SitesBLAST
Comparing AO356_18255 AO356_18255 glycerol uptake facilitator GlpF 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)
68% identity, 98% coverage: 6:283/283 of query aligns to 3:280/281 of P0AER0
- HLN 66:68 (= HLN 69:71) binding
- Y138 (= Y141) binding
- GFA 199:201 (= GFA 202:204) binding
- N203 (= N206) binding
- R206 (= R209) binding
- 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)
73% 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)
65% 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)
39% identity, 93% coverage: 10:271/283 of query aligns to 20:277/301 of Q96PS8
- E27 (= E17) mutation to Q: Abolishes permeability to glycerol.
- G73 (≠ S62) mutation to A: Increased permeability to glycerol at acidic pH.; mutation to F: Abolishes permeability to glycerol.
- S77 (= S66) mutation S->A,D: Nearly abolishes permeability to glycerol.
- H80 (= H69) mutation to A: Abolishes permeability to glycerol.
- F85 (≠ V74) mutation to A: Nearly abolishes permeability to glycerol.
- R94 (≠ D83) mutation to A: Abolishes permeability to glycerol.
- N133 (≠ R122) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to Q: Abolishes N-glycosylation.
6f7hC Crystal structure of human aqp10 (see paper)
40% 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 4 papers)
34% identity, 94% coverage: 7:272/283 of query aligns to 30:290/342 of O14520
- V59 (vs. gap) to L: in dbSNP:rs4008659
- Y135 (≠ S112) Important for permeability to glycerol; mutation to A: Strongly decreased permeability to glycerol. Mildly decreased water permeability.
- H165 (≠ A145) mutation to A: Decreased permeability to glycerol. Mildly decreased water permeability.
- G264 (= G246) to V: affects water and glycerol transport; dbSNP:rs62542743
Sites not aligning to the query:
- 1:32 mutation Missing: Decreased interaction with PLIN1.
- 12 R → C: in dbSNP:rs139297434
8c9hA Aqp7_inhibitor
35% identity, 88% coverage: 7:254/283 of query aligns to 5:247/253 of 8c9hA
6n1gA Crystal structure of aquaglyceroporin aqp7 (see paper)
35% 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)
39% identity, 84% coverage: 13:250/283 of query aligns to 60:292/306 of I1CR68
- H275 (vs. gap) mutation to A: Affects pH sensing; when associated with A-85.
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
2evuA Crystal structure of aquaporin aqpm at 2.3a resolution (see paper)
33% identity, 88% coverage: 9:257/283 of query aligns to 3:243/245 of 2evuA
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, 98% coverage: 5:281/283 of query aligns to 4:249/271 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 (≠ T82) 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 (≠ S264) 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.
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)
29% identity, 98% coverage: 5:281/283 of query aligns to 4:249/271 of P56402
- T126 (≠ S147) 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
P08995 Nodulin-26; N-26 from Glycine max (Soybean) (Glycine hispida) (see paper)
30% identity, 95% coverage: 12:279/283 of query aligns to 38:267/271 of P08995
- S262 (≠ P274) modified: Phosphoserine; by CPK
4nefA X-ray structure of human aquaporin 2 (see paper)
31% identity, 89% coverage: 3:255/283 of query aligns to 1:219/239 of 4nefA
Q9SAI4 Aquaporin NIP6-1; NOD26-like intrinsic protein 6-1; AtNIP6;1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 90% coverage: 1:254/283 of query aligns to 67:285/305 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.
P09011 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Rattus norvegicus (Rat) (see 2 papers)
29% identity, 98% coverage: 5:281/283 of query aligns to 2:248/261 of P09011
- S233 (≠ T267) modified: Phosphoserine
- N244 (≠ D277) mutation to D: No effects.
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)
29% identity, 85% coverage: 8:247/283 of query aligns to 45:251/298 of Q6Z2T3
- A132 (≠ S95) mutation to T: In lsi; impairs silicon uptake. Grain discoloration. Reduces grain yield 10-fold.
P30301 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Homo sapiens (Human) (see 10 papers)
28% identity, 99% coverage: 5:283/283 of query aligns to 4:252/263 of P30301
- R33 (≠ K36) to C: in CTRCT15; reduces cell-to-cell adhesion, reduces cell-to-cell gap junction coupling, no loss of cell membrane localization, no loss of water channel activity; dbSNP:rs864309693
- V107 (≠ L110) to I: in CTRCT15; likely benign; dbSNP:rs74641138
- E134 (= E155) to G: in CTRCT15; non-progressive lamellar cataract; loss of activity; dbSNP:rs121917869
- T138 (= T159) to R: in CTRCT15; progressive polymorphic and lamellar cataract; loss of activity; dbSNP:rs121917867
- D150 (= D171) to H: in CTRCT15; loss of plasma membrane expression; dbSNP:rs778327521
- G165 (= G187) to D: in CTRCT15; uncertain significance; loss of plasma membrane expression
- Y177 (≠ P199) to C: in CTRCT15; uncertain significance
- S235 (≠ T267) modified: Phosphoserine
- N246 (≠ D277) modified: Deamidated asparagine; by deterioration
Sites not aligning to the query:
- 204:263 natural variant: Missing (in CTRCT15; uncertain significance)
- 211:263 natural variant: Missing (in CTRCT15; uncertain significance)
- 259 modified: Deamidated asparagine; by deterioration
Query Sequence
>AO356_18255 AO356_18255 glycerol uptake facilitator GlpF
MTTALQQPSLSSQCLAEFLGTGLLIFFGTGCVAALKVAGASFGLWEISLIWGVGVSMAIY
LSAGISGAHLNPAVSIALCMFTDFEKRKLPFYIASQVTGAFCGALLVYTLYSNLFFDFEQ
SRHMVRGTEMSLELASVFSTYPHAALSTGQAFLVEAIITAILMGVIMSLTDDNNGLPRGP
LAPLLIGLLIAVIGSSMGPLTGFAMNPARDFGPKLMTFFAGWGEISLTGGRDIPYFLVPI
FAPIVGACLGAAAYRGLIARHLPSAVTATKDAEPAIDGKPRTS
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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