SitesBLAST
Comparing 3608674 FitnessBrowser__Dino:3608674 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, 89% coverage: 30:503/534 of query aligns to 9:466/467 of 5da0A
Sites not aligning to the query:
Q55415 Bicarbonate transporter BicA from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
29% identity, 85% coverage: 32:486/534 of query aligns to 15:502/564 of Q55415
- T69 (= T86) binding ; mutation to A: Alters bicarbonate transport.
- D258 (≠ E262) binding ; mutation D->A,E: Alters bicarbonate transport.
- T262 (= T266) binding ; mutation to A: Alters bicarbonate transport.
- G300 (≠ A304) binding
- A301 (≠ M305) binding
- T302 (≠ I306) binding ; mutation to A: Alters bicarbonate transport.
- A471 (≠ Q455) mutation to N: Alters bicarbonate transport.
- L476 (≠ F460) mutation to S: Alters bicarbonate transport.
- A486 (= A470) mutation to E: Alters bicarbonate transport.
- L490 (≠ I474) mutation to Q: Alters bicarbonate transport.
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
33% identity, 68% coverage: 32:396/534 of query aligns to 14:391/392 of 6ki1B
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
22% identity, 89% coverage: 30:505/534 of query aligns to 27:552/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (≠ F122), R127 (≠ K123), W130 (≠ K126)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (= L124), L131 (≠ F127), E409 (≠ A393), L413 (≠ V397), G417 (≠ I401), A421 (= A406)
- binding sulfate ion: A84 (= A90), S321 (≠ M305), F322 (≠ I306)
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
24% identity, 89% coverage: 32:505/534 of query aligns to 26:566/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
23% identity, 89% coverage: 32:505/534 of query aligns to 26:574/605 of 7v75A
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, 69% coverage: 39:405/534 of query aligns to 100:502/759 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 (≠ F127) 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.
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)
23% identity, 69% coverage: 39:405/534 of query aligns to 102:503/758 of Q8CIW6
Sites not aligning to the query:
- 552 T→A: Does not inhibit formate transport in PMA-induced cells.
7xulA Human slc26a3 in complex with tenidap
22% identity, 76% coverage: 32:439/534 of query aligns to 62:517/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (≠ A42), L75 (≠ P45), Q76 (≠ E46), E262 (≠ A201), S367 (≠ G307), L412 (≠ V352), N416 (≠ V356)
- binding cholesterol hemisuccinate: I157 (= I114), F162 (= F119), P209 (vs. gap), K214 (vs. gap), Y217 (vs. gap), V302 (≠ M242), Q306 (= Q246), V309 (≠ A249), V450 (≠ L389)
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
22% identity, 77% coverage: 32:440/534 of query aligns to 83:549/744 of P58743
- F101 (= F50) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ G307) binding
7lguA Structure of human prestin in the presence of nacl (see paper)
22% identity, 77% coverage: 32:440/534 of query aligns to 71:537/680 of 7lguA
7xujA Human slc26a3 in complex with uk5099
23% identity, 76% coverage: 32:439/534 of query aligns to 69:526/703 of 7xujA
- binding (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid: V79 (≠ A42), Q83 (≠ E46), E271 (≠ A201), S376 (≠ G307), R377 (≠ Q308), V380 (≠ I311), L421 (= L349), A422 (≠ V350), N425 (≠ M353)
- binding cholesterol hemisuccinate: F171 (= F119), V311 (≠ M242), Q315 (= Q246)
7xuhA Down-regulated in adenoma in complex with tqr1122
22% identity, 76% coverage: 32:439/534 of query aligns to 69:530/707 of 7xuhA
- binding 2-[4,8-dimethyl-2-oxidanylidene-7-[[3-(trifluoromethyl)phenyl]methoxy]chromen-3-yl]ethanoic acid: P124 (≠ G87), I125 (≠ A88), L187 (≠ V131), I192 (≠ M136), F195 (= F139), V335 (vs. gap), S338 (vs. gap), S380 (≠ G307), M433 (≠ T360)
- binding cholesterol hemisuccinate: V223 (vs. gap), F226 (vs. gap), K227 (vs. gap), Y230 (vs. gap), F318 (≠ L245), Q319 (= Q246)
Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see 3 papers)
22% identity, 77% coverage: 32:440/534 of query aligns to 83:549/744 of Q9EPH0
- L104 (≠ V53) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (= V91) 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 (= E103) mutation to Q: No effect.
- K177 (vs. gap) mutation to Q: No effect.
- R197 (≠ K123) mutation to Q: Shifts the voltage-sensitivity to more negative values.
- A202 (≠ I128) 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 (= K156) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ P158) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (≠ N159) 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 (≠ K191) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (≠ T193) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (≠ V195) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (≠ M242) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (≠ E243) mutation to Q: No effect.
- D342 (≠ Y251) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ G271) 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 (≠ G298) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ G307) 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 (≠ Q308) 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 (= G317) 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 (≠ R318) mutation to Q: No effect.
- L431 (= L340) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (≠ P373) 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 (≠ A393) 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.
