI2; mutant protein does not fold properly and is not functional; dbSNP:rs104894341
V194 (= V191) to I: in dbSNP:rs772051028
S216 (≠ L206) to P: in NDI2; loss of water channel activity; dbSNP:rs104894329
L217 (= L207) mutation to A: Abolishes interaction with MIAC; when associated with A-221.
Y221 (≠ A211) 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.

Q9SAI4 Aquaporin NIP6-1; NOD26-like intrinsic protein 6-1; AtNIP6;1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 46% coverage: 2:112/241 of query aligns to 76:183/305 of Q9SAI4

query
sites
Q9SAI4

I

V

G

S

L

L

P

Y

R

R

Q

K

I

L

A

G

G

A

E

E

V

F

I

V

G

G

T

T

A

L

L

I

L

L

L

I

A

F

V

A

V

G

I

T

G

A

S

T

G

A

I

I

M

V

A

N

E

Q

R

K

L

T

A

D

G

G

G

A

N

E

V

T

A

L

V

I

A

G

L

C

L

A

A

A

N

S

T

-

L

-

A

-

T

-

V

-

G
x
A

G

G

L

L

Y

A

V

V

L

M

I

I

E

V

V

I

F

L

-

S

-

T

G

G

P

H

I

I

S

S

G

G

A

A

H

H

F

L

N

N

P

P

A

A

V

V

S

T

M

I

V

A

M

F

A

A

V

A

K

L

G

K

E

H

L

F

P

P

R

W

Y

K

A

H

L

V

A

P

P

V

Y

Y

I

I

V

G

A

A

Q

Q

L

V

A

M

G

A

A

S

V

V

L

S

G

A

A

A

W

F

L

A

A

L

H

K

A

A

M

V

F

F

D

E

V

P

S

T

I

M

A119 (≠ G50) mutation to W: 6-fold increase in water transport activity, but impaired in urea transport.

Sites not aligning to the query:

252 V→A: No effect.

P55088 Aquaporin-4; AQP-4; Mercurial-insensitive water channel; MIWC; WCH4 from Mus musculus (Mouse) (see 2 papers)
26% identity, 51% coverage: 55:176/241 of query aligns to 84:219/323 of P55088

query
sites
P55088

L

M

I

V

E

Q

V

C

F

F

G

G

P

H

I

I

S

S

G

G

A

G

H

H

F

I

N

N

P

P

A

A

V

V

S

T

M

V

V

A

M

M

A

V

V

C

K

T

G

R

E

K

L

I

P
x
S

R

I

Y

A

A

K

L

S

A

V

P

F

Y

Y

I

I

V

I

A

A

Q

Q

L

C

A

L

G

G

A

A

V

I

L

I

G

G

A

A

W

G

L

I

A

L

H

Y

A

L

M

V

F

T

D

P

V

P

S

S

I

V

L

V

-

G

-

L

-

G

-

V

-

T

Q

T

L

V

S

H

A

G

K

N

M

L

R

T

S

A

G

G

P

H

G

G

Q

L

W

-

I

L

A

V

E

E

A

L

V

I

A

I

T

T

A

F

G

Q

L

L

I

V

L

F

V

T

I

I

L

F

R

A

A

S

P

C

D

D

G

S

R

K

A

R

P

T

A

D

M

V

V

T

A

G

S

S

Y

I

-

A

-

L

-

A

-

I

-

G

-

F

-

S

-

V

-

A

I

I

G

G

A

H

A

L

Y

F

W

A

F

I

T

N

A

Y

S

T

T

G

S

A

F

S

A

M

N

N

P

P

A

A

A

R

A

S

F

F

G

G

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

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)
24% identity, 93% coverage: 6:230/241 of query aligns to 10:247/247 of 8ct2D

