SitesBLAST
Comparing 6937849 FitnessBrowser__SB2B:6937849 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)
5da0A Structure of the the slc26 transporter slc26dg in complex with a nanobody (see paper)
45% identity, 95% coverage: 6:495/518 of query aligns to 2:466/467 of 5da0A
Q55415 Bicarbonate transporter BicA from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
31% identity, 93% coverage: 13:495/518 of query aligns to 13:519/564 of Q55415
- T69 (= T69) binding ; mutation to A: Alters bicarbonate transport.
- D258 (≠ E254) binding ; mutation D->A,E: Alters bicarbonate transport.
- T262 (= T258) binding ; mutation to A: Alters bicarbonate transport.
- G300 (≠ A296) binding
- A301 (≠ M297) binding
- T302 (≠ I298) binding ; mutation to A: Alters bicarbonate transport.
- A471 (≠ D447) mutation to N: Alters bicarbonate transport.
- L476 (≠ F452) mutation to S: Alters bicarbonate transport.
- A486 (= A462) mutation to E: Alters bicarbonate transport.
- L490 (≠ I466) mutation to Q: Alters bicarbonate transport.
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
35% identity, 73% coverage: 13:388/518 of query aligns to 12:391/392 of 6ki1B
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
24% identity, 96% coverage: 2:497/518 of query aligns to 14:552/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (≠ F105), R127 (≠ K106), W130 (≠ K109)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (= L107), L131 (≠ F110), E409 (≠ A385), L413 (≠ F389), G417 (≠ I393), A421 (= A396)
- binding sulfate ion: A84 (≠ V75), S321 (≠ M297), F322 (≠ I298)
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
25% identity, 93% coverage: 15:497/518 of query aligns to 26:566/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
25% identity, 90% coverage: 15:478/518 of query aligns to 26:510/605 of 7v75A
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
21% identity, 81% coverage: 15:431/518 of query aligns to 83:548/744 of P58743
- F101 (= F33) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ G299) binding
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
21% identity, 81% coverage: 15:431/518 of query aligns to 83:548/744 of Q9JKQ2
- 158:168 (vs. 79:84, 27% identical) Involved in motor function
- S398 (≠ G299) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (≠ Q300) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see 3 papers)
21% identity, 81% coverage: 15:431/518 of query aligns to 83:548/744 of Q9EPH0
- L104 (≠ V36) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (= V74) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D154 (vs. gap) mutation to N: Shifts the voltage-sensitivity to more negative values.
- D155 (vs. gap) mutation to N: Shifts the voltage-sensitivity to more negative values.
- E169 (vs. gap) mutation to Q: No effect.
- K177 (≠ Q86) mutation to Q: No effect.
- R197 (≠ K106) mutation to Q: Shifts the voltage-sensitivity to more negative values.
- A202 (≠ I111) mutation to C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application.
- K233 (= K139) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ P141) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (≠ G142) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.; mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-235.
- K276 (vs. gap) mutation to C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application.
- E277 (vs. gap) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
- R281 (≠ H170) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (≠ L172) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (= K174) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (≠ F232) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (≠ T233) mutation to Q: No effect.
- D342 (≠ Y243) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ T260) mutation to C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application.
- Q389 (≠ G290) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ G299) Controls the electromotile activity; mutation to C: Does not affect anion-dependent electromotility-related charge movement. Strongly attenuates inhibition by oxalate of electromotility-related charge movement. Is sensible to intracellular thiol-reactive reagents. Is completely insensitive to both reagents applied to the extracellular face of the membrane. Strongly affects the interaction with oxalate.
- R399 (≠ Q300) Contributes to anion binding; mutation to C: Largely abolishes anion-dependent electromotility-related charge movement.; mutation to E: Fully abolishes anion-dependent electromotility-related charge movement.; mutation to K: Does not affect anion-dependent electromotility-related charge movement.; mutation to Q: Fully abolishes anion-dependent electromotility-related charge movement.; mutation to S: Does not affect anion-dependent electromotility-related charge movement. Abrogates salicylate inhibition of electromotility-related charge movement.
