SitesBLAST
Comparing AO353_12815 FitnessBrowser__pseudo3_N2E3:AO353_12815 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 16 hits to proteins with known functional sites (download)
P07117 Sodium/proline symporter; Proline carrier; Proline permease; Propionate transporter from Escherichia coli (strain K12) (see 4 papers)
76% identity, 99% coverage: 1:491/494 of query aligns to 1:492/502 of P07117
- R257 (= R257) mutation to C: Sodium-independent binding affinity for proline.
- C281 (= C281) 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 (= C344) mutation to S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
- C349 (= C349) 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 (= R376) mutation R->E,Q: No change in activity.; mutation to K: Loss of activity.
3dh4A Crystal structure of sodium/sugar symporter with bound galactose from vibrio parahaemolyticus (see paper)
25% identity, 74% coverage: 72:435/494 of query aligns to 43:426/512 of 3dh4A
Sites not aligning to the query:
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)
24% identity, 73% coverage: 33:391/494 of query aligns to 43:401/610 of Q8N695
- V193 (≠ A191) to I: in dbSNP:rs1709189
- F251 (≠ M242) 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.
Q9GZV3 High affinity choline transporter 1; hCHT1; Hemicholinium-3-sensitive choline transporter; CHT; Solute carrier family 5 member 7 from Homo sapiens (Human) (see 5 papers)
26% identity, 87% coverage: 8:437/494 of query aligns to 8:442/580 of Q9GZV3
- D48 (≠ S41) to G: in CMS20; decreased choline transmembrane transporter activity; no effect on localization at plasma membrane; dbSNP:rs886039768
- G65 (= G58) to E: in CMS20; loss of choline transmembrane transporter activity; no effect on localization at plasma membrane; dbSNP:rs886039765
- I89 (= I80) to V: 40% reduction in choline transmembrane transporter activity; found in 0.06 of Ashkenazi Jews; dbSNP:rs1013940; mutation to A: Decreased choline transmembrane transporter activity, only 20% of wild-type choline uptake activity.
- P105 (≠ R96) to S: in CMS20; decreased choline transmembrane transporter activity; no effect on localization at plasma membrane; dbSNP:rs886039766
- Y111 (≠ A107) to H: in CMS20; no effect on localization at plasma membrane
- Y175 (= Y174) to C: in CMS20; uncertain significance; dbSNP:rs1331713195
- I291 (≠ V288) to T: in CMS20; uncertain significance; dbSNP:rs375397889
- V344 (= V338) to L: in CMS20; uncertain significance
- R361 (≠ E355) to Q: in CMS20; decreased choline transmembrane transporter activity; no effect on localization at plasma membrane; dbSNP:rs147656110
- F418 (≠ G413) to V: in CMS20; uncertain significance
Sites not aligning to the query:
- 446 R → G: in CMS20; decreased choline transmembrane transporter activity; no effect on localization at plasma membrane
- 451 E→Q: Decreased choline transmembrane transporter activity, only 5% of wild-type choline uptake activity.
- 527:532 Dileucine-like motif
- 530 I→A: No change in protein internalization. No change in choline transmembrane transporter activity.
- 531 L→A: Loss of protein internalization to vesicular structures in neurons. Increased choline transmembrane transporter activity.
- 531:532 LV→AA: Decreased protein internalization; when associated with V-538. Increased choline transmembrane transporter activity; when associated with V-538.
- 532 V→A: Decreased protein internalization. Increased choline transmembrane transporter activity.
- 538 K→V: Decreased protein internalization; when associated with 531-L-V-532. Increased choline transmembrane transporter activity; when associated with 531-L-V-532.
Q9ET37 Solute carrier family 5 member 4A; SGLT3-a from Mus musculus (Mouse) (see paper)
23% identity, 86% coverage: 12:437/494 of query aligns to 33:492/656 of Q9ET37
- E457 (≠ A406) mutation to Q: Confers sodium-dependent sugar transport activity not found in the wild type protein.
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)
24% identity, 87% coverage: 12:439/494 of query aligns to 33:494/662 of P11170
- C255 (≠ F227) modified: Disulfide link with 608
- Q457 (≠ S402) mutation to W: Drasticly decreased affinity for glucose and phlorizin.
- T460 (≠ W405) mutation to W: Decreased affinity for glucose and phlorizin.
Sites not aligning to the query:
- 608 modified: Disulfide link with 255
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)
22% identity, 74% coverage: 24:391/494 of query aligns to 36:403/643 of Q92911
- A102 (≠ W90) natural variant: A -> P
- H226 (≠ Q222) mutation H->A,D,E,K: Significant loss of iodide transport activity but no effect on its localization to the cell membrane.
- D237 (= D228) mutation to A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization.
