SitesBLAST
Comparing Echvi_3497 FitnessBrowser__Cola:Echvi_3497 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)
3dh4A Crystal structure of sodium/sugar symporter with bound galactose from vibrio parahaemolyticus (see paper)
32% identity, 79% coverage: 38:454/527 of query aligns to 19:438/512 of 3dh4A
Q9ET37 Solute carrier family 5 member 4A; SGLT3-a from Mus musculus (Mouse) (see paper)
30% identity, 84% coverage: 5:445/527 of query aligns to 32:493/656 of Q9ET37
- E457 (≠ Q409) mutation to Q: Confers sodium-dependent sugar transport activity not found in the wild type protein.
7sl8A Cryoem structure of sglt1 at 3.4 a resolution (see paper)
29% identity, 76% coverage: 39:437/527 of query aligns to 31:453/582 of 7sl8A
Sites not aligning to the query:
7slaA Cryoem structure of sglt1 at 3.15 angstrom resolution (see paper)
29% identity, 76% coverage: 39:437/527 of query aligns to 32:454/585 of 7slaA
Sites not aligning to the query:
7wmvA Structure of human sglt1-map17 complex bound with lx2761 (see paper)
29% identity, 81% coverage: 9:437/527 of query aligns to 17:468/602 of 7wmvA
- binding N-[2-(dimethylamino)ethyl]-2-methyl-2-[4-[4-[[2-methyl-5-[(2S,3R,4R,5S,6R)-6-methylsulfanyl-3,4,5-tris(oxidanyl)oxan-2-yl]phenyl]methyl]phenyl]butanoylamino]propanamide: N61 (= N54), H66 (= H59), L70 (≠ M63), I81 (= I74), F84 (≠ W77), L257 (= L241), M266 (≠ L250), L269 (≠ N253), T270 (≠ Q254), Y273 (≠ F257), W274 (= W258), F436 (= F405), D437 (≠ Q406), Q440 (= Q409)
Sites not aligning to the query:
P13866 Sodium/glucose cotransporter 1; Na(+)/glucose cotransporter 1; High affinity sodium-glucose cotransporter; Solute carrier family 5 member 1 from Homo sapiens (Human) (see 6 papers)
29% identity, 81% coverage: 9:437/527 of query aligns to 34:485/664 of P13866
- N51 (= N27) to S: in GGM; slightly decreased activity; dbSNP:rs17683011
- W67 (≠ G43) mutation to A: Strong reduction in D-glucose transporter activity.
- S77 (≠ T53) mutation to A: Loss of activity.
- H83 (= H59) mutation to L: Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with A-287 and C-290.; mutation to Q: Loss of D-glucose transporter activity.
- R135 (= R111) to W: in GGM; loss of activity
- S159 (≠ P134) to P: in GGM; loss of activity
- A166 (= A141) to T: in GGM; about 90% reduction in activity
- D204 (= D189) mutation to A: Loss of activity.
- N248 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to Q: Loss of N-glycosylation.
- C255 (≠ V223) modified: Disulfide link with 511
- W276 (≠ F243) to L: in GGM; about 95% reduction in activity
- T287 (≠ Q254) mutation to A: Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with L-83 and C-290.; mutation to N: Loss of D-glucose transporter activity. Has strict selectivity for D-galactose.; mutation T->S,A: Has normal D-glucose and D-galactose transporter activity.
- Y290 (≠ F257) mutation to C: Loss of D-galactose transporter activity. Has strict selectivity for D-glucose. Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with A-287 and L-83.
- W291 (= W258) mutation to A: Loss of D-glucose transporter activity.
- C292 (= C259) to Y: in GGM; loss of activity; mutation to A: Has no effect on water permeability.
- Q295 (= Q262) to R: in GGM; loss of activity
- R300 (= R267) to S: in GGM; loss of activity
- A304 (= A271) to V: in GGM; impairs trafficking to the plasma membrane
- K321 (= K288) mutation to Q: Acquires D-mannose and D-allose transporter activity comparable to glucose and galactose.
- C345 (vs. gap) modified: Disulfide link with 351
- C351 (≠ N313) modified: Disulfide link with 345
- C355 (vs. gap) modified: Disulfide link with 361
- C361 (vs. gap) modified: Disulfide link with 355
- N363 (≠ D315) mutation to A: Loss of water permeation.
