SitesBLAST
Comparing AO353_04175 FitnessBrowser__pseudo3_N2E3:AO353_04175 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P0AER0 Glycerol uptake facilitator protein; Aquaglyceroporin; Glycerol facilitator from Escherichia coli (strain K12) (see 3 papers)
70% identity, 99% coverage: 5:283/283 of query aligns to 2:280/281 of P0AER0
- HLN 66:68 (= HLN 69:71) binding glycerol
- Y138 (≠ F141) binding glycerol
- GFA 199:201 (= GFA 202:204) binding glycerol
- N203 (= N206) binding glycerol
- R206 (= R209) binding glycerol
- PL 236:237 (≠ PI 239:240) mutation to FW: No detectable water or glycerol permeability.
1fx8A Crystal structure of the e. Coli glycerol facilitator (glpf) with substrate glycerol (see paper)
74% identity, 90% coverage: 9:262/283 of query aligns to 1:254/254 of 1fx8A
B1VB61 Propanediol uptake facilitator PduF from Citrobacter freundii (see paper)
66% identity, 95% coverage: 6:273/283 of query aligns to 1:268/269 of B1VB61
P37451 Propanediol uptake facilitator PduF from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
68% identity, 90% coverage: 9:263/283 of query aligns to 4:258/264 of P37451
Q96PS8 Aquaporin-10; AQP-10; Aquaglyceroporin-10; Small intestine aquaporin from Homo sapiens (Human) (see 2 papers)
40% identity, 95% coverage: 10:277/283 of query aligns to 20:277/301 of Q96PS8
- E27 (= E17) mutation to Q: Loss of glycerol channel activity.
- G73 (≠ T62) mutation to A: Increased glycerol channel activity at acidic pH.; mutation to F: Loss of glycerol channel activity.
- S77 (= S66) mutation S->A,D: Decreased glycerol channel activity.
- H80 (= H69) pH-sensor; mutation to A: Loss of glycerol channel activity.
- F85 (≠ V74) mutation to A: Decreased glycerol channel activity.
- R94 (≠ D83) mutation to A: Loss of glycerol channel activity.
- N133 (≠ H122) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to Q: Abolishes N-glycosylation.
6f7hC Crystal structure of human aqp10 (see paper)
41% identity, 89% coverage: 10:261/283 of query aligns to 5:252/253 of 6f7hC
O14520 Aquaporin-7; AQP-7; Aquaglyceroporin-7; Aquaporin adipose; AQPap; Aquaporin-7-like from Homo sapiens (Human) (see 5 papers)
34% identity, 91% coverage: 7:263/283 of query aligns to 30:281/342 of O14520
- V59 (vs. gap) to L: in dbSNP:rs4008659
- Y67 (≠ S41) mutation to A: No effect on glycerol channel activity. No effect on water channel activity.
- F74 (≠ W51) mutation to W: No effect on glycerol channel activity. No effect on water channel activity. Decreased glycerol channel activity; when associated with F-233.
- Y135 (≠ S112) Important for permeability to glycerol; mutation to A: Strongly decreased glycerol channel activity. Mildly decreased water channel activity.
- H165 (≠ A145) mutation to A: Decreased glycerol channel activity. Mildly decreased water channel activity.
- Y223 (≠ F203) mutation to F: No effect on glycerol channel activity. No effect on water channel activity. Decreased glycerol channel activity; when associated with W-74.
- G264 (= G246) to V: loss of glycerol channel activity; loss of water channel activity; dbSNP:rs62542743
Sites not aligning to the query:
- 10:11 ST→AA: Loss of phosphorylation by PKA. Increased interaction with PLIN1.
- 12 R → C: in dbSNP:rs139297434
8c9hA Aqp7_inhibitor (see paper)
34% identity, 88% coverage: 7:254/283 of query aligns to 5:247/253 of 8c9hA
6n1gA Crystal structure of aquaglyceroporin aqp7 (see paper)
34% identity, 87% coverage: 9:254/283 of query aligns to 1:241/249 of 6n1gA
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)
38% identity, 83% coverage: 15:250/283 of query aligns to 62:292/306 of I1CR68
- H275 (≠ R231) mutation to A: Affects pH sensing; when associated with A-85.
Q8II36 Aquaglyceroporin; PfAQP; Aquaporin-1 from Plasmodium falciparum (isolate 3D7) (see 2 papers)
34% identity, 94% coverage: 8:273/283 of query aligns to 7:254/258 of Q8II36
- G66 (= G67) binding glycerol
- A67 (= A68) binding glycerol
- N70 (= N71) binding glycerol
- L71 (≠ P72) mutation to P: No significant effects on transport activity; when associated with A-131.
- LA 71:72 (≠ PA 72:73) mutation to PS: Reduces stability and abolishes transport activity; when associated with 130-L-A-131.
- S127 (≠ F141) binding glycerol
- PS 130:131 (≠ PA 144:145) mutation to LA: Reduces stability and abolishes transport activity; when associated with 71-P-S-72.
- S131 (≠ A145) mutation to A: No significant effects on transport activity; when associated with P-71.
