SitesBLAST
Comparing WP_037576110.1 NCBI__GCF_000744815.1:WP_037576110.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
8uy6A Aquaporin z with alfa tag and bound to nanobody (see paper)
46% identity, 84% coverage: 6:206/240 of query aligns to 3:208/244 of 8uy6A
Sites not aligning to the query:
P60844 Aquaporin Z; Bacterial nodulin-like intrinsic protein; Water channel AqpZ from Escherichia coli (strain K12) (see paper)
46% identity, 84% coverage: 6:206/240 of query aligns to 3:208/231 of P60844
- C9 (≠ F12) mutation to S: No effect.
- C20 (≠ V23) mutation to S: Loss of oligomerization; no alteration of water permeability.
- T183 (= T181) mutation to C: No effect.
- R189 (= R187) mutation R->V,S: Loss of function.
2o9eA Crystal structure of aqpz mutant t183c complexed with mercury (see paper)
46% identity, 84% coverage: 6:206/240 of query aligns to 5:210/232 of 2o9eA
3nkaA Crystal structure of aqpz h174g,t183f (see paper)
45% identity, 85% coverage: 2:206/240 of query aligns to 1:210/230 of 3nkaA
P55064 Aquaporin-5; AQP-5 from Homo sapiens (Human) (see 3 papers)
41% identity, 90% coverage: 5:220/240 of query aligns to 11:220/265 of P55064
- A38 (≠ F32) to E: in PPKB; no effect on localization to plasma membrane; dbSNP:rs398123054
- I45 (= I38) to S: in PPKB; no effect on localization to plasma membrane; dbSNP:rs398123055
- N123 (≠ S124) to D: in PPKB; no effect on localization to plasma membrane; dbSNP:rs398123057; to Y: in PPKB; changed water channel activity; the channel is either leaky and/or more sensitive to hypotonicity; associated with increased TRPV4 basal activity
- S156 (= S155) mutation to A: No effect on localization to plasma membrane.; mutation to E: Increased localization to plasma membrane.
- I177 (= I176) to F: in PPKB; no effect on localization to plasma membrane; dbSNP:rs398123056
- R188 (= R187) to C: in PPKB; no effect on localization to plasma membrane; dbSNP:rs368292687
5dyeD Crystal structure of the full length s156e mutant of human aquaporin 5 (see paper)
41% identity, 90% coverage: 5:220/240 of query aligns to 10:219/253 of 5dyeD
P08995 Nodulin-26; N-26 from Glycine max (Soybean) (Glycine hispida) (see paper)
35% identity, 98% coverage: 5:239/240 of query aligns to 37:262/271 of P08995
- S262 (= S239) 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)
38% identity, 95% coverage: 6:234/240 of query aligns to 11:233/271 of P56402
- T126 (≠ S124) 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
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)
38% identity, 90% coverage: 6:220/240 of query aligns to 11:218/271 of P41181
- G64 (= G58) to R: in NDI2; loss of water channel activity; dbSNP:rs104894326
- G78 (≠ A72) mutation to A: Does not affect interaction with MIAC; when associated with A-79.
- C79 (≠ R73) mutation to A: Does not affect interaction with MIAC; when associated with A-78.
- S148 (≠ V150) 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 (= R187) to C: in NDI2; loss of water channel activity; mutant protein does not fold properly; dbSNP:rs104894328
- A190 (≠ G190) to T: in NDI2; mutant protein does not fold properly and is not functional; dbSNP:rs104894341
- V194 (≠ F194) to I: in dbSNP:rs772051028
- S216 (≠ A218) to P: in NDI2; loss of water channel activity; dbSNP:rs104894329
- L217 (= L219) mutation to A: Abolishes interaction with MIAC; when associated with A-221.
Sites not aligning to the query:
- 221 Y→A: Abolishes interaction with MIAC; when associated with A-217.
- 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)
38% identity, 90% coverage: 6:220/240 of query aligns to 10:217/239 of 4nefA
P29972 Aquaporin-1; AQP-1; Aquaporin-CHIP; Channel-like integral membrane protein of 28 kDa; Urine water channel from Homo sapiens (Human) (see 4 papers)
35% identity, 95% coverage: 6:234/240 of query aligns to 12:241/269 of P29972
- P38 (≠ F32) to L: in Co(A-B-) antigen; non functional AQP1; red cells show low osmotic water permeability; dbSNP:rs104894004
- A45 (vs. gap) to V: in Co(A-B+) antigen; dbSNP:rs28362692
- G165 (≠ Y157) to D: in dbSNP:rs28362731
- H180 (= H172) mutation to A: No effect on water channel activity.
- C189 (≠ T181) Hg(2+)-sensitive residue; mutation to S: No effect on water channel activity.
- H209 (≠ L203) mutation to A: Decreased water channel activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
35% identity, 95% coverage: 6:234/240 of query aligns to 10:239/247 of 8ct2D
Q9XF58 Aquaporin PIP2-5; Plasma membrane intrinsic protein 2-5; ZmPIP2-5; ZmPIP2;5; ZmPIP2a from Zea mays (Maize) (see paper)
36% identity, 89% coverage: 6:218/240 of query aligns to 37:263/285 of Q9XF58
- G104 (≠ C59) mutation to W: Loss of water transport.
