SitesBLAST
Comparing WP_090446088.1 NCBI__GCF_900100495.1:WP_090446088.1 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)
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
30% identity, 96% coverage: 8:509/522 of query aligns to 6:564/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
29% identity, 96% coverage: 8:509/522 of query aligns to 6:572/605 of 7v75A
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
28% identity, 99% coverage: 7:522/522 of query aligns to 8:568/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (= L124), R127 (= R125), W130 (≠ A128)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (≠ F126), L131 (= L129), E409 (≠ Q402), L413 (≠ Y406), G417 (≠ L410), A421 (≠ F414)
- binding sulfate ion: A84 (= A82), S321 (= S314), F322 (= F315)
Q9BXS9 Solute carrier family 26 member 6; Anion exchange transporter; Pendrin-like protein 1; Pendrin-L1 from Homo sapiens (Human) (see 3 papers)
30% identity, 87% coverage: 10:462/522 of query aligns to 75:569/759 of Q9BXS9
- N167 (vs. gap) 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 (≠ L129) to M: in dbSNP:rs13324142
- ATV 547:549 (≠ GSI 440:442) mutation to NVN: Does not inhibit cell membrane localization. Inhibits interaction with CA2 and bicarbonate transport.
- N553 (≠ A446) mutation to A: Does not inhibit interaction with CA2. Inhibits interaction with CA2 and bicarbonate transport in PMA-induced cells.
Sites not aligning to the query:
- 582 S→A: Does not inhibit interaction with CA2. Does not inhibit interaction with CA2 and bicarbonate transport in PMA-induced cells.
8sieC Pendrin in complex with bicarbonate (see paper)
25% identity, 99% coverage: 7:522/522 of query aligns to 26:592/613 of 8sieC
- binding Lauryl Maltose Neopentyl Glycol: G198 (≠ T167), S296 (= S253), T300 (≠ P259), F303 (≠ V262)
- binding bicarbonate ion: Y65 (= Y45), F101 (≠ T81), L356 (≠ F315), S357 (≠ T316), V403 (≠ P354), N406 (≠ S357)
- binding cholesterol: L226 (≠ F192), V255 (≠ L212), I262 (≠ L219), Y272 (≠ G229), F411 (≠ I362), V414 (≠ I365), V414 (≠ I365), C415 (= C366), C415 (= C366), I436 (≠ L394), M452 (≠ L410), F453 (≠ A411)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: W421 (≠ F379), V429 (≠ L387), V432 (≠ A390), F433 (≠ L391), I436 (≠ L394)
8shcC Pendrin in complex with niflumic acid (see paper)
25% identity, 99% coverage: 7:522/522 of query aligns to 26:592/613 of 8shcC
- binding cholesterol: I199 (≠ A168), A223 (≠ L189), V255 (≠ L212), Y272 (≠ G229), M412 (≠ L363), C415 (= C366), M452 (≠ L410), F453 (≠ A411)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: Q156 (≠ R125), W421 (≠ F379), V432 (≠ A390), F433 (≠ L391), F455 (≠ L413)
- binding 2-{[3-(trifluoromethyl)phenyl]amino}nicotinic acid: Y65 (= Y45), F101 (≠ T81), T173 (= T142), E252 (vs. gap), I312 (≠ T271), L356 (≠ F315), S357 (≠ T316), V402 (≠ I353), N406 (≠ S357)
8sh3C Pendrin in complex with iodide (see paper)
25% identity, 99% coverage: 7:522/522 of query aligns to 26:592/613 of 8sh3C
- binding Lauryl Maltose Neopentyl Glycol: S114 (≠ P94), G198 (≠ T167), E297 (= E256), T300 (≠ P259), F303 (≠ V262)
- binding cholesterol: I199 (≠ A168), A223 (≠ L189), V255 (≠ L212), I258 (= I215), I262 (≠ L219), Y272 (≠ G229), F411 (≠ I362), V414 (≠ I365), C415 (= C366), V417 (≠ I372), I439 (≠ L397), M452 (≠ L410), F453 (≠ A411)
- binding iodide ion: Y65 (= Y45), N406 (≠ S357)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L155 (= L124), F159 (≠ A128), W421 (≠ F379), V429 (≠ L387), V432 (≠ A390), F433 (≠ L391), I436 (≠ L394), L451 (≠ V409), F455 (≠ L413), F464 (≠ Q422), P465 (= P423)
8sgwC Pendrin in complex with chloride (see paper)
25% identity, 99% coverage: 7:522/522 of query aligns to 26:592/613 of 8sgwC
- binding Lauryl Maltose Neopentyl Glycol: G198 (≠ T167), S296 (= S253), T300 (≠ P259), F303 (≠ V262)
- binding chloride ion: Y65 (= Y45), N406 (≠ S357)
