SitesBLAST
Comparing Echvi_1880 FitnessBrowser__Cola:Echvi_1880 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)
52% identity, 76% coverage: 46:520/624 of query aligns to 20:471/512 of 3dh4A
7wmvA Structure of human sglt1-map17 complex bound with lx2761 (see paper)
34% identity, 74% coverage: 9:469/624 of query aligns to 11:470/602 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 (= N61), H66 (= H66), L70 (≠ T70), I81 (= I81), F84 (≠ Y84), L257 (= L254), M266 (= M264), L269 (≠ T267), T270 (≠ N268), Y273 (= Y271), W274 (= W272), F436 (= F435), D437 (≠ Q436), Q440 (= Q439)
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)
34% identity, 74% coverage: 9:469/624 of query aligns to 28:487/664 of P13866
- N51 (≠ K31) to S: in GGM; slightly decreased activity; dbSNP:rs17683011
- W67 (= W50) mutation to A: Strong reduction in D-glucose transporter activity.
- S77 (≠ A60) mutation to A: Loss of activity.
- H83 (= H66) 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 (= R118) to W: in GGM; loss of activity
- S159 (≠ T141) to P: in GGM; loss of activity
- A166 (= A148) to T: in GGM; about 90% reduction in activity
- D204 (= D186) mutation to A: Loss of activity.
- N248 (≠ K226) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to Q: Loss of N-glycosylation.
- C255 (≠ V238) modified: Disulfide link with 511
- W276 (≠ G256) to L: in GGM; about 95% reduction in activity
- T287 (≠ N268) 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 (= Y271) 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 (= W272) mutation to A: Loss of D-glucose transporter activity.
- C292 (≠ G273) to Y: in GGM; loss of activity; mutation to A: Has no effect on water permeability.
- Q295 (= Q276) to R: in GGM; loss of activity
- R300 (≠ K281) to S: in GGM; loss of activity
- A304 (= A285) to V: in GGM; impairs trafficking to the plasma membrane
- K321 (= K302) mutation to Q: Acquires D-mannose and D-allose transporter activity comparable to glucose and galactose.
- C345 (≠ A330) modified: Disulfide link with 351
- C351 (≠ V336) modified: Disulfide link with 345
- C355 (≠ I339) modified: Disulfide link with 361
- C361 (≠ K344) modified: Disulfide link with 355
- N363 (≠ D346) mutation to A: Loss of water permeation.
- L369 (= L352) to S: in GGM; loss of activity
- R379 (= R362) to Q: in GGM; loss of activity
- A388 (= A371) to V: in GGM; loss of activity
- S396 (= S379) mutation to A: Loss of activity.
- F405 (= F388) to S: in GGM; loss of activity
- A411 (≠ V395) to T: in GGM; slightly decreased activity; dbSNP:rs17683430
- G426 (= G410) to R: in GGM; loss of activity
- Q451 (= Q433) mutation to A: Strong reduction in water permeation.
- L452 (≠ V434) mutation to A: Loss of water permeation.
- D454 (≠ Q436) mutation to A: Has no effect on water permeation.
- Q457 (= Q439) mutation to A: Loss of D-glucose transporter activity.; mutation to C: Strong reduction in D-glucose transporter activity.
- T460 (= T442) mutation to A: Loss of D-glucose transporter activity.
- V470 (= V452) 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.