- G189 (= G202) binding glycerol
- F190 (= F203) binding glycerol
- N193 (= N206) binding glycerol
- R196 (= R209) binding glycerol
3c02A X-ray structure of the aquaglyceroporin from plasmodium falciparum (see paper)
35% identity, 89% coverage: 9:259/283 of query aligns to 1:236/242 of 3c02A
8ofxA Molecular mechanism of trypanosomal aqp2
33% identity, 85% coverage: 15:255/283 of query aligns to 7:239/244 of 8ofxA
- binding [(2~{R},4~{S})-2-[4-[[4,6-bis(azanyl)-1,3,5-triazin-2-yl]amino]phenyl]-1,3,2-dithiarsolan-4-yl]methanol: G58 (= G67), G59 (≠ A68), H60 (= H69), L61 (= L70), N62 (= N71), V65 (= V74), L150 (= L162), V154 (≠ I166), F158 (≠ T170), I173 (= I186), V177 (≠ I190), A191 (= A204), M192 (= M205), N193 (= N206), L196 (≠ R209)
8jy8A Structure of tbaqp2 in complex with anti-trypanosomatid drug pentamidine (see paper)
33% identity, 85% coverage: 15:255/283 of query aligns to 5:237/242 of 8jy8A
8jy6A Structure of tbaqp2 in complex with anti-trypanosomatid drug melarsoprol (see paper)
33% identity, 85% coverage: 15:255/283 of query aligns to 5:237/242 of 8jy6A
- binding [(4~{R})-2-[4-[[4,6-bis(azanyl)-1,3,5-triazin-2-yl]amino]phenyl]-1,3,2-dithiarsolan-4-yl]methanol: H58 (= H69), L59 (= L70), M126 (≠ T140), I171 (= I186), V175 (≠ I190), V179 (≠ G194), A189 (= A204), N191 (= N206), L194 (≠ R209)
2evuA Crystal structure of aquaporin aqpm at 2.3a resolution (see paper)
34% identity, 88% coverage: 9:257/283 of query aligns to 3:243/245 of 2evuA
P08995 Nodulin-26; N-26 from Glycine max (Soybean) (Glycine hispida) (see paper)
31% identity, 95% coverage: 12:280/283 of query aligns to 38:268/271 of P08995
- S262 (≠ P274) modified: Phosphoserine; by CPK
Q9SAI4 Aquaporin NIP6-1; NOD26-like intrinsic protein 6-1; AtNIP6;1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
32% identity, 87% coverage: 9:254/283 of query aligns to 77:285/305 of Q9SAI4
- A119 (≠ W51) mutation to W: 6-fold increase in water transport activity, but impaired in urea transport.
- V252 (≠ A208) mutation to A: No effect.
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)
29% identity, 96% coverage: 9:281/283 of query aligns to 8:249/271 of P41181
- G64 (= G67) to R: in NDI2; loss of water channel activity; dbSNP:rs104894326
- G78 (≠ F81) mutation to A: Does not affect interaction with MIAC; when associated with A-79.
- C79 (≠ A82) mutation to A: Does not affect interaction with MIAC; when associated with A-78.
- S148 (≠ L169) 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 (= R209) to C: in NDI2; loss of water channel activity; mutant protein does not fold properly; dbSNP:rs104894328
- A190 (≠ G212) to T: in NDI2; mutant protein does not fold properly and is not functional; dbSNP:rs104894341
- V194 (≠ M216) to I: in dbSNP:rs772051028
- S216 (≠ A251) to P: in NDI2; loss of water channel activity; dbSNP:rs104894329
- L217 (≠ A252) mutation to A: Abolishes interaction with MIAC; when associated with A-221.
- Y221 (≠ G256) mutation to A: Abolishes interaction with MIAC; when associated with A-217.
- S229 (≠ H261) mutation to A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; mutation to D: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
- S231 (≠ P263) mutation to A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; mutation to D: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
- E232 (≠ I264) mutation to A: Reduces interaction with MIAC.
- T244 (≠ I276) mutation to A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; mutation to E: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
Sites not aligning to the query:
- 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.
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)
28% identity, 87% coverage: 8:254/283 of query aligns to 45:254/298 of Q6Z2T3
- A132 (≠ S95) mutation to T: In lsi; impairs silicon uptake. Grain discoloration. Reduces grain yield 10-fold.
Query Sequence
>AO353_04175 FitnessBrowser__pseudo3_N2E3:AO353_04175
MTTASQQPSLSSQCMAEFLGTALLIFFGTGCVAALKVAGASFGLWEISIIWGIGVSMAIY
LTAGVSGAHLNPAVSIALCIFADFEKRKLPLYIFSQVAGAFCAALLVYTLYSNLFFDFEQ
THQMVRGTQASLELASVFSTFPNPALSTAQAFLVEVIITAILMGVIMSLTDDNNGLPKGP
LAPLLIGLLIAVIGSSMGPLTGFAMNPARDFGPKLMTFFAGWGEISFTGGRDIPYFLIPI
FAPILGACLGAAAYRGLIARHLPIAIPATKDAEPAIDGKARIS
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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