SitesBLAST
Comparing 5209114 FitnessBrowser__PV4:5209114 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, 94% coverage: 6:495/519 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: 13:495/519 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)
36% identity, 72% coverage: 13:388/519 of query aligns to 12:391/392 of 6ki1B
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
26% identity, 93% coverage: 14:497/519 of query aligns to 25:566/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
26% identity, 93% coverage: 14:497/519 of query aligns to 25:574/605 of 7v75A
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
24% identity, 96% coverage: 2:497/519 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 (= A78), S321 (≠ M297), F322 (≠ I298)
Q9BXS9 Solute carrier family 26 member 6; Anion exchange transporter; Pendrin-like protein 1; Pendrin-L1 from Homo sapiens (Human) (see 3 papers)
23% identity, 80% coverage: 22:435/519 of query aligns to 100:556/759 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 (≠ F110) to M: in dbSNP:rs13324142
- ATV 547:549 (≠ GPL 425:427) mutation to NVN: Does not inhibit cell membrane localization. Inhibits interaction with CA2 and bicarbonate transport.
- N553 (≠ S431) 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.
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
21% identity, 83% coverage: 15:443/519 of query aligns to 83:560/744 of Q9JKQ2
- 158:168 (vs. 78:84, 9% 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.
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
21% identity, 83% coverage: 15:443/519 of query aligns to 83:560/744 of P58743
- F101 (= F33) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ G299) binding
7lguA Structure of human prestin in the presence of nacl (see paper)
21% identity, 83% coverage: 15:443/519 of query aligns to 71:548/680 of 7lguA
Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see 3 papers)
21% identity, 83% coverage: 15:443/519 of query aligns to 83:560/744 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 (≠ D142) 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 (≠ L234) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (≠ E235) mutation to Q: No effect.
- D342 (≠ F245) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ D263) 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 (= L332) 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.
- K557 (≠ H440) mutation to Q: No effect; when associated with Q-558 and Q-559.
- R558 (≠ A441) mutation to Q: No effect; when associated with Q-557 and Q-559.
- K559 (= K442) 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.
7xulA Human slc26a3 in complex with tenidap
21% identity, 81% coverage: 14:435/519 of query aligns to 61:521/690 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 (≠ V344), N416 (≠ V348)
- binding cholesterol hemisuccinate: I157 (≠ L97), F162 (≠ C102), P209 (vs. gap), K214 (vs. gap), Y217 (vs. gap), V302 (≠ L234), Q306 (≠ S238), V309 (≠ L241), V450 (≠ F381)
D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
21% identity, 83% coverage: 15:443/519 of query aligns to 83:560/741 of D7PC76
- GG 274:275 (vs. gap) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ G299) binding
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, 81% coverage: 22:442/519 of query aligns to 102:565/758 of Q8CIW6
- F552 (= F429) mutation to A: Does not inhibit formate transport in PMA-induced cells.
7xujA Human slc26a3 in complex with uk5099
22% identity, 81% coverage: 14:435/519 of query aligns to 68:530/703 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 (≠ V344), A422 (≠ M345), N425 (≠ V348)
- binding cholesterol hemisuccinate: F171 (≠ C102), V311 (≠ L234), Q315 (≠ S238)
7xuhA Down-regulated in adenoma in complex with tqr1122
21% identity, 81% coverage: 14:435/519 of query aligns to 68:534/707 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 (≠ T352)
- binding cholesterol hemisuccinate: V223 (vs. gap), F226 (vs. gap), K227 (vs. gap), Y230 (vs. gap), F318 (≠ L237), Q319 (≠ S238)
Q62273 Sulfate transporter; Diastrophic dysplasia protein homolog; ST-OB; Solute carrier family 26 member 2 from Mus musculus (Mouse) (see paper)
21% identity, 82% coverage: 15:442/519 of query aligns to 111:602/739 of Q62273
- F368 (= F225) mutation to A: Reduced sulfate-chloride exchange activity.
- E417 (= E275) mutation E->A,K: Loss of sulfate-chloride exchange activity.
