SitesBLAST
Comparing Echvi_1871 FitnessBrowser__Cola:Echvi_1871 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)
3dh4A Crystal structure of sodium/sugar symporter with bound galactose from vibrio parahaemolyticus (see paper)
53% identity, 92% coverage: 44:547/547 of query aligns to 20:508/512 of 3dh4A
7slaA Cryoem structure of sglt1 at 3.15 angstrom resolution (see paper)
34% identity, 84% coverage: 4:460/547 of query aligns to 7:454/585 of 7slaA
Sites not aligning to the query:
7wmvA Structure of human sglt1-map17 complex bound with lx2761 (see paper)
33% identity, 84% coverage: 4:461/547 of query aligns to 8:469/602 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 (= N59), H66 (≠ Q64), L70 (≠ M68), I81 (= I79), F84 (≠ Y82), L257 (= L249), M266 (= M261), L269 (≠ V264), T270 (≠ N265), Y273 (= Y268), W274 (= W269), F436 (= F428), D437 (≠ Q429), Q440 (= Q432)
Sites not aligning to the query:
7sl8A Cryoem structure of sglt1 at 3.4 a resolution (see paper)
34% identity, 84% coverage: 4:460/547 of query aligns to 6:453/582 of 7sl8A
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)
33% identity, 84% coverage: 4:461/547 of query aligns to 25:486/664 of P13866
- N51 (≠ K29) to S: in GGM; slightly decreased activity; dbSNP:rs17683011
- W67 (= W48) mutation to A: Strong reduction in D-glucose transporter activity.
- S77 (= S58) mutation to A: Loss of activity.
- H83 (≠ Q64) 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 (= R116) to W: in GGM; loss of activity
- S159 (≠ T139) to P: in GGM; loss of activity
- A166 (= A146) to T: in GGM; about 90% reduction in activity
- D204 (= D184) mutation to A: Loss of activity.
- N248 (≠ E234) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to Q: Loss of N-glycosylation.
- C255 (≠ S241) modified: Disulfide link with 511
- W276 (≠ L254) to L: in GGM; about 95% reduction in activity
- T287 (≠ N265) 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 (= Y268) 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 (= W269) mutation to A: Loss of D-glucose transporter activity.
- C292 (≠ G270) to Y: in GGM; loss of activity; mutation to A: Has no effect on water permeability.
- Q295 (= Q273) to R: in GGM; loss of activity
- R300 (= R278) to S: in GGM; loss of activity
- A304 (= A282) to V: in GGM; impairs trafficking to the plasma membrane
- K321 (= K299) mutation to Q: Acquires D-mannose and D-allose transporter activity comparable to glucose and galactose.
- C345 (≠ S324) modified: Disulfide link with 351
- C351 (≠ T330) modified: Disulfide link with 345
- C355 (≠ T334) modified: Disulfide link with 361
- C361 (≠ K338) modified: Disulfide link with 355
- N363 (≠ D340) mutation to A: Loss of water permeation.
- L369 (= L346) to S: in GGM; loss of activity
- R379 (≠ K355) to Q: in GGM; loss of activity
- A388 (= A364) to V: in GGM; loss of activity
- S396 (= S372) mutation to A: Loss of activity.
- F405 (= F381) to S: in GGM; loss of activity
- A411 (≠ K387) to T: in GGM; slightly decreased activity; dbSNP:rs17683430
- G426 (= G403) to R: in GGM; loss of activity
- Q451 (= Q426) mutation to A: Strong reduction in water permeation.
- L452 (≠ A427) mutation to A: Loss of water permeation.
- D454 (≠ Q429) mutation to A: Has no effect on water permeation.
- Q457 (= Q432) mutation to A: Loss of D-glucose transporter activity.; mutation to C: Strong reduction in D-glucose transporter activity.
- T460 (= T435) mutation to A: Loss of D-glucose transporter activity.
- V470 (≠ I445) 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.