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
22% identity, 77% coverage: 32:440/534 of query aligns to 83:549/744 of Q9JKQ2
- 158:168 (vs. 95:102, 18% identical) Involved in motor function
- S398 (≠ G307) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (≠ Q308) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
P58735 Sulfate anion transporter 1; SAT-1; Solute carrier family 26 member 1 from Mus musculus (Mouse) (see paper)
23% identity, 78% coverage: 32:445/534 of query aligns to 72:561/704 of P58735
- T190 (≠ V109) mutation to M: Decreased sulfate-hydrogencarbonate exchange activity. Loss of localization to plasma membrane.
- S363 (≠ L265) 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.
P40879 Chloride anion exchanger; Down-regulated in adenoma; Protein DRA; Solute carrier family 26 member 3 from Homo sapiens (Human) (see 3 papers)
22% identity, 76% coverage: 32:439/534 of query aligns to 76:548/764 of P40879
- N153 (≠ A90) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N161 (≠ A98) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N165 (≠ V102) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- C307 (≠ I215) 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.
8sieC Pendrin in complex with bicarbonate
24% identity, 78% coverage: 32:450/534 of query aligns to 47:518/613 of 8sieC
- binding Lauryl Maltose Neopentyl Glycol: G198 (= G162), S296 (≠ M242), T300 (≠ Q246), F303 (≠ A249)
- binding bicarbonate ion: Y65 (≠ F50), F101 (≠ G87), L356 (≠ I306), S357 (≠ G307), V403 (≠ M353), N406 (≠ V356)
- binding cholesterol: L226 (≠ G177), V255 (= V206), I262 (= I211), Y272 (vs. gap), F411 (= F361), V414 (≠ S365), V414 (≠ S365), C415 (≠ L366), C415 (≠ L366), I436 (≠ V385), M452 (vs. gap), F453 (vs. gap)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: W421 (vs. gap), V429 (≠ L378), V432 (= V381), F433 (≠ L382), I436 (≠ V385)
8shcC Pendrin in complex with niflumic acid
24% identity, 78% coverage: 32:450/534 of query aligns to 47:518/613 of 8shcC
- binding cholesterol: I199 (vs. gap), A223 (≠ I174), V255 (= V206), Y272 (vs. gap), M412 (≠ A362), C415 (≠ L366), M452 (vs. gap), F453 (vs. gap)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: Q156 (≠ K123), W421 (vs. gap), V432 (= V381), F433 (≠ L382), F455 (vs. gap)
- binding 2-{[3-(trifluoromethyl)phenyl]amino}nicotinic acid: Y65 (≠ F50), F101 (≠ G87), T173 (≠ V140), E252 (≠ I203), I312 (= I258), L356 (≠ I306), S357 (≠ G307), V402 (= V352), N406 (≠ V356)
8sgwC Pendrin in complex with chloride
24% identity, 78% coverage: 32:450/534 of query aligns to 47:518/613 of 8sgwC
- binding Lauryl Maltose Neopentyl Glycol: G198 (= G162), S296 (≠ M242), T300 (≠ Q246), F303 (≠ A249)
- binding cholesterol: I228 (≠ V179), V255 (= V206), I262 (= I211), Y272 (vs. gap), K408 (≠ I358), F411 (= F361), M412 (≠ A362), M412 (≠ A362), V414 (≠ S365), C415 (≠ L366), V417 (≠ I368), I439 (≠ V388)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: F159 (≠ K126), Y163 (≠ L130), F284 (≠ L230), P286 (≠ S232), I289 (= I235), F343 (≠ V293), F346 (= F296), W421 (vs. gap), F433 (≠ L382), I436 (≠ V385), F455 (vs. gap), F464 (≠ A406), P465 (≠ Y407)
Query Sequence
>3608674 FitnessBrowser__Dino:3608674
MPRALLASFANRIAFSAPTADETLSISRIRIELLSGLTVALALVPEAVAFAFVAGVHPLV
GLYAAFIVGLITALIGGRPGMISGATGALAVVMVALVAEHGVEYLFATVVLMGILQILFG
IFKLGKFIRLVPHPVMLGFVNGLAIVIFLAQLTQFKVPNDAGEMVWMTGWPLVIMLGLVA
LTMAIIWGMPKITRVIPAPLAGIGIVAVLVIAFGIDVPRVGDLASIAGGLPSLHIPMVPL
NMETLQIIAPYAFILAAIGLIESLLTLNLVGEITGKRGGASQECIAQGVANTVTGFFGGM
GGCAMIGQSMINVKSGGRTRIAGVAAALFLLLFIVAASPLIEQIPLAALVGVMFMVVIGT
FAWQSLTILRRVPLTDALVIVLVTVVTVLTDLAIAVVVGVIVSALAYAWNNASRIHAKTY
TTPEGAKVYQVQGPLFFGSSAGFVELFDVTHDPGQVIVDFADSRVVDQSALTAIEAMAAK
YADAGKNLQLRHLSRDCHQLLTKAGQLMIDSDDDPDYAIAADYQVKTGILGGGH
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