SitesBLAST
Comparing Ga0059261_0571 FitnessBrowser__Korea:Ga0059261_0571 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)
5nv9A Substrate-bound outward-open state of a na+-coupled sialic acid symporter reveals a novel na+-site (see paper)
33% identity, 60% coverage: 299:777/793 of query aligns to 1:477/480 of 5nv9A
- binding sodium ion: A52 (= A352), T53 (≠ G353), L55 (≠ I355), S56 (= S356), V174 (= V475), D178 (= D479), A335 (= A633), S338 (≠ G636), S338 (≠ G636), S339 (≠ T637), S341 (= S639), S342 (≠ G640)
- binding N-acetyl-beta-neuraminic acid: T54 (≠ S354), S56 (= S356), I58 (= I358), T59 (≠ S359), G77 (≠ S377), Q78 (≠ K378), R131 (= R432), F239 (≠ V537)
Q9Y289 Sodium-dependent multivitamin transporter; Na(+)-dependent multivitamin transporter; hSMVT; Solute carrier family 5 member 6 from Homo sapiens (Human) (see 10 papers)
28% identity, 56% coverage: 299:744/793 of query aligns to 23:470/635 of Q9Y289
- C68 (≠ A343) mutation to A: No effect on biotin transport.
- T78 (≠ G353) mutation to A: Reduced membrane localization. Decrease in biotin transport.
- C104 (≠ M379) mutation to A: No effect on biotin transport.
- R123 (= R398) to L: in SMVTD; reduced membrane localization; impaired biotin transport
- S128 (= S403) mutation to A: No effect on biotin transport.
- N138 (≠ H413) mutation to A: Reduced protein levels. Decrease in biotin transport.
- C144 (≠ L419) mutation to A: No effect on biotin transport.
- Y162 (≠ F438) to C: in COMNB; no effect on membrane localization
- C187 (≠ T463) mutation to A: No effect on biotin transport.
- S242 (≠ D517) mutation to A: No effect on biotin transport.
- S283 (≠ A557) mutation to A: No effect on protein levels or membrane localization.
- T286 (≠ S560) 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 (≠ V568) 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 (≠ Y583) mutation to A: No effect on biotin transport.
- C358 (≠ G629) mutation to A: No effect on biotin transport.
- T366 (= T637) mutation to A: No effect on biotin transport.
- R400 (≠ E670) to T: in SMVTD; impaired biotin transport; dbSNP:rs370950187
- C410 (≠ G680) mutation to A: No effect on biotin transport.
- S429 (≠ E701) to G: in COMNB; no effect on membrane localization
- C443 (≠ T715) mutation to A: No effect on biotin transport.
- C450 (≠ R722) 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)
- 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.
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)
28% identity, 57% coverage: 296:750/793 of query aligns to 8:467/643 of Q92911
- A102 (= A389) natural variant: A -> P
- H226 (≠ F513) mutation H->A,D,E,K: Significant loss of iodide transport activity but no effect on its localization to the cell membrane.
- D237 (= D524) mutation to A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization.
- Y242 (≠ P528) 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 (= T529) 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
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)
27% identity, 54% coverage: 320:750/793 of query aligns to 31:464/610 of Q8N695
- V193 (= V483) to I: in dbSNP:rs1709189
- F251 (= F539) 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.
7sl9A Cryoem structure of smct1 (see paper)
28% identity, 51% coverage: 348:750/793 of query aligns to 38:443/497 of 7sl9A
7uuzA Structure of the sodium/iodide symporter (nis) in complex with perrhenate and sodium (see paper)
27% identity, 51% coverage: 347:750/793 of query aligns to 35:437/501 of 7uuzA
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)
25% identity, 45% coverage: 304:658/793 of query aligns to 25:414/672 of P31639
- V95 (≠ Y374) mutation to A: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
- F98 (≠ S377) mutation to A: Slightly decreases D-glucose transporter activity. Abolishes the binding to inhibitor, empagliflozin.
- V157 (≠ I435) mutation to A: Decreases D-glucose transporter activity.
- L283 (= L538) mutation to M: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
Sites not aligning to the query:
- 453 F→A: Slightly decreases D-glucose transporter activity. Greatly reduces the binding to inhibitor, empagliflozin.