- binding cholesterol: I228 (≠ L194), V255 (≠ L212), I262 (≠ L219), Y272 (≠ G229), K408 (≠ A359), F411 (≠ I362), M412 (≠ L363), M412 (≠ L363), V414 (≠ I365), C415 (= C366), V417 (≠ I372), I439 (≠ L397)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: F159 (≠ A128), Y163 (≠ F132), F284 (≠ R240), P286 (= P242), I289 (≠ S245), F343 (≠ V302), F346 (≠ W305), W421 (≠ F379), F433 (≠ L391), I436 (≠ L394), F455 (≠ L413), F464 (≠ Q422), P465 (= P423)
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)
31% identity, 80% coverage: 10:427/522 of query aligns to 77:516/758 of Q8CIW6
Sites not aligning to the query:
- 552 T→A: Does not inhibit formate transport in PMA-induced cells.
Q9URY8 Probable sulfate permease C869.05c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 80% coverage: 7:424/522 of query aligns to 104:542/840 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)
26% identity, 80% coverage: 8:427/522 of query aligns to 64:516/742 of A0FKN5
- S404 (≠ T316) 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 (= R317) mutation to C: Fully abolishes anion transport.
7lguA Structure of human prestin in the presence of nacl (see paper)
24% identity, 90% coverage: 9:478/522 of query aligns to 52:570/680 of 7lguA
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
24% identity, 87% coverage: 9:461/522 of query aligns to 64:563/744 of P58743
- F101 (≠ Y45) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ T316) binding salicylate
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
24% identity, 87% coverage: 9:461/522 of query aligns to 64:563/744 of Q9JKQ2
- 158:168 (vs. 97:103, 18% identical) Involved in motor function
- S398 (≠ T316) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (= R317) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
24% identity, 87% coverage: 9:461/522 of query aligns to 64:563/741 of D7PC76
- GG 274:275 (vs. gap) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ T316) binding salicylate
Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see 3 papers)
23% identity, 87% coverage: 9:461/522 of query aligns to 64:563/744 of Q9EPH0
- L104 (≠ I48) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (vs. gap) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D154 (≠ S93) mutation to N: Shifts the voltage-sensitivity to more negative values.
- D155 (≠ P94) mutation to N: Shifts the voltage-sensitivity to more negative values.
- E169 (vs. gap) mutation to Q: No effect.
- K177 (≠ A105) mutation to Q: No effect.
- R197 (= R125) mutation to Q: Shifts the voltage-sensitivity to more negative values.
- A202 (≠ V130) 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 (≠ H161) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ P163) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (≠ S164) 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 (= R202) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (≠ W204) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (≠ R206) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (= P246) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (= D250) mutation to Q: No effect.
- D342 (≠ A260) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ R277) 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 (≠ A307) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ T316) 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 (= R317) 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 (≠ A326) 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 (≠ R327) mutation to Q: No effect.
- L431 (= L349) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (= S382) 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 (≠ Q402) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- K557 (≠ Q455) mutation to Q: No effect; when associated with Q-558 and Q-559.
- R558 (= R456) mutation to Q: No effect; when associated with Q-557 and Q-559.