- L369 (= L321) to S: in GGM; loss of activity
- R379 (≠ T331) to Q: in GGM; loss of activity
- A388 (≠ G340) to V: in GGM; loss of activity
- S396 (= S348) mutation to A: Loss of activity.
- F405 (= F357) to S: in GGM; loss of activity
- A411 (≠ K363) to T: in GGM; slightly decreased activity; dbSNP:rs17683430
- G426 (= G379) to R: in GGM; loss of activity
- Q451 (vs. gap) mutation to A: Strong reduction in water permeation.
- L452 (= L404) mutation to A: Loss of water permeation.
- D454 (≠ Q406) mutation to A: Has no effect on water permeation.
- Q457 (= Q409) mutation to A: Loss of D-glucose transporter activity.; mutation to C: Strong reduction in D-glucose transporter activity.
- T460 (≠ N412) mutation to A: Loss of D-glucose transporter activity.
- V470 (≠ I422) to N: in GGM; about 90% reduction in activity; requires 2 nucleotide substitutions
Sites not aligning to the query:
- 191:664 natural variant: Missing (in GGM; loss of activity)
- 379:664 natural variant: Missing (in GGM; loss of activity)
- 499 R → H: in GGM; impairs trafficking to the plasma membrane; decreases the sugar affinity
- 511 modified: Disulfide link with 255
- 517 modified: Disulfide link with 522
- 522 modified: Disulfide link with 517
- 615 H → Q: in GGM; slightly decreased activity
- 641 W→A: Slightly reduced D-glucose transporter activity.
- 660:661 HA→WG: Loss of D-glucose transporter activity.
8hezA Structure of human sglt2-map17 complex with dapagliflozin (see paper)
28% identity, 81% coverage: 11:437/527 of query aligns to 13:465/582 of 8hezA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (= N54), G59 (≠ E58), H60 (= H59), G63 (= G62), L64 (≠ M63), T67 (≠ S66), F78 (≠ W77), E79 (= E78), V266 (≠ N253), S267 (≠ Q254), W271 (= W258), K301 (= K288), F433 (= F405), Q437 (= Q409)
- binding sodium ion: A53 (≠ M52), I56 (= I55), G57 (≠ S56), A369 (= A341), S372 (= S344), S373 (≠ T345)
Sites not aligning to the query:
8hg7A Structure of human sglt2-map17 complex with sotagliflozin (see paper)
28% identity, 81% coverage: 11:437/527 of query aligns to 13:465/590 of 8hg7A
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-methylsulfanyl-oxane-3,4,5-triol: N55 (= N54), G59 (≠ E58), H60 (= H59), G63 (= G62), L64 (≠ M63), E79 (= E78), V266 (≠ N253), S267 (≠ Q254), Y270 (≠ F257), W271 (= W258), K301 (= K288), F433 (= F405), Q437 (= Q409)
- binding sodium ion: A53 (≠ M52), S54 (≠ T53), I56 (= I55), G57 (≠ S56), A369 (= A341), S372 (= S344), S373 (≠ T345)
Sites not aligning to the query:
7vsiA Structure of human sglt2-map17 complex bound with empagliflozin (see paper)
28% identity, 81% coverage: 11:437/527 of query aligns to 13:465/586 of 7vsiA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[[4-[(3S)-oxolan-3-yl]oxyphenyl]methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (= N54), H60 (= H59), G63 (= G62), L64 (≠ M63), V75 (≠ I74), F78 (≠ W77), E79 (= E78), V266 (≠ N253), S267 (≠ Q254), Y270 (≠ F257), F433 (= F405), D434 (≠ Q406), Q437 (= Q409)
8hdhA Structure of human sglt2-map17 complex with canagliflozin (see paper)
28% identity, 81% coverage: 11:437/527 of query aligns to 13:465/586 of 8hdhA
- binding (2~{S},3~{R},4~{R},5~{S},6~{R})-2-[3-[[5-(4-fluorophenyl)thiophen-2-yl]methyl]-4-methyl-phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (= N54), G59 (≠ E58), H60 (= H59), G63 (= G62), L64 (≠ M63), F78 (≠ W77), E79 (= E78), S267 (≠ Q254), W271 (= W258), F433 (= F405), D434 (≠ Q406), Q437 (= Q409)
- binding sodium ion: A53 (≠ M52), S54 (≠ T53), I56 (= I55), G57 (≠ S56), A369 (= A341), S372 (= S344), S373 (≠ T345)
Sites not aligning to the query:
- binding (2~{S},3~{R},4~{R},5~{S},6~{R})-2-[3-[[5-(4-fluorophenyl)thiophen-2-yl]methyl]-4-methyl-phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: 506