P09011 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Rattus norvegicus (Rat) (see 2 papers)
37% identity, 95% coverage: 6:234/240 of query aligns to 11:233/263 of P09011
Sites not aligning to the query:
- 235 modified: Phosphoserine
- 246 N→D: No effects.
P30301 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Homo sapiens (Human) (see 10 papers)
36% identity, 95% coverage: 6:234/240 of query aligns to 11:233/263 of P30301
- R33 (≠ I28) to C: in CTRCT15; reduced cell-to-cell adhesion; no effetc on plasma membrane localization; no effect on water channel activity; dbSNP:rs864309693
- V107 (≠ L101) to I: in CTRCT15; likely benign; dbSNP:rs74641138
- E134 (= E136) to G: in CTRCT15; non-progressive lamellar cataract; loss of localization to the plasma membrane; dominant negative effect on water transport; dbSNP:rs121917869
- T138 (= T140) to R: in CTRCT15; progressive polymorphic and lamellar cataract; loss of localization to the plasma membrane; dominant negative effect on water transport; dbSNP:rs121917867
- D150 (vs. gap) to H: in CTRCT15; loss of localization to the plasma membrane; dbSNP:rs778327521
- G165 (= G165) to D: in CTRCT15; uncertain significance; loss of localization to the plasma membrane
- Y177 (≠ P177) to C: in CTRCT15; uncertain significance
Sites not aligning to the query:
- 204:263 natural variant: Missing (in CTRCT15; uncertain significance)
- 211:263 natural variant: Missing (in CTRCT15; uncertain significance)
- 235 modified: Phosphoserine
- 246 modified: Deamidated asparagine; by deterioration
- 259 modified: Deamidated asparagine; by deterioration
Q6J8I9 Lens fiber major intrinsic protein; Aquaporin-0 from Ovis aries (Sheep) (see 2 papers)
36% identity, 95% coverage: 6:234/240 of query aligns to 11:233/263 of Q6J8I9
- Y149 (vs. gap) mutation to G: Loss of inhibition by calcium.; mutation to L: Decreased water channel activity. Loss of inhibition by calcium.; mutation to S: Decreased water channel activity. Loss of inhibition by calcium.
Sites not aligning to the query:
- 234:235 Cleavage; promotes interactions between tetramers from adjoining membranes
- 243:244 Cleavage; promotes interactions between tetramers from adjoining membranes
8sjxA Structure of lens aquaporin-0 array in sphingomyelin/cholesterol bilayer (2sm:1chol) (see paper)
38% identity, 90% coverage: 6:222/240 of query aligns to 6:215/220 of 8sjxA
- binding cholesterol: I82 (≠ A81), F193 (≠ L200), W200 (≠ I207)
- binding [(E,2S,3R)-2-(hexadecanoylamino)-3-oxidanyl-octadec-4-enyl] 2-(trimethylazaniumyl)ethyl phosphate: F9 (= F9), F9 (= F9), F12 (= F12), V86 (= V85), V86 (= V85), L89 (≠ F88), L90 (≠ V89), L90 (≠ V89), L90 (≠ V89), Y100 (= Y99), Y100 (= Y99), S101 (≠ L100), I188 (= I193), L189 (≠ F194), R191 (≠ G196), F193 (≠ L200)
Sites not aligning to the query:
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)
34% identity, 90% coverage: 6:222/240 of query aligns to 37:265/285 of P43287
- R194 (≠ K158) mutation to A: Reduced sensitivity to cytosolic acidification. Insensitive to cytosolic acidification; when associated with A-197.
- D195 (vs. gap) mutation to A: Reduced sensitivity to cytosolic acidification. Insensitive to cytosolic acidification; when associated with A-197.
- H197 (vs. gap) 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.
- H264 (≠ A221) mutation to A: No effect.
Sites not aligning to the query:
- 3 modified: N6,N6-dimethyllysine; partial
Q06611 Aquaporin PIP1-2; AtPIP1;2; Plasma membrane intrinsic protein 1b; PIP1b; Transmembrane protein A; AthH2; TMP-A from Arabidopsis thaliana (Mouse-ear cress) (see paper)
38% identity, 89% coverage: 6:219/240 of query aligns to 52:271/286 of Q06611
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)
36% identity, 91% coverage: 6:223/240 of query aligns to 52:275/286 of Q08733
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
Query Sequence
>WP_037576110.1 NCBI__GCF_000744815.1:WP_037576110.1
MNDKIRAIFCEFLGTALLVFFAVGSAVISAQFIGTFGIALAFGFVLMALVYAIGPVSGCH
VNPAVTMGALVARRIDLITAACYWVAQFVGGIAGAALLYLLAHQVPGLTTHDAFGSNGYG
DRSSVHLSQGGAFLAEVVLTFLLVWVVLSVTHRVSLYKFAGLAIGVSLTVIHLVGIPLTG
TSVNPARSLGPAIFAGGGALSQLWLFIVAPLIGGVIAALVAEVTHPRTAPLPDEKPEPSA
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