8hdhA Structure of human sglt2-map17 complex with canagliflozin (see paper)
33% identity, 84% coverage: 4:460/547 of query aligns to 2:465/586 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 (= N59), G59 (≠ E63), H60 (≠ Q64), G63 (= G67), L64 (≠ M68), F78 (≠ Y82), E79 (= E83), S267 (≠ N265), W271 (= W269), F433 (= F428), D434 (≠ Q429), Q437 (= Q432)
- binding sodium ion: A53 (= A57), S54 (= S58), I56 (= I60), G57 (≠ S61), A369 (= A365), S372 (= S368), S373 (= S369)
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)
33% identity, 84% coverage: 4:460/547 of query aligns to 2:465/586 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 (= N59), H60 (≠ Q64), G63 (= G67), L64 (≠ M68), T67 (≠ S71), V75 (≠ I79), F78 (≠ Y82), E79 (= E83), V137 (≠ S140), V266 (= V264), S267 (≠ N265), W271 (= W269), F433 (= F428), Q437 (= Q432)
- binding sodium ion: A53 (= A57), I56 (= I60), G57 (≠ S61), A369 (= A365), S372 (= S368), S373 (= S369)
Sites not aligning to the query:
8hezA Structure of human sglt2-map17 complex with dapagliflozin (see paper)
33% identity, 84% coverage: 4:460/547 of query aligns to 2:465/582 of 8hezA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (= N59), G59 (≠ E63), H60 (≠ Q64), G63 (= G67), L64 (≠ M68), T67 (≠ S71), F78 (≠ Y82), E79 (= E83), V266 (= V264), S267 (≠ N265), W271 (= W269), K301 (= K299), F433 (= F428), Q437 (= Q432)
- binding sodium ion: A53 (= A57), I56 (= I60), G57 (≠ S61), A369 (= A365), S372 (= S368), S373 (= S369)
Sites not aligning to the query:
7vsiA Structure of human sglt2-map17 complex bound with empagliflozin (see paper)
33% identity, 84% coverage: 4:460/547 of query aligns to 2:465/586 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 (= N59), H60 (≠ Q64), G63 (= G67), L64 (≠ M68), V75 (≠ I79), F78 (≠ Y82), E79 (= E83), V266 (= V264), S267 (≠ N265), Y270 (= Y268), F433 (= F428), D434 (≠ Q429), Q437 (= Q432)
8hg7A Structure of human sglt2-map17 complex with sotagliflozin (see paper)
33% identity, 84% coverage: 4:460/547 of query aligns to 2:465/590 of 8hg7A
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-methylsulfanyl-oxane-3,4,5-triol: N55 (= N59), G59 (≠ E63), H60 (≠ Q64), G63 (= G67), L64 (≠ M68), E79 (= E83), V266 (= V264), S267 (≠ N265), Y270 (= Y268), W271 (= W269), K301 (= K299), F433 (= F428), Q437 (= Q432)
- binding sodium ion: A53 (= A57), S54 (= S58), I56 (= I60), G57 (≠ S61), A369 (= A365), S372 (= S368), S373 (= S369)
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)
33% identity, 84% coverage: 4:460/547 of query aligns to 22:485/672 of P31639
- V95 (≠ I79) mutation to A: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
- F98 (≠ Y82) mutation to A: Slightly decreases D-glucose transporter activity. Abolishes the binding to inhibitor, empagliflozin.
- V157 (≠ S140) mutation to A: Decreases D-glucose transporter activity.
- L283 (≠ M261) mutation to M: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
- F453 (= F428) mutation to A: Slightly decreases D-glucose transporter activity. Greatly reduces the binding to inhibitor, empagliflozin.
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)
32% identity, 85% coverage: 4:466/547 of query aligns to 25:491/662 of P11170
- C255 (≠ S241) modified: Disulfide link with 608
- Q457 (= Q432) mutation to W: Drasticly decreased affinity for glucose and phlorizin.
- T460 (= T435) mutation to W: Decreased affinity for glucose and phlorizin.
Sites not aligning to the query:
- 608 modified: Disulfide link with 255
Q9NY91 Probable glucose sensor protein SLC5A4; Solute carrier family 5 member 4 from Homo sapiens (Human) (see paper)
30% identity, 84% coverage: 4:460/547 of query aligns to 25:485/659 of Q9NY91
- E457 (≠ Q432) mutation to Q: Confers sugar transport activity not found in the wild-type protein. Increased sensitivity to inhibitor phlorizin.