- G408 (= G309) mutation to C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application.
- K409 (≠ R310) mutation to Q: No effect.
- L431 (≠ F332) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (≠ P365) mutation to C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application.
- D485 (≠ A385) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
Sites not aligning to the query:
- 505:718 Extended region for STAS domain
- 557 K→Q: No effect; when associated with Q-558 and Q-559.
- 558 R→Q: No effect; when associated with Q-557 and Q-559.
- 559 K→Q: No effect; when associated with Q-557 and Q-558.
- 571 R→Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-572 and Q-577.
- 572 R→Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-571 and Q-577.
- 577 K→Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-571 and Q-572.
7lguA Structure of human prestin in the presence of nacl (see paper)
21% identity, 81% coverage: 15:431/518 of query aligns to 71:536/680 of 7lguA
Q62273 Sulfate transporter; Diastrophic dysplasia protein homolog; ST-OB; Solute carrier family 26 member 2 from Mus musculus (Mouse) (see paper)
24% identity, 59% coverage: 15:319/518 of query aligns to 111:461/739 of Q62273
- F368 (= F225) mutation to A: Reduced sulfate-chloride exchange activity.
- E417 (= E275) mutation E->A,K: Loss of sulfate-chloride exchange activity.
D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
20% identity, 81% coverage: 15:431/518 of query aligns to 83:548/741 of D7PC76
- GG 274:275 (vs. gap) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ G299) binding
7xulA Human slc26a3 in complex with tenidap
23% identity, 83% coverage: 14:441/518 of query aligns to 61:528/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (≠ A25), L75 (≠ P28), Q76 (≠ E29), E262 (≠ A184), S367 (≠ G299), L412 (≠ V348), N416 (≠ T352)
- binding cholesterol hemisuccinate: I157 (≠ L97), F162 (≠ A102), P209 (≠ E146), K214 (≠ T151), Y217 (= Y156), V302 (≠ W234), Q306 (= Q238), V309 (≠ L241), V450 (≠ T379)
7xujA Human slc26a3 in complex with uk5099
23% identity, 83% coverage: 14:441/518 of query aligns to 68:537/703 of 7xujA
- binding (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid: V79 (≠ A25), Q83 (≠ E29), E271 (≠ A184), S376 (≠ G299), R377 (≠ Q300), V380 (≠ I303), L421 (≠ V348), A422 (≠ V349), N425 (≠ T352)
- binding cholesterol hemisuccinate: F171 (≠ A102), V311 (≠ W234), Q315 (= Q238)
Q8CIW6 Solute carrier family 26 member 6; Anion exchange transporter; Chloride-formate exchanger; Pendrin-L1; Pendrin-like protein 1; Putative anion transporter-1; Pat-1 from Mus musculus (Mouse) (see paper)
22% identity, 73% coverage: 22:398/518 of query aligns to 102:504/758 of Q8CIW6
Sites not aligning to the query:
- 552 T→A: Does not inhibit formate transport in PMA-induced cells.
Q9BXS9 Solute carrier family 26 member 6; Anion exchange transporter; Pendrin-like protein 1; Pendrin-L1 from Homo sapiens (Human) (see 3 papers)
20% identity, 73% coverage: 22:398/518 of query aligns to 100:503/759 of Q9BXS9
- N167 (≠ F89) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- N172 (vs. gap) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- V206 (≠ F110) to M: in dbSNP:rs13324142
Sites not aligning to the query:
- 547:549 DVD→NVN: Does not inhibit cell membrane localization. Inhibits interaction with CA2 and bicarbonate transport.
- 553 S→A: Does not inhibit interaction with CA2. Inhibits interaction with CA2 and bicarbonate transport in PMA-induced cells.