7sl8A Cryoem structure of sglt1 at 3.4 a resolution (see paper)
35% identity, 74% coverage: 9:469/624 of query aligns to 9:455/582 of 7sl8A
Sites not aligning to the query:
7slaA Cryoem structure of sglt1 at 3.15 angstrom resolution (see paper)
35% identity, 74% coverage: 9:469/624 of query aligns to 10:456/585 of 7slaA
Sites not aligning to the query:
7vsiA Structure of human sglt2-map17 complex bound with empagliflozin (see paper)
35% identity, 74% coverage: 9:469/624 of query aligns to 5:467/586 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 (= N61), H60 (= H66), G63 (= G69), L64 (≠ T70), V75 (≠ I81), F78 (≠ Y84), E79 (= E85), V266 (≠ T267), S267 (≠ N268), Y270 (= Y271), F433 (= F435), D434 (≠ Q436), Q437 (= Q439)
8hg7A Structure of human sglt2-map17 complex with sotagliflozin (see paper)
35% identity, 74% coverage: 9:469/624 of query aligns to 5:467/590 of 8hg7A
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-methylsulfanyl-oxane-3,4,5-triol: N55 (= N61), G59 (≠ E65), H60 (= H66), G63 (= G69), L64 (≠ T70), E79 (= E85), V266 (≠ T267), S267 (≠ N268), Y270 (= Y271), W271 (= W272), K301 (= K302), F433 (= F435), Q437 (= Q439)
- binding sodium ion: A53 (= A59), S54 (≠ A60), I56 (= I62), G57 (≠ S63), A369 (= A372), S372 (= S375), S373 (= S376)
Sites not aligning to the query:
8hdhA Structure of human sglt2-map17 complex with canagliflozin (see paper)
35% identity, 74% coverage: 9:469/624 of query aligns to 5:467/586 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 (= N61), G59 (≠ E65), H60 (= H66), G63 (= G69), L64 (≠ T70), F78 (≠ Y84), E79 (= E85), S267 (≠ N268), W271 (= W272), F433 (= F435), D434 (≠ Q436), Q437 (= Q439)
- binding sodium ion: A53 (= A59), S54 (≠ A60), I56 (= I62), G57 (≠ S63), A369 (= A372), S372 (= S375), S373 (= S376)
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)
35% identity, 74% coverage: 9:469/624 of query aligns to 5:467/586 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 (= N61), H60 (= H66), G63 (= G69), L64 (≠ T70), T67 (≠ S73), V75 (≠ I81), F78 (≠ Y84), E79 (= E85), V137 (≠ S142), V266 (≠ T267), S267 (≠ N268), W271 (= W272), F433 (= F435), Q437 (= Q439)
- binding sodium ion: A53 (= A59), I56 (= I62), G57 (≠ S63), A369 (= A372), S372 (= S375), S373 (= S376)
Sites not aligning to the query:
8hezA Structure of human sglt2-map17 complex with dapagliflozin (see paper)
35% identity, 74% coverage: 9:469/624 of query aligns to 5:467/582 of 8hezA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (= N61), G59 (≠ E65), H60 (= H66), G63 (= G69), L64 (≠ T70), T67 (≠ S73), F78 (≠ Y84), E79 (= E85), V266 (≠ T267), S267 (≠ N268), W271 (= W272), K301 (= K302), F433 (= F435), Q437 (= Q439)
- binding sodium ion: A53 (= A59), I56 (= I62), G57 (≠ S63), A369 (= A372), S372 (= S375), S373 (= S376)
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)
35% identity, 74% coverage: 9:469/624 of query aligns to 25:487/672 of P31639
- V95 (≠ I81) mutation to A: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
- F98 (≠ Y84) mutation to A: Slightly decreases D-glucose transporter activity. Abolishes the binding to inhibitor, empagliflozin.
- V157 (≠ S142) mutation to A: Decreases D-glucose transporter activity.
- L283 (≠ M264) mutation to M: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
- F453 (= F435) 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, 74% coverage: 9:469/624 of query aligns to 28:487/662 of P11170
- C255 (≠ L244) modified: Disulfide link with 608
- Q457 (= Q439) mutation to W: Drasticly decreased affinity for glucose and phlorizin.