query
sites
8ct2D

R

R

Q

A

I

V

A

V

G

A

E

E

V

F

I

L

G

A

T

T

A

T

L

L

L

F

L

V

A

F

V

I

V

S

I

I

G

G

S

S

G

A

I

-

M

L

A

G

E

F

R

K

L

Y

A

P

G

V

G

G

N

N

V

N

A

Q

V

T

A

A

L

V

L

Q

A

D

N

N

T

V

L

K

A

V

T

S

V

L

G

A

-

F

G

G

L

L

Y

S

V

I

-

A

-

T

L

L

I

A

E

Q

V

S

F

V

G

G

P

H

I

I

S

S

G

G

A

A

H

H

F

L

N

N

P

P

A

A

V

V

S

T

M

L

V

G

M

L

A

L

V

L

K

S

G

C

E

Q

L

I

P

S

R

I

Y

F

A

R

L

A

A

L

P

M

Y

Y

I

I

V

I

A

A

Q

Q

L

C

A

V

G

G

A

A

V

I

L

V

G

A

A

T

W

A

L

I

A

L

H

S

A

G

M

I

F

T

-

S

-

L

-

T

-

G

-

N

D

S

V

L

S

G

I

R

L

N

Q

D

L

L

S

A

A

D

K

G

M

V

R

N

S

S

G
|
G

P

Q

G

G

Q

L

W
x
G

I

I

A

-

E

E

A

I

V

I

A

G

T

T

A

L

G

Q

L

L

I

V

L

L

V

C

I

V

L

L

R

A

A

T

P

T

D

D

G

R

R

R

-

R

-

D

-

L

-

G

-

S

A

A

P

P

A

L

M

A

V

I

A

G

S

L

Y

S

I

V

G

A

A

L

A

G

Y

H

W

L

F

L

T

A

A

I

S

D

T

Y

S

T

F

G

A

C

-

G

-

I

N

N

P

P

A

A

A

R

A

S

F

F

G

G

-

S

-

A

-

V

-

I

-

T

R

H

M

N

F

F

S

S

N

N

S

H

F

W

A

I

G

-

I

-

A

-

P

-

A

-

S

-

V

-

P

-

G

-

F

F

V

W

L

V

A

G

E

P

L

F

L

I

G

G

A

G

C

A

I

L

G

A

L

V

L

L

L

I

H

Y

T

D

A

F

L

I

L

L

-

A

P

P

R

R

V

S

Q

S

E

D

Q

L

G

T

H

D

P

R

N

V

V

K

I

V

E

W

A

T

S

S

G

G

Q

Q

binding cholesterol: G134 (= G122), G138 (≠ W126)

P47863 Aquaporin-4; AQP-4; Mercurial-insensitive water channel; MIWC; WCH4 from Rattus norvegicus (Rat) (see 4 papers)
26% identity, 51% coverage: 55:176/241 of query aligns to 84:219/323 of P47863

query
sites
P47863

L

M

I

V

E

Q

V

C

F

F

G

G

P

H

I

I

S

S

G

G

A

G

H

H

F

I

N

N

P

P

A

A

V

V

S

T

M

V

V

A

M

M

A

V

V

C

K

T

G

R

E

K

L

I

P

S

R

I

Y

A

A

K

L

S

A

V

P

F

Y

Y

I

I

V

T

A

A

Q

Q

L

C

A

L

G

G

A

A

V

I

L

I

G

G

A

A

W

G

L

I

A

L

H

Y

A

L

M

V

F

T

D

P

V

P

S

S

I

V

L

V

-

G

-

L

-

G

-

V

-

T

Q

T

L

V

S

H

A

G

K

N

M

L

R

T

S

A

G

G

P

H

G

G

Q

L

W

-

I

L

A

V

E

E

A

L

V

I

A

I

T

T

A

F

G

Q

L

L

I

V

L

F

V

T

I

I

L

F

R

A

A

S

P

C

D

D

G
x
S

R

K

A

R

P

T

A

D

M

V

V

T

A

G

S

S

Y

V

-

A

-

L

-

A

-

I

-

G

-

F

-

S

-

V

-

A

I

I

G

G

A
x
H

A

L

Y

F

W

A

F

I

T

N

A

Y

S

T

T

G

S

A

F

S

A

M

N

N

P

P

A

A

A

R

A

S

F

F

G

G

S180 (≠ G146) modified: Phosphoserine; by PKC; mutation to A: Decreases internalization from the cell membrane in response to PKC activation.
H201 (≠ A158) 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

>RR42_RS29350 FitnessBrowser__Cup4G11:RR42_RS29350
MIGLPRQIAGEVIGTALLLAVVIGSGIMAERLAGGNVAVALLANTLATVGGLYVLIEVFG
PISGAHFNPAVSMVMAVKGELPRYALAPYIVAQLAGAVLGAWLAHAMFDVSILQLSAKMR
SGPGQWIAEAVATAGLILVILRAPDGRAPAMVASYIGAAYWFTASTSFANPAAAFGRMFS
NSFAGIAPASVPGFVLAELLGACIGLLLHTALLPRVQEQGHPNVIEASGQQEDSPATGGH
I

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