- 582 S→A: Does not inhibit interaction with CA2. Does not inhibit interaction with CA2 and bicarbonate transport in PMA-induced cells.
P58735 Sulfate anion transporter 1; SAT-1; Solute carrier family 26 member 1 from Mus musculus (Mouse) (see paper)
21% identity, 82% coverage: 15:437/518 of query aligns to 72:561/704 of P58735
- T190 (≠ V92) mutation to M: Decreased sulfate-hydrogencarbonate exchange activity. Loss of localization to plasma membrane.
- S363 (≠ L257) mutation to L: Decreased sulfate-hydrogencarbonate exchange activity. Increased accumulation of protein in ER.
Sites not aligning to the query:
- 56 A→T: Decreased sulfate-hydrogencarbonate exchange activity. Does not affect localization to plasma membrane.
7xuhA Down-regulated in adenoma in complex with tqr1122
23% identity, 83% coverage: 14:441/518 of query aligns to 68:541/707 of 7xuhA
- binding 2-[4,8-dimethyl-2-oxidanylidene-7-[[3-(trifluoromethyl)phenyl]methoxy]chromen-3-yl]ethanoic acid: P124 (vs. gap), I125 (vs. gap), L187 (≠ V114), I192 (≠ M119), F195 (= F122), V335 (≠ E254), S338 (≠ L257), S380 (≠ G299), M433 (vs. gap)
- binding cholesterol hemisuccinate: V223 (≠ L147), F226 (≠ L150), K227 (≠ T151), Y230 (= Y156), F318 (≠ L237), Q319 (= Q238)
Q9URY8 Probable sulfate permease C869.05c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
23% identity, 73% coverage: 15:392/518 of query aligns to 124:527/840 of Q9URY8
Sites not aligning to the query:
- 823 modified: Phosphoserine
A0FKN5 Prestin; Solute carrier family 26 member 5 from Gallus gallus (Chicken) (see paper)
21% identity, 66% coverage: 15:354/518 of query aligns to 84:459/742 of A0FKN5
- S404 (≠ G299) Controls the anion transport; mutation to A: Alters anion selectivity.; mutation to C: Abolishes sulfate transport. Does not affect oxalate transport. Is accesible both from extracellular and intracellular side by methane-thiosulphonate (MTS) reagents. Inhibits divalent transport upon extracellular application of (2-sulphonatoethyl)methane-thiosulphonate (MTSES) but not [2-(trimethylammonium)ethyl]methane-thiosulphonate (MTSET). Abolishes anion transport upon intracellular MTSET application.
- R405 (≠ Q300) mutation to C: Fully abolishes anion transport.
Query Sequence
>6937849 FitnessBrowser__SB2B:6937849
MFELIRHKTASHKADLLSGLTVALALVPEAVAFAFVAGVEPMVGLYAAFIMGLVTAMIGG
RPGMISGATGAMAVVMVALVATHGVQYLFAAVVLAGLLQVAAGIFKLGKFIRIVPYPVMI
GFVNGLAIVIFLAQLGQFKVPGDNGELTWLTGDGLYLMLGLVALTMAIIHFLPKLTTAIP
SSLAAILTVTGLVVFFELDTRTVVDFLKTMSGDDNATIAGTLPTFAIPHVPFTWETLQII
LPYSVILAAVGLIESLLTLTVLDEMTGTRGRGNKECVGQGVGNITSGFFGAMGGCAMIGQ
SMININSGGRGRLSGITAALALLTFILFGAAFIEIIPLAALVGVMFMVVLGTFEWASFKV
MRKVPKHDAFVIVLVTTVTVFTDLAVAVFVGVIVSALVFAWEHAKHISARTVINANGSKV
YQLSGPLFFGSVSHFLELFDAANDPKDVIVDFGQSRVADHSALDAIDTLAERYNTLGKTL
HLVHLSEDCKALLAKAGDLVEVNLLEDPHYRVADDKLD
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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