- binding : 575, 579, 580, 583, 584
8hb0A Structure of human sglt2-map17 complex with ta1887 (see paper)
28% identity, 81% coverage: 11:437/527 of query aligns to 13:465/586 of 8hb0A
- binding (2R,3R,4S,5S,6R)-2-[3-[(4-cyclopropylphenyl)methyl]-4-fluoranyl-indol-1-yl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (= N54), H60 (= H59), G63 (= G62), L64 (≠ M63), T67 (≠ S66), V75 (≠ I74), F78 (≠ W77), E79 (= E78), V137 (≠ I135), V266 (≠ N253), S267 (≠ Q254), W271 (= W258), F433 (= F405), Q437 (= Q409)
- binding sodium ion: A53 (≠ M52), I56 (= I55), G57 (≠ S56), A369 (= A341), S372 (= S344), S373 (≠ T345)
Sites not aligning to the query:
P31639 Sodium/glucose cotransporter 2; Na(+)/glucose cotransporter 2; Low affinity sodium-glucose cotransporter; Solute carrier family 5 member 2 from Homo sapiens (Human) (see paper)
28% identity, 81% coverage: 11:437/527 of query aligns to 33:485/672 of P31639
- V95 (≠ I74) mutation to A: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
- F98 (≠ W77) mutation to A: Slightly decreases D-glucose transporter activity. Abolishes the binding to inhibitor, empagliflozin.
- V157 (≠ I135) mutation to A: Decreases D-glucose transporter activity.
- L283 (= L250) mutation to M: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
- F453 (= F405) mutation to A: Slightly decreases D-glucose transporter activity. Greatly reduces the binding to inhibitor, empagliflozin.
Q9NY91 Probable glucose sensor protein SLC5A4; Solute carrier family 5 member 4 from Homo sapiens (Human) (see paper)
26% identity, 86% coverage: 5:458/527 of query aligns to 32:509/659 of Q9NY91
- E457 (≠ Q409) mutation to Q: Confers sugar transport activity not found in the wild-type protein. Increased sensitivity to inhibitor phlorizin.
P11170 Sodium/glucose cotransporter 1; Na(+)/glucose cotransporter 1; High affinity sodium-glucose cotransporter; Solute carrier family 5 member 1 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
27% identity, 83% coverage: 9:445/527 of query aligns to 34:493/662 of P11170
- C255 (≠ V223) modified: Disulfide link with 608
- Q457 (= Q409) mutation to W: Drasticly decreased affinity for glucose and phlorizin.
- T460 (≠ N412) mutation to W: Decreased affinity for glucose and phlorizin.
Sites not aligning to the query:
- 608 modified: Disulfide link with 255
8hinA Structure of human sglt2-map17 complex with phlorizin (see paper)
27% identity, 76% coverage: 38:437/527 of query aligns to 35:461/588 of 8hinA
- binding 1-[2-[(2S,3R,4S,5S,6R)-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-4,6-bis(oxidanyl)phenyl]-3-(4-hydroxyphenyl)propan-1-one: S46 (= S49), A49 (≠ M52), S50 (≠ T53), G53 (≠ S56), D177 (= D189), T181 (≠ G193), R276 (= R267), S369 (≠ T345)
Sites not aligning to the query:
7yniA Structure of human sglt1-map17 complex bound with substrate 4d4fdg in the occluded conformation (see paper)
28% identity, 76% coverage: 39:437/527 of query aligns to 31:447/566 of 7yniA
- binding (2R,3R,4R,5S,6R)-5-fluoranyl-6-(hydroxymethyl)oxane-2,3,4-triol: H51 (= H59), E70 (= E78), L248 (≠ N253), Y252 (≠ F257), F415 (= F405), Q419 (= Q409)
Sites not aligning to the query:
7ynjA Structure of human sglt2-map17 complex bound with substrate amg in the occluded conformation (see paper)
27% identity, 76% coverage: 39:437/527 of query aligns to 22:443/564 of 7ynjA
Sites not aligning to the query:
P07117 Sodium/proline symporter; Proline carrier; Proline permease; Propionate transporter from Escherichia coli (strain K12) (see 4 papers)
27% identity, 72% coverage: 1:380/527 of query aligns to 7:376/502 of P07117
- R257 (= R267) mutation to C: Sodium-independent binding affinity for proline.
