SitesBLAST

T49 (= T47) mutation T->F,W: Increases uptake of both methylarsenite and methylarsenate and exhibits higher sensitivity to methylarsenite.
V177 (= V175) 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.

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)
30% identity, 95% coverage: 5:215/221 of query aligns to 10:229/247 of 8ct2D

query
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8ct2D

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binding cholesterol: G134 (= G125), G138 (≠ A129)

P30302 Aquaporin PIP2-3; Plasma membrane intrinsic protein 2-3; AtPIP2;3; Plasma membrane intrinsic protein 2c; PIP2c; RD28-PIP; TMP2C; Water stress-induced tonoplast intrinsic protein; WSI-TIP from Arabidopsis thaliana (Mouse-ear cress) (see paper)
33% identity, 70% coverage: 2:156/221 of query aligns to 34:208/285 of P30302

query
sites
P30302

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Sites not aligning to the query:

223 T→C: Creates some mercury-sensitivity.

P43287 Aquaporin PIP2-2; Plasma membrane intrinsic protein 2-2; AtPIP2;2; Plasma membrane intrinsic protein 2b; PIP2b; TMP2b from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
33% identity, 70% coverage: 2:156/221 of query aligns to 34:208/285 of P43287

query
sites
P43287

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R194 (vs. gap) mutation to A: Reduced sensitivity to cytosolic acidification. Insensitive to cytosolic acidification; when associated with A-197.
D195 (≠ G143) mutation to A: Reduced sensitivity to cytosolic acidification. Insensitive to cytosolic acidification; when associated with A-197.
H197 (= H145) mutation to A: Reduced water transport activity. Reduced sensitivity to cytosolic acidification. Insensitive to cytosolic acidification; when associated with A-194 or A-195.; mutation to D: Reduced water transport activity. Insensitive to cytosolic acidification.; mutation to K: Very low water transport activity. Insensitive to cytosolic acidification.

Sites not aligning to the query:

3 modified: N6,N6-dimethyllysine; partial
264 H→A: No effect.

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)
33% identity, 70% coverage: 2:156/221 of query aligns to 36:210/287 of P43286

query
sites
P43286

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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.

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, 99% coverage: 3:221/221 of query aligns to 47:264/298 of Q6Z2T3

query
sites
Q6Z2T3

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A132 (= A91) mutation to T: In lsi; impairs silicon uptake. Grain discoloration. Reduces grain yield 10-fold.

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)
30% identity, 97% coverage: 1:215/221 of query aligns to 7:223/271 of P56402

query
sites
P56402

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F

V

W

A

I

G

G

Q

P

L

L

A

V

G

G

A

A

I

V

A

I

A

G

L

S

L

L

F

L

F

Y

T

N

W

Y

L

L

T126 (vs. gap) 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

Q9XF58 Aquaporin PIP2-5; Plasma membrane intrinsic protein 2-5; ZmPIP2-5; ZmPIP2;5; ZmPIP2a from Zea mays (Maize) (see paper)
31% identity, 70% coverage: 2:156/221 of query aligns to 34:210/285 of Q9XF58

query
sites
Q9XF58

T

S

L

L

A

Y

R

R

R

A

V

V

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I

A

A

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E

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F

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A

T

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M

L

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L

A

Y

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I

-

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V

-

A

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T

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A

A

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A

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V

L

L

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A

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x
G

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A

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G

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G

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G

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D

E

-

L

-

S

-

A

G

G

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K

G

G

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-

G

-

L

-

A

A

A

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E

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I

A

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F

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L

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A

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-

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L

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A

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L

A

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I

G

G

L

F

G104 (≠ A64) mutation to W: Loss of water transport.