8hg7A Structure of human sglt2-map17 complex with sotagliflozin (see paper)
25% identity, 45% coverage: 304:658/793 of query aligns to 5:394/590 of 8hg7A
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-methylsulfanyl-oxane-3,4,5-triol: N55 (≠ S354), G59 (≠ I358), H60 (≠ S359), G63 (≠ A362), L64 (≠ I363), E79 (≠ K378), V266 (= V541), S267 (≠ V542), Y270 (≠ T544), W271 (≠ F545), K301 (≠ L575)
- binding sodium ion: A53 (= A352), S54 (≠ G353), I56 (= I355), G57 (≠ S356), A369 (= A633), S372 (≠ G636), S373 (≠ T637)
Sites not aligning to the query:
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-methylsulfanyl-oxane-3,4,5-triol: 433, 437
- binding : 579, 583, 584, 587, 588
7vsiA Structure of human sglt2-map17 complex bound with empagliflozin (see paper)
25% identity, 45% coverage: 304:658/793 of query aligns to 5:394/586 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 (≠ S354), H60 (≠ S359), G63 (≠ A362), L64 (≠ I363), V75 (≠ Y374), F78 (≠ S377), E79 (≠ K378), V266 (= V541), S267 (≠ V542), Y270 (≠ T544)
Sites not aligning to the query:
8hdhA Structure of human sglt2-map17 complex with canagliflozin (see paper)
25% identity, 45% coverage: 304:658/793 of query aligns to 5:394/586 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 (≠ S354), G59 (≠ I358), H60 (≠ S359), G63 (≠ A362), L64 (≠ I363), F78 (≠ S377), E79 (≠ K378), S267 (≠ V542), W271 (≠ F545)
- binding sodium ion: A53 (= A352), S54 (≠ G353), I56 (= I355), G57 (≠ S356), A369 (= A633), S372 (≠ G636), S373 (≠ T637)
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: 433, 434, 437, 506
- binding : 575, 579, 580, 583, 584
8hb0A Structure of human sglt2-map17 complex with ta1887 (see paper)
25% identity, 45% coverage: 304:658/793 of query aligns to 5:394/586 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 (≠ S354), H60 (≠ S359), G63 (≠ A362), L64 (≠ I363), T67 (≠ K366), V75 (≠ Y374), F78 (≠ S377), E79 (≠ K378), V137 (≠ I435), V266 (= V541), S267 (≠ V542), W271 (≠ F545)
- binding sodium ion: A53 (= A352), I56 (= I355), G57 (≠ S356), A369 (= A633), S372 (≠ G636), S373 (≠ T637)
Sites not aligning to the query:
- binding (2R,3R,4S,5S,6R)-2-[3-[(4-cyclopropylphenyl)methyl]-4-fluoranyl-indol-1-yl]-6-(hydroxymethyl)oxane-3,4,5-triol: 433, 437
- binding : 575, 576, 579, 580, 583, 584
8hezA Structure of human sglt2-map17 complex with dapagliflozin (see paper)
25% identity, 45% coverage: 304:658/793 of query aligns to 5:394/582 of 8hezA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (≠ S354), G59 (≠ I358), H60 (≠ S359), G63 (≠ A362), L64 (≠ I363), T67 (≠ K366), F78 (≠ S377), E79 (≠ K378), V266 (= V541), S267 (≠ V542), W271 (≠ F545), K301 (≠ L575)
- binding sodium ion: A53 (= A352), I56 (= I355), G57 (≠ S356), A369 (= A633), S372 (≠ G636), S373 (≠ T637)
Sites not aligning to the query:
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: 433, 437
- binding : 568, 571, 572, 575, 576, 579, 580
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, 55% coverage: 304:738/793 of query aligns to 28:495/662 of P11170
- C255 (≠ S522) modified: Disulfide link with 608
- Q457 (≠ I700) mutation to W: Drasticly decreased affinity for glucose and phlorizin.
- T460 (≠ F703) 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)
22% identity, 53% coverage: 304:727/793 of query aligns to 28:484/659 of Q9NY91
- E457 (≠ I700) mutation to Q: Confers sugar transport activity not found in the wild-type protein. Increased sensitivity to inhibitor phlorizin.
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)
24% identity, 53% coverage: 304:727/793 of query aligns to 28:484/664 of P13866
- N51 (≠ K327) to S: in GGM; slightly decreased activity; dbSNP:rs17683011
- W67 (≠ A343) mutation to A: Strong reduction in D-glucose transporter activity.
- S77 (≠ G353) mutation to A: Loss of activity.
- H83 (≠ S359) 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 (= R411) to W: in GGM; loss of activity
- S159 (≠ G434) to P: in GGM; loss of activity
- A166 (= A441) to T: in GGM; about 90% reduction in activity
- D204 (= D479) mutation to A: Loss of activity.
- N248 (≠ K515) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to Q: Loss of N-glycosylation.
- C255 (vs. gap) modified: Disulfide link with 511
- W276 (= W531) to L: in GGM; about 95% reduction in activity
- T287 (≠ V541) 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 (≠ T544) 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 (≠ F545) mutation to A: Loss of D-glucose transporter activity.
- C292 (≠ P546) to Y: in GGM; loss of activity; mutation to A: Has no effect on water permeability.
- Q295 (= Q549) to R: in GGM; loss of activity
- R300 (= R554) to S: in GGM; loss of activity
- A304 (≠ T558) to V: in GGM; impairs trafficking to the plasma membrane
- K321 (≠ L575) mutation to Q: Acquires D-mannose and D-allose transporter activity comparable to glucose and galactose.