- C281 (≠ V291) mutation to S: Does not affect proline uptake activity. Confers resistance to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
- C344 (≠ S348) mutation to S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
- C349 (≠ A353) mutation to S: Does not affect proline uptake activity. Sensitive to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
- R376 (≠ K380) mutation R->E,Q: No change in activity.; mutation to K: Loss of activity.
Q8N695 Sodium-coupled monocarboxylate transporter 1; Apical iodide transporter; Electrogenic sodium monocarboxylate cotransporter; Sodium iodide-related cotransporter; Solute carrier family 5 member 8 from Homo sapiens (Human) (see 3 papers)
25% identity, 79% coverage: 30:445/527 of query aligns to 42:450/610 of Q8N695
- V193 (≠ Y194) to I: in dbSNP:rs1709189
- F251 (≠ Y256) to V: in dbSNP:rs11834933
Sites not aligning to the query:
- 608 T→A: Loss of interaction with PDZK1.
- 608:610 PDZ-binding
- 610 L→A: Loss of interaction with PDZK1.
Q92911 Sodium/iodide cotransporter; Na(+)/I(-) cotransporter; Natrium iodide transporter; Sodium-iodide symporter; Na(+)/I(-) symporter; Solute carrier family 5 member 5 from Homo sapiens (Human) (see 3 papers)
24% identity, 66% coverage: 20:367/527 of query aligns to 33:376/643 of Q92911
- A102 (= A89) natural variant: A -> P
- H226 (≠ P228) mutation H->A,D,E,K: Significant loss of iodide transport activity but no effect on its localization to the cell membrane.
- D237 (≠ G236) mutation to A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization.
- Y242 (≠ L241) Required for homodimerization; mutation to A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471. Loss of iodide transport activity; when associated with F-535.
- T243 (≠ P242) Required for homodimerization; mutation to A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471.
Sites not aligning to the query:
- 471 Required for homodimerization; Q→A: No effect on localization to the cell membrane, iodide transport activity and homodimerization. Significant loss of homodimerization; when associated with A-242 or A243.
- 525 A→F: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Loss of iodide transport activity; when associated with A-242.
- 536 T → Q: requires 2 nucleotide substitutions
- 556 S → Q: requires 2 nucleotide substitutions
Query Sequence
>Echvi_3497 FitnessBrowser__Cola:Echvi_3497
MNITILTFIAFTLLVAVYAWLKTRKENLDSEDGYFLGGRSLTGVVIAGSMIMTNISTEHL
VGMNGSSYKNGFVIVAWEVTSALALIVAAVYFVPRYLKMGLTTVPQYLENRFDAGTRSLV
AFFLLISFAVTLLPIVLYTGAINLESLFNISDTLNISQEQGLWYTVLAVGGIGSIYAIFG
GLKAVAVSDTINGYGLLLAGLMVPVIALFMIGDNNPLLGLERVFENSPEKFNVVGGKDSV
LPFSTLFTGLIINQLYFWCMNQTIIQRALGAKNLKEAQKGLLYTGALKLLVPFIIVLPGV
IGFYFFGDRLYENQDMVYPELVKKVLPVGLTGVFAAVIMGAVLSTFNSVLNSASTIFSID
IYKRLIRPGASAGQLVKAGKLSATILAITSMVAAPMVANAPEGLFQLLQQLNGIFFIPIA
SIMLAGFFTKWVSPLAAKVALVTGLTFYVLTTFVFDIGIHFVHIWGIEFVLNVLIMYVVS
VAWPMAKPTEKTLISAKINTDKWKYASLVSIILVIITVVIYMLLGNI
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