8sieC Pendrin in complex with bicarbonate
23% identity, 81% coverage: 14:432/519 of query aligns to 46:508/613 of 8sieC
- binding Lauryl Maltose Neopentyl Glycol: G198 (= G145), S296 (= S238), T300 (≠ P242), F303 (= F245)
- binding bicarbonate ion: Y65 (≠ F33), F101 (≠ G70), L356 (≠ I298), S357 (≠ G299), V403 (≠ M345), N406 (≠ V348)
- binding cholesterol: L226 (= L164), V255 (= V193), I262 (≠ L204), Y272 (≠ E214), F411 (= F353), V414 (≠ W355), V414 (≠ W355), C415 (≠ A356), C415 (≠ A356), I436 (≠ V377), M452 (vs. gap), F453 (vs. gap)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: W421 (≠ R362), V429 (≠ F370), V432 (= V373), F433 (≠ L374), I436 (≠ V377)
8shcC Pendrin in complex with niflumic acid
23% identity, 81% coverage: 14:432/519 of query aligns to 46:508/613 of 8shcC
- binding cholesterol: I199 (≠ V146), A223 (≠ L159), V255 (= V193), Y272 (≠ E214), M412 (vs. gap), C415 (≠ A356), M452 (vs. gap), F453 (vs. gap)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: Q156 (≠ K106), W421 (≠ R362), V432 (= V373), F433 (≠ L374), F455 (= F389)
- binding 2-{[3-(trifluoromethyl)phenyl]amino}nicotinic acid: Y65 (≠ F33), F101 (≠ G70), T173 (≠ V123), E252 (≠ T190), I312 (≠ E254), L356 (≠ I298), S357 (≠ G299), V402 (= V344), N406 (≠ V348)
8sgwC Pendrin in complex with chloride
23% identity, 81% coverage: 14:432/519 of query aligns to 46:508/613 of 8sgwC
- binding Lauryl Maltose Neopentyl Glycol: G198 (= G145), S296 (= S238), T300 (≠ P242), F303 (= F245)
- binding cholesterol: I228 (≠ M166), V255 (= V193), I262 (≠ L204), Y272 (≠ E214), K408 (≠ L350), F411 (= F353), M412 (vs. gap), M412 (vs. gap), V414 (≠ W355), C415 (≠ A356), V417 (≠ F358), I439 (≠ V380)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: F159 (≠ K109), Y163 (≠ I113), F284 (= F225), P286 (≠ I227), I289 (≠ V230), F343 (≠ T285), F346 (= F288), W421 (≠ R362), F433 (≠ L374), I436 (≠ V377), F455 (= F389), F464 (≠ V398), P465 (≠ F399)
Query Sequence
>5209114 FitnessBrowser__PV4:5209114
MFDLIRHKTSSHRADLLSGLTVALALVPEAVAFAFVAGVEPMVGLYAAFIMGLVTALIGG
RPGMISGATGAMAVVMVALVSEHGVQYLFAAVVLAGLIQVTCGLFKLGKFIRIVPYPVMI
GFVNGLAIVIFLAQLGQFKVPDANGVLTWLPQDQLILMLGLVALTMAIIHFLPKLTTAFP
SSLAAILTVTAIVVYFELDTRNVLDFLKSMSGDEHATIAGNLPSFAIPSVPFNLETLSII
LPYSFILAAVGLIESLLTLTVIDEMTSTRGKGNKECVGQGIGNITSGFFGAMGGCAMIGQ
SMININSGGRGRLSGITAAIALLTFILFGSALIEMIPLAALVGVMFMVVLGTFEWASFKV
MRKVPKHDAFVIVLVTVVTVFTDLAFAVFVGVIVSALVFAWEHAKHINVDVSEDANGWKV
YKLNGPLFFGSVAEFLELFHAKTDPQDVIVDFQNSRVCDHSALEAIDTLAERYVSAGKRL
HLRHLSHDCKKLLHKAGDLVEVNLIEDPHYKVADDKLDS
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