- C345 (≠ Q599) modified: Disulfide link with 351
- C351 (vs. gap) modified: Disulfide link with 345
- C355 (vs. gap) modified: Disulfide link with 361
- C361 (≠ P605) modified: Disulfide link with 355
- N363 (≠ D607) mutation to A: Loss of water permeation.
- L369 (≠ F613) to S: in GGM; loss of activity
- R379 (≠ T623) to Q: in GGM; loss of activity
- A388 (= A632) to V: in GGM; loss of activity
- S396 (≠ G640) mutation to A: Loss of activity.
- F405 (≠ L649) to S: in GGM; loss of activity
- A411 (≠ G655) to T: in GGM; slightly decreased activity; dbSNP:rs17683430
- G426 (≠ E670) to R: in GGM; loss of activity
- Q451 (≠ S694) mutation to A: Strong reduction in water permeation.
- L452 (= L695) mutation to A: Loss of water permeation.
- D454 (= D697) mutation to A: Has no effect on water permeation.
- Q457 (≠ I700) mutation to A: Loss of D-glucose transporter activity.; mutation to C: Strong reduction in D-glucose transporter activity.
- T460 (≠ F703) mutation to A: Loss of D-glucose transporter activity.
- V470 (≠ A713) 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.
7wmvA Structure of human sglt1-map17 complex bound with lx2761 (see paper)
24% identity, 53% coverage: 304:727/793 of query aligns to 11:467/602 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 (≠ S354), H66 (≠ S359), L70 (≠ I363), I81 (vs. gap), F84 (≠ W372), L257 (vs. gap), M266 (≠ V537), L269 (≠ D540), T270 (≠ V541), Y273 (≠ T544), W274 (≠ F545), F436 (≠ L696), D437 (= D697), Q440 (≠ I700)
Sites not aligning to the query:
3dh4A Crystal structure of sodium/sugar symporter with bound galactose from vibrio parahaemolyticus (see paper)
25% identity, 50% coverage: 339:735/793 of query aligns to 20:428/512 of 3dh4A
8hinA Structure of human sglt2-map17 complex with phlorizin (see paper)
24% identity, 45% coverage: 304:658/793 of query aligns to 12:390/588 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 (= S349), A49 (= A352), S50 (≠ G353), G53 (≠ S356), D177 (= D479), T181 (≠ V483), R276 (= R554), S369 (≠ T637)
Sites not aligning to the query:
7sl8A Cryoem structure of sglt1 at 3.4 a resolution (see paper)
24% identity, 49% coverage: 338:727/793 of query aligns to 30:452/582 of 7sl8A
Sites not aligning to the query:
7slaA Cryoem structure of sglt1 at 3.15 angstrom resolution (see paper)
24% identity, 49% coverage: 338:727/793 of query aligns to 31:453/585 of 7slaA
Sites not aligning to the query:
Query Sequence
>Ga0059261_0571 FitnessBrowser__Korea:Ga0059261_0571
MTARLLSWPLAVLLLVLTSVAPAMAGTGAPVSSKTSPLPALPDTGDRIRLAGVDGQPVVL
DGRRAFRLSADKRRWEPLRADALADLGEIAAASDGNRTVLIAGRGGVAERIVRLTIANDG
LAVHPLAALPVPLHAAQAAIRDDSIWLAGLGPDGAARLYKASLSAPGRWAAQAAWPGGAA
PVALGAQNKGVFVTLADGAQWRWFSDKGWRVGARAPAAIVPGSTRAIGQAYLLYLGSGAD
GATRLYSYSAITDAWAALGAPQAGTPQAAVSYGEGLLAARSNANGLAFTTTELVSERQSL
ALLDWLIIGVYMFGMLGVGFYFYRGAKNGSSNEFFLGSRSIPAWAAGISMFAGSISSISY
LAIPAKAYETNWQYIMSKMSTIAGLIFVAIMIVPLFRRLNLVSVFNYLETRFHPSIRLLS
SALWMLMQIGGRMGIVLFLPAMAIGTITDTNIVACIVVVGIFTIIYTALGGMKAVVWTDV
FQVMVLTGGACFAIGFIIYQLGLMPVVETARAFEKTDMVNLSFDITQPTLWGFLILVLFD
VVLTFPKDQVLMQRVLATPSEKEASRSVWVFAVVLLPSAFMFYIIGTVLFAYYRENPAQL
NPMLPIDAVFPAFIGTELPAGVTGLIIAGLFAAAMGTLSGIINSVATLLSVDFYGKFRNP
TQEQTVRFAEWMSVVVGLIGIGIAIILSRMDIHSLLDLTIELFGLLGGSCAGAYTLGMFT
RRANWQGVAIGIVAASLLTLVVWIFGLIHPYWYLALAIMASIVIGYLASLLFPPPSHSLE
GLTIYDKARKQAA
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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