- K559 (≠ S457) mutation to Q: No effect; when associated with Q-557 and Q-558.
Sites not aligning to the query:
- 505:718 Extended region for STAS domain
- 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.
7xujA Human slc26a3 in complex with uk5099
27% identity, 80% coverage: 8:424/522 of query aligns to 49:485/703 of 7xujA
- binding (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid: V79 (≠ L37), Q83 (= Q41), E271 (vs. gap), S376 (≠ T316), R377 (= R317), V380 (≠ L320), L421 (≠ G361), A422 (≠ I362), N425 (≠ I365)
- binding cholesterol hemisuccinate: F171 (≠ L121), V311 (≠ L251), Q315 (≠ L255)
7xulA Human slc26a3 in complex with tenidap
28% identity, 80% coverage: 8:424/522 of query aligns to 42:476/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (≠ L37), L75 (≠ P40), Q76 (= Q41), E262 (vs. gap), S367 (≠ T316), L412 (≠ G361), N416 (≠ I365)
- binding cholesterol hemisuccinate: I157 (≠ L116), F162 (≠ L121), P209 (≠ A168), K214 (vs. gap), Y217 (≠ L173), V302 (≠ L251), Q306 (≠ L255), V309 (≠ L258), V450 (≠ L398)
7xuhA Down-regulated in adenoma in complex with tqr1122
27% identity, 80% coverage: 8:424/522 of query aligns to 49:489/707 of 7xuhA
- binding 2-[4,8-dimethyl-2-oxidanylidene-7-[[3-(trifluoromethyl)phenyl]methoxy]chromen-3-yl]ethanoic acid: P124 (≠ A82), I125 (≠ A83), L187 (≠ V133), I192 (≠ V138), F195 (= F141), V335 (≠ T271), S338 (= S274), S380 (≠ T316), M433 (vs. gap)
- binding cholesterol hemisuccinate: V223 (≠ L169), F226 (vs. gap), K227 (vs. gap), Y230 (≠ L173), F318 (≠ V254), Q319 (≠ L255)
P40879 Chloride anion exchanger; Down-regulated in adenoma; Protein DRA; Solute carrier family 26 member 3 from Homo sapiens (Human) (see 3 papers)
27% identity, 80% coverage: 8:424/522 of query aligns to 56:507/764 of P40879
- N153 (≠ I104) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N161 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N165 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- C307 (≠ A223) to W: in dbSNP:rs34407351
Sites not aligning to the query:
- 761:764 PDZ-binding; mutation Missing: Loss of interaction with NHERF4. No effect on localization to cell membrane or its exchanger activity.
Query Sequence
>WP_090446088.1 NCBI__GCF_900100495.1:WP_090446088.1
MPLPSRQTLLPFLSWLPTTSRRSLANDLLVGLSGAILALPQSIAYALIAGLPAEYGLYAA
IVPVIIASLWGSSWHLICGPTAAISIVLFTSVSPLATPGSADFIALVLLLSFLAGLFQWL
LGLLRFGALVNFVSHSVVLGFTLGAALVIALGQLPNLLGIHMPSQATALATLLDIGQHLG
QADWRALALALFTLAVSLLVRRFWPRLPALLLGLIAGSLAVLAWPAQLGGIALVSAFDGR
LPPFSPLRLDLASVLELLPAAVACGMLGLVTSLSIARALASKSQQFLDANQEVRAQGLSN
LVGPWFAASLSAGSFTRSALNLQAGARSPLAGVFSALLVALFALLGAGLLAHIPLPSMAA
GILLICWGLVDIPGVRALFRVSRSEFLVMALTLLATLLLELQTAIYAGVLASLFFYLKRT
SQPRVKVWQEGEEELLRVEGSIFFGACHYLQQLLQRSRGARVVIDAHHVNFIDYAGVEML
HQEARRLLAQNRSLTLRRARPQVIEEIHKLEGAEHCPLRFED
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