- Y242 (≠ T233) 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 (≠ S234) 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)
24% identity, 71% coverage: 41:391/494 of query aligns to 30:380/497 of 7sl9A
7slaA Cryoem structure of sglt1 at 3.15 angstrom resolution (see paper)
22% identity, 74% coverage: 66:430/494 of query aligns to 49:454/585 of 7slaA
Sites not aligning to the query:
7sl8A Cryoem structure of sglt1 at 3.4 a resolution (see paper)
22% identity, 74% coverage: 66:430/494 of query aligns to 48:453/582 of 7sl8A
Sites not aligning to the query:
Q9NY91 Probable glucose sensor protein SLC5A4; Solute carrier family 5 member 4 from Homo sapiens (Human) (see paper)
27% identity, 37% coverage: 12:195/494 of query aligns to 33:212/659 of Q9NY91
Sites not aligning to the query:
- 457 E→Q: Confers sugar transport activity not found in the wild-type protein. Increased sensitivity to inhibitor phlorizin.
7wmvA Structure of human sglt1-map17 complex bound with lx2761 (see paper)
29% identity, 41% coverage: 12:213/494 of query aligns to 16:213/602 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 (≠ D55), H66 (≠ L60), L70 (= L64), I81 (= I80), F84 (vs. gap)
Sites not aligning to the query:
- 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: 257, 266, 269, 270, 273, 274, 436, 437, 440, 508
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, 41% coverage: 12:213/494 of query aligns to 33:230/664 of P13866
- N51 (= N30) to S: in GGM; slightly decreased activity; dbSNP:rs17683011
- W67 (≠ S44) mutation to A: Strong reduction in D-glucose transporter activity.
- S77 (= S54) mutation to A: Loss of activity.
- H83 (≠ L60) 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 (= R117) to W: in GGM; loss of activity
- S159 (≠ C141) to P: in GGM; loss of activity
- A166 (= A149) to T: in GGM; about 90% reduction in activity
- D204 (= D187) mutation to A: Loss of activity.
Sites not aligning to the query:
- 191:664 natural variant: Missing (in GGM; loss of activity)
- 248 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→Q: Loss of N-glycosylation.
- 255 modified: Disulfide link with 511
- 276 W → L: in GGM; about 95% reduction in activity
- 287 T→A: Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with L-83 and C-290.; T→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.
- 290 Y→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.
- 291 W→A: Loss of D-glucose transporter activity.
- 292 C → Y: in GGM; loss of activity; C→A: Has no effect on water permeability.
- 295 Q → R: in GGM; loss of activity
- 300 R → S: in GGM; loss of activity
- 304 A → V: in GGM; impairs trafficking to the plasma membrane
- 321 K→Q: Acquires D-mannose and D-allose transporter activity comparable to glucose and galactose.
- 345 modified: Disulfide link with 351
- 351 modified: Disulfide link with 345
- 355 modified: Disulfide link with 361
- 361 modified: Disulfide link with 355
- 363 N→A: Loss of water permeation.
- 369 L → S: in GGM; loss of activity
- 379 R → Q: in GGM; loss of activity
- 379:664 natural variant: Missing (in GGM; loss of activity)
- 388 A → V: in GGM; loss of activity
- 396 S→A: Loss of activity.
- 405 F → S: in GGM; loss of activity
- 411 A → T: in GGM; slightly decreased activity; dbSNP:rs17683430
- 426 G → R: in GGM; loss of activity
- 451 Q→A: Strong reduction in water permeation.
- 452 L→A: Loss of water permeation.
- 454 D→A: Has no effect on water permeation.
- 457 Q→A: Loss of D-glucose transporter activity.; Q→C: Strong reduction in D-glucose transporter activity.
- 460 T→A: Loss of D-glucose transporter activity.
- 470 V → N: in GGM; about 90% reduction in activity; requires 2 nucleotide substitutions
- 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.
Q9Y289 Sodium-dependent multivitamin transporter; Na(+)-dependent multivitamin transporter; hSMVT; Solute carrier family 5 member 6 from Homo sapiens (Human) (see 10 papers)
20% identity, 73% coverage: 30:390/494 of query aligns to 54:414/635 of Q9Y289
- C68 (≠ S44) mutation to A: No effect on biotin transport.
- T78 (≠ S54) mutation to A: Reduced membrane localization. Decrease in biotin transport.
- C104 (vs. gap) mutation to A: No effect on biotin transport.
- R123 (= R96) to L: in SMVTD; reduced membrane localization; impaired biotin transport
- S128 (≠ T101) mutation to A: No effect on biotin transport.
- N138 (≠ E119) mutation to A: Reduced protein levels. Decrease in biotin transport.
- C144 (≠ I128) mutation to A: No effect on biotin transport.
- Y162 (≠ V146) to C: in COMNB; no effect on membrane localization
- C187 (≠ T171) mutation to A: No effect on biotin transport.
- S242 (vs. gap) mutation to A: No effect on biotin transport.
- S283 (≠ A260) mutation to A: No effect on protein levels or membrane localization.