- T460 (= T442) 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)
33% identity, 74% coverage: 9:469/624 of query aligns to 12:463/588 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 (= S56), A49 (= A59), S50 (≠ A60), G53 (≠ S63), D177 (= D186), T181 (≠ V190), R276 (≠ K281), S369 (= S376)
Sites not aligning to the query:
Q9NY91 Probable glucose sensor protein SLC5A4; Solute carrier family 5 member 4 from Homo sapiens (Human) (see paper)
29% identity, 76% coverage: 9:483/624 of query aligns to 28:501/659 of Q9NY91
- E457 (≠ Q439) mutation to Q: Confers sugar transport activity not found in the wild-type protein. Increased sensitivity to inhibitor phlorizin.
7yniA Structure of human sglt1-map17 complex bound with substrate 4d4fdg in the occluded conformation (see paper)
32% identity, 74% coverage: 9:469/624 of query aligns to 10:449/566 of 7yniA
- binding (2R,3R,4R,5S,6R)-5-fluoranyl-6-(hydroxymethyl)oxane-2,3,4-triol: H51 (= H66), E70 (= E85), L248 (≠ T267), Y252 (= Y271), F415 (= F435), Q419 (= Q439)
Sites not aligning to the query:
7ynjA Structure of human sglt2-map17 complex bound with substrate amg in the occluded conformation (see paper)
33% identity, 73% coverage: 16:469/624 of query aligns to 7:445/564 of 7ynjA
Sites not aligning to the query:
Q9ET37 Solute carrier family 5 member 4A; SGLT3-a from Mus musculus (Mouse) (see paper)
30% identity, 76% coverage: 9:480/624 of query aligns to 28:498/656 of Q9ET37
- E457 (≠ Q439) mutation to Q: Confers sodium-dependent sugar transport activity not found in the wild type protein.
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, 67% coverage: 5:422/624 of query aligns to 10:399/610 of Q8N695
- V193 (= V190) to I: in dbSNP:rs1709189
- F251 (≠ W265) 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, 63% coverage: 5:398/624 of query aligns to 12:376/643 of Q92911
- A102 (= A96) natural variant: A -> P
- H226 (≠ D224) mutation H->A,D,E,K: Significant loss of iodide transport activity but no effect on its localization to the cell membrane.
- D237 (≠ Q235) mutation to A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization.
- Y242 (≠ D249) 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 (≠ A250) 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
7sl9A Cryoem structure of smct1 (see paper)
27% identity, 59% coverage: 53:422/624 of query aligns to 36:378/497 of 7sl9A
Query Sequence
>Echvi_1880 FitnessBrowser__Cola:Echvi_1880
MSAGFSTLDYVIFIVYALAIVSVGLWVSRTKKGLEKTAQEYFLADKSLTWWAVGASLLAA
NISAEHFIGTSGSGFAIGLGISAYEWIAAIALIIVAKYFLPIFLKHGVYTMPQFLSERFN
KGVSTAFAVFWLLVYVFVNLTSVSYLGALALDKIMGIPLQYGIIGLLIFSGIYSIYGGLE
AVAWTDVVQVIILVAGGLITTFLALDAVGMGDGIFAGMSNLYNDAKDHFVMIMPQGRVMV
PDGLGGSRDAFQDLPGLAVILGGMWLTNLGYWGFNQYIIQKGLAAKSIEEAKKGLLFAGY
LKLLMPIIVVIPGIAAYVLINDYSPEQLAAILNMPVEHIGTIQKSDEAYPWLLRNFIPNG
IRGLAFAALAAAIVSSLASMINSTSTIFTMDIYKVYFKPNANNHQLVRTGRIVAVVALAI
AMIVAPQLASLDQVFQYIQEYTGYIYPGVVVVFGMGLIWRQATASAALWTAIATIPAGIV
FKIFYPEMPFLLRMGYVFIILCFIASLISFAEKKKFANPDYKTNKQAAKTVASSYFFIIL
GIICAVLGFALFNSYEHVGIESIFMIAALFLMLGTILYTNVKMETADPKSFNTDPVLFNT
TSSFNLGAAGIILIVGLLYYFFWM
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