8hinA Structure of human sglt2-map17 complex with phlorizin (see paper)
32% identity, 84% coverage: 4:460/547 of query aligns to 9:461/588 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 (= S54), A49 (= A57), S50 (= S58), G53 (≠ S61), D177 (= D184), T181 (≠ V188), R276 (= R278), S369 (= S369)
Sites not aligning to the query:
7yniA Structure of human sglt1-map17 complex bound with substrate 4d4fdg in the occluded conformation (see paper)
32% identity, 84% coverage: 44:502/547 of query aligns to 31:491/566 of 7yniA
- binding (2R,3R,4R,5S,6R)-5-fluoranyl-6-(hydroxymethyl)oxane-2,3,4-triol: H51 (≠ Q64), E70 (= E83), L248 (≠ V264), Y252 (= Y268), F415 (= F428), Q419 (= Q432)
Sites not aligning to the query:
Q9ET37 Solute carrier family 5 member 4A; SGLT3-a from Mus musculus (Mouse) (see paper)
31% identity, 84% coverage: 4:460/547 of query aligns to 25:485/656 of Q9ET37
- E457 (≠ Q432) mutation to Q: Confers sodium-dependent sugar transport activity not found in the wild type protein.
7ynjA Structure of human sglt2-map17 complex bound with substrate amg in the occluded conformation (see paper)
31% identity, 83% coverage: 8:460/547 of query aligns to 1:443/564 of 7ynjA
Sites not aligning to the query:
5nv9A Substrate-bound outward-open state of a na+-coupled sialic acid symporter reveals a novel na+-site (see paper)
23% identity, 85% coverage: 3:468/547 of query aligns to 2:436/480 of 5nv9A
- binding sodium ion: A52 (= A57), T53 (≠ S58), L55 (≠ I60), S56 (= S61), V174 (= V180), D178 (= D184), A335 (= A365), S338 (= S368), S338 (= S368), S339 (= S369), S341 (≠ A371), S342 (= S372)
- binding N-acetyl-beta-neuraminic acid: T54 (≠ N59), S56 (= S61), I58 (≠ E63), T59 (≠ Q64), G77 (≠ Y82), Q78 (≠ E83), R131 (≠ N137), F239 (≠ M261)
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)
26% identity, 72% coverage: 2:396/547 of query aligns to 9:378/610 of Q8N695
- V193 (= V188) to I: in dbSNP:rs1709189
- F251 (≠ W262) 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, 74% coverage: 2:404/547 of query aligns to 11:388/643 of Q92911
- A102 (= A94) natural variant: A -> P
- H226 (≠ K232) mutation H->A,D,E,K: Significant loss of iodide transport activity but no effect on its localization to the cell membrane.
- D237 (≠ G243) mutation to A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization.
- Y242 (= Y248) 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 (≠ L249) 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_1871 FitnessBrowser__Cola:Echvi_1871
MTFNTLDLVVFVAYCLLIITMGIVVSREKKGHVKDSKDYFLASKALPWWAVGASLIASNI
SAEQFIGMSGSGFALGLAISTYEWMAAATLLVVAIFFLPIYLKEGIYTMPQFLNRRYDGR
VRTVMAIFWLLIYVFVNLTSVLYLGALSLETIMGVPLTYGIIGLALFAMVYSIYGGLKAV
AWTDVVQVVFLVAGGLATTYLALSLVGDGDVWEGIGILRKAAPSHFSMIIEKGEMMIPDG
SGGSRDAYLDLPGLSVLIGGMWIVNLNYWGCNQYITQRALAAKSLGEAQTGMVFAGFLKL
LMPLIVVIPGIAAYVIVQKGADASFIESMTDPVTGLAKSDRAYPTLLHLLPPGLKGLAFA
ALTAAIVSSLASMANSTSTIFTIDIYKEFFNKNVSEGKQVTIGRITAVVAFIIAAIVAPQ
LRQLDQAFQYIQEYTGFVSPGVFAIFIFGFFWKKTTSNAALTAAVLTIPLSAAFKVITPN
LPFIDRMGVVFLVLSVLIIAISLYEGKGKDSKKAIEVDAELFSTSTKFKVGAVLICGILV
ALYSVFW
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