- T286 (≠ S263) mutation to A: Resistant to phorbol 12-myristate 13-acetate (PMA)-induced inhibition of biotin transport. No effect on protein levels or membrane localization.
- C294 (≠ N269) mutation to A: Reduced membrane localization. Decrease in biotin transport (decreased Vmax, no change in Km).; mutation C->S,M: Decrease in biotin transport.
- C309 (≠ V286) mutation to A: No effect on biotin transport.
- C358 (≠ A333) mutation to A: No effect on biotin transport.
- T366 (= T341) mutation to A: No effect on biotin transport.
- R400 (= R376) to T: in SMVTD; impaired biotin transport; dbSNP:rs370950187
- C410 (≠ A386) mutation to A: No effect on biotin transport.
Sites not aligning to the query:
- 94:635 natural variant: Missing (in SMVTD and COMNB; reduced membrane localization; impaired biotin transport; dbSNP:rs994218778)
- 429 S → G: in COMNB; no effect on membrane localization
- 443 C→A: No effect on biotin transport.
- 450 C→A: No effect on biotin transport.
- 481 S → F: in dbSNP:rs1395
- 489 N→A: Slight decrease in protein levels. Decrease in biotin transport.
- 498 N→A: No effect on biotin transport.
- 534 N→A: No effect on biotin transport.
- 567:635 mutation Missing: Loss of biotin transport. Loss of membrane localization.
- 570:635 mutation Missing: Loss of biotin transport. Loss of membrane localization.
- 575:635 mutation Missing: Partial loss (75%) of biotine transport. Apical membrane localization and intracellular structure localization in polarized cells.
- 577 C→A: No effect on biotin transport.
- 583 C→A: No effect on biotin transport.
- 584:635 mutation Missing: Partial loss (75%) of biotine transport. Apical membrane localization and intracellular structure localization in polarized cells.
- 600:635 mutation Missing: Partial loss (75%) of biotine transport. Apical membrane localization and intracellular structure localization in polarized cells.
- 612:635 mutation Missing: Partial loss (75%) of biotine transport. Apical membrane localization and intracellular structure localization in polarized cells.
- 616:635 mutation Missing: Loss of apical membrane localization in polarized cells. Basolateral localization in polarized cells.
- 620:635 mutation Missing: Partial loss (25%) of biotine transport. No change in apical membrane localization in polarized cells.
- 624:635 mutation Missing: Partial loss (25%) of biotine transport. No change in apical membrane localization in polarized cells.
- 627 T→A: No effect on biotin transport.
- 628 mutation C->A,S: Decrease in biotin transport.
- 632:635 mutation Missing: Partial loss (25%) of biotine transport. No change in apical membrane localization in polarized cells.
5nv9A Substrate-bound outward-open state of a na+-coupled sialic acid symporter reveals a novel na+-site (see paper)
22% identity, 60% coverage: 14:309/494 of query aligns to 13:307/480 of 5nv9A
- binding sodium ion: A52 (= A53), T53 (≠ S54), L55 (≠ M56), S56 (= S57), V174 (= V183), D178 (= D187)
- binding N-acetyl-beta-neuraminic acid: T54 (≠ D55), S56 (= S57), I58 (≠ W59), T59 (≠ L60), G77 (≠ E75), Q78 (≠ S76), R131 (≠ A130), F239 (≠ L241)
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, 21% coverage: 326:431/494 of query aligns to 340:448/566 of 7yniA
Sites not aligning to the query:
- binding (2R,3R,4R,5S,6R)-5-fluoranyl-6-(hydroxymethyl)oxane-2,3,4-triol: 51, 70, 248, 252
- binding : 548, 552, 555, 556, 559, 560, 563, 564
Query Sequence
>AO353_12815 FitnessBrowser__pseudo3_N2E3:AO353_12815
MSASNPTLITFVIYIAAMVLIGFMAYRSTNNLSDYILGGRSLGSVVTALSAGASDMSGWL
LMGLPGAIYMSGLSESWIAIGLIVGAYLNWLFVAGRLRVQTEHNGDALTLPDYFSSRFED
KSGLLRIISAVVILVFFTIYCASGIVAGARLFESTFGMSYETALWAGAAATIAYTFVGGF
LAVSWTDTVQATLMIFALLLTPIIVLLATGGIDTTFLAIEAQDPGNFDMLKNTSFIGIIS
LMGWGLGYFGQPHILARFMAADSVKSIANARRISMTWMILCLGGTVAVGFFGIAYFSANP
AVAMPVSENHERVFIELAKILFNPWIAGVLLSAILAAVMSTLSCQLLVCSSALTEDFYKS
FLRKNASQVELVWVGRAMVLAVALIAIALAANPENRVLGLVSYAWAGFGAAFGPVVLISV
LWKGMTRNGALAGIVVGALTVIVWKHFNLLGLYEIIPGFIFASLAILLVSKMGVPSAGML
QRFAAAEKDFHLNK
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