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)
28% identity, 97% coverage: 1:215/221 of query aligns to 7:223/271 of P41181

query
sites
P41181

V

I

T

A

L

F

A

S

R

R

R

A

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M

-

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|
G

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x
S

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R

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G

-

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-

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R

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S

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x
A

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S

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F

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A
x
V

G

T

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G

A

K

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F

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D

A

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G

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L

L

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G

G

A

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I

A

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G

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x
S

L
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L

F

L

F

Y

T

N

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x
Y

L

V

L

L

G64 (= G63) to R: in NDI2; loss of water channel activity; dbSNP:rs104894326
G78 (≠ K77) mutation to A: Does not affect interaction with MIAC; when associated with A-79.
C79 (≠ R78) mutation to A: Does not affect interaction with MIAC; when associated with A-78.
S148 (vs. gap) 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 (= R179) to C: in NDI2; loss of water channel activity; mutant protein does not fold properly; dbSNP:rs104894328
A190 (≠ S182) to T: in NDI2; mutant protein does not fold properly and is not functional; dbSNP:rs104894341
V194 (≠ A186) to I: in dbSNP:rs772051028
S216 (≠ L208) to P: in NDI2; loss of water channel activity; dbSNP:rs104894329
L217 (= L209) mutation to A: Abolishes interaction with MIAC; when associated with A-221.
Y221 (≠ W213) 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.

P23645 Neurogenic protein big brain from Drosophila melanogaster (Fruit fly) (see 3 papers)
30% identity, 80% coverage: 40:215/221 of query aligns to 99:277/696 of P23645

query
sites
P23645

L

L

G

A

N

T

T

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D

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D253 (≠ H191) mutation to N: No effect on transport activity.
E274 (≠ T212) mutation to Q: No effect on transport activity.

Sites not aligning to the query:

46 modified: Phosphoserine
47 modified: Phosphothreonine
71 E→D: Partial loss of transport activity and increased sensitivity to blocking by the magnesium ion.; E→K: Loss of expression in cell membrane.; E→N: Loss of transport activity.; E→Q: Loss of transport activity.
300 modified: Phosphoserine
394 modified: Phosphoserine
576 modified: Phosphoserine

4nefA X-ray structure of human aquaporin 2 (see paper)
28% identity, 97% coverage: 1:215/221 of query aligns to 6:222/239 of 4nefA

query
sites
4nefA

V

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M

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C

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A

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L

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L

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N

W

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L

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L

L

binding zinc ion: C74 (≠ L74), H79 (≠ E79)

Q39196 Probable aquaporin PIP1-4; Plasma membrane intrinsic protein 1-4; AtPIP1;4; Transmembrane protein C; TMP-C from Arabidopsis thaliana (Mouse-ear cress) (see paper)
26% identity, 97% coverage: 2:216/221 of query aligns to 50:279/287 of Q39196

query
sites
Q39196

T

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A

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D

-

A

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K

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A

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D

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R

R

Sites not aligning to the query:

1 modified: N-acetylmethionine

Q08733 Aquaporin PIP1-3; AtPIP1;3; Plasma membrane intrinsic protein 1c; PIP1c; Transmembrane protein B; TMP-B from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 70% coverage: 2:156/221 of query aligns to 49:217/286 of Q08733

query
sites
Q08733

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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

T

T

L

F

T

G

L

L

L

F

L

L

K

A

R

R

E

K

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L

D

S

A

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R

T

T

R

A

A

A

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F

Y

Y

A

I

A

V

A

M

Q

Q

F

C

A

L

G

G

A

A

I

I

L

C

G

G

V

A

W

G

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V

A

V

H

K

A

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M

F

F

Q

A

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E

N

P

P

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Y

L

Q

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T

L

L

S

G

A

G

K

G

A

A

R

N

-

T

-

V

-

A

D

H

G

G

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Y

P

T

Q

K

G

G

L

S

-

G

-

L

-

G

A

A

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E

A

I

V

I

A

G

T

T

F

F

G

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L

L

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C

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A

-

T

-

D

-

A

-

K

-

R

-

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-

A

-

R

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D

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I

A

L

T

A

P

P

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L

A

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I

G

G

L

F

Sites not aligning to the query:

1 modified: N-acetylmethionine

P55088 Aquaporin-4; AQP-4; Mercurial-insensitive water channel; MIWC; WCH4 from Mus musculus (Mouse) (see 2 papers)
29% identity, 77% coverage: 5:174/221 of query aligns to 36:215/323 of P55088

query
sites
P55088

R

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R

A

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V

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S

A

A

E

E

F

F

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A

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S

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-

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-

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A

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A

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N

T

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G

A

A

-

S

-

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N

N

P

P

A

A

S111 (≠ D81) 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)
29% identity, 77% coverage: 5:174/221 of query aligns to 36:215/323 of P47863

query
sites
P47863

R

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R

A

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V

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A

A

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E

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x
S

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x
H

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T

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N

P

P

A

A

S180 (≠ G143) modified: Phosphoserine; by PKC; mutation to A: Decreases internalization from the cell membrane in response to PKC activation.
H201 (≠ Y162) 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

Q9SAI4 Aquaporin NIP6-1; NOD26-like intrinsic protein 6-1; AtNIP6;1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
30% identity, 62% coverage: 1:136/221 of query aligns to 76:209/305 of Q9SAI4

query
sites
Q9SAI4

V

V

T

S

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L

A

Y

R

R

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x
A

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A

-

L

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F

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G

N

L

L

I

M

A119 (≠ T47) 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.

5dyeD Crystal structure of the full length s156e mutant of human aquaporin 5 (see paper)
37% identity, 45% coverage: 1:99/221 of query aligns to 7:100/253 of 5dyeD

query
sites
5dyeD

V

V

T

A

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F

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A

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A

A

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Q

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G

G

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G

G

Sites not aligning to the query:

binding O-[(S)-{[(2S)-2-(hexanoyloxy)-3-(tetradecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-D-serine: 158, 159

P55064 Aquaporin-5; AQP-5 from Homo sapiens (Human) (see 2 papers)
37% identity, 45% coverage: 1:99/221 of query aligns to 8:101/265 of P55064

query
sites
P55064

V

V

T

A

L

F

A

L

R

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G

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x
A

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N
x
I

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Y

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A

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G

G

A

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I

I

L

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G

G

A38 (≠ D36) to E: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123054
I45 (≠ N43) to S: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123055

Sites not aligning to the query:

123 N → D: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123057
156 S→A: No effect on location at the cell membrane.; S→E: Increased location at the cell membrane.
177 I → F: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123056
188 R → C: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs368292687

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)
27% identity, 52% coverage: 5:119/221 of query aligns to 59:171/306 of I1CR68

query
sites
I1CR68

R

R

R

E

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R

Sites not aligning to the query:

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

Q54WT8 Aquaporin-B from Dictyostelium discoideum (Social amoeba) (see paper)
31% identity, 48% coverage: 3:107/221 of query aligns to 45:146/294 of Q54WT8

query
sites
Q54WT8

L

L

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W

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F

F

S75 (≠ N35) modified: carbohydrate, O-linked (GalNAc...) serine
S120 (≠ D81) mutation to A: Permanently unphosphorylated state, impermeable to water in Xenopus oocytes.; mutation to D: Permanently phosphorylated, impermeable to water in Xenopus oocytes.

Sites not aligning to the query:

208:212 mutation Missing: Impermeable to water in Xenopus oocytes.
208:219 Required for water permeability; mutation Missing: Permeable to water in Xenopus oocytes and liposomes, impermeable to glycerol and urea.
239 Selectivity filter
275 D→A: Impermeable to water in Xenopus oocytes.; D→P: Impermeable to water in Xenopus oocytes.

Query Sequence

>Ga0059261_3272 FitnessBrowser__Korea:Ga0059261_3272
VTLARRVIAEFTGTAMLLAIVVGSGIMGERLSGGNDAIALLGNTLATGAGLIVLIQMFGP
ISGAHFNPAVTLTLLLKRESDARTAALYAAAQFAGAILGVWVAHAMFAEPVLQLSAKARD
GLPQGLAEAVATFGLIGTILCTGRHRPDATPVAVGLYITAAYWFTSSTSFANPAVTVART
LSDSFAGIAPHSAPLFVAGQLAGAIAALLFFTWLLREERPQ

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