SitesBLAST
Comparing CA265_RS24540 FitnessBrowser__Pedo557:CA265_RS24540 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)
40% identity, 93% coverage: 15:490/511 of query aligns to 7:466/467 of 5da0A
Sites not aligning to the query:
Q55415 Bicarbonate transporter BicA from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
27% identity, 93% coverage: 15:490/511 of query aligns to 11:519/564 of Q55415
- T69 (≠ A73) binding ; mutation to A: Alters bicarbonate transport.
- D258 (≠ E248) binding ; mutation D->A,E: Alters bicarbonate transport.
- T262 (= T252) binding ; mutation to A: Alters bicarbonate transport.
- G300 (≠ P290) binding
- A301 (≠ M291) binding
- T302 (≠ I292) binding ; mutation to A: Alters bicarbonate transport.
- A471 (≠ H442) mutation to N: Alters bicarbonate transport.
- L476 (≠ F447) mutation to S: Alters bicarbonate transport.
- A486 (≠ G457) mutation to E: Alters bicarbonate transport.
- L490 (= L461) mutation to Q: Alters bicarbonate transport.
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
31% identity, 70% coverage: 15:374/511 of query aligns to 10:383/392 of 6ki1B
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
22% identity, 94% coverage: 4:483/511 of query aligns to 16:543/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (≠ F109), R127 (≠ K110), W130 (≠ K113)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (= L111), L131 (≠ F114), E409 (≠ A380), L413 (= L384), G417 (≠ I388), A421 (= A391)
- binding sulfate ion: A84 (≠ V79), S321 (≠ M291), F322 (≠ I292)
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
24% identity, 93% coverage: 4:477/511 of query aligns to 7:551/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
25% identity, 92% coverage: 4:473/511 of query aligns to 7:510/605 of 7v75A
7xulA Human slc26a3 in complex with tenidap
24% identity, 95% coverage: 18:501/511 of query aligns to 61:579/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (≠ T29), L75 (≠ P32), Q76 (≠ E33), E262 (≠ V187), S367 (≠ A293), L412 (≠ V330), N416 (≠ A334)
- binding cholesterol hemisuccinate: I157 (≠ L101), F162 (≠ V106), P209 (≠ W152), K214 (≠ T156), Y217 (= Y159), V302 (= V224), Q306 (≠ L228), V309 (≠ L231), V450 (≠ W375)
7xujA Human slc26a3 in complex with uk5099
24% identity, 95% coverage: 18:501/511 of query aligns to 68:592/703 of 7xujA
- binding (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid: V79 (≠ T29), Q83 (≠ E33), E271 (≠ V187), S376 (≠ A293), R377 (≠ Q294), V380 (= V297), L421 (≠ V330), A422 (≠ P331), N425 (≠ A334)
- binding cholesterol hemisuccinate: F171 (≠ V106), V311 (= V224), Q315 (≠ L228)
7xuhA Down-regulated in adenoma in complex with tqr1122
23% identity, 95% coverage: 18:501/511 of query aligns to 68:596/707 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 (≠ V118), I192 (≠ M123), F195 (= F126), V335 (= V244), S338 (≠ T247), S380 (≠ A293), M433 (≠ V338)
- binding cholesterol hemisuccinate: V223 (≠ L153), F226 (≠ G155), K227 (≠ T156), Y230 (= Y159), F318 (≠ N227), Q319 (≠ L228)
P40879 Chloride anion exchanger; Down-regulated in adenoma; Protein DRA; Solute carrier family 26 member 3 from Homo sapiens (Human) (see 3 papers)
24% identity, 95% coverage: 18:501/511 of query aligns to 75:614/764 of P40879
- N153 (≠ G74) 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 (≠ I201) 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
22% identity, 96% coverage: 1:491/511 of query aligns to 25:587/613 of 8sieC
- binding Lauryl Maltose Neopentyl Glycol: G198 (= G155), S296 (≠ L228), T300 (≠ K232), F303 (= F235)
- binding bicarbonate ion: Y65 (≠ F37), F101 (≠ P66), L356 (≠ I292), S357 (≠ A293), V403 (≠ P331), N406 (≠ A334)
- binding cholesterol: L226 (= L167), V255 (= V192), I262 (≠ F199), Y272 (vs. gap), F411 (≠ M339), V414 (= V342), V414 (= V342), C415 (≠ A343), C415 (≠ A343), I436 (≠ L368), M452 (≠ L384), F453 (≠ I385)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: W421 (= W349), V429 (≠ Q361), V432 (≠ I364), F433 (≠ I365), I436 (≠ L368)
8shcC Pendrin in complex with niflumic acid
22% identity, 96% coverage: 1:491/511 of query aligns to 25:587/613 of 8shcC
- binding cholesterol: I199 (vs. gap), A223 (vs. gap), V255 (= V192), Y272 (vs. gap), M412 (= M340), C415 (≠ A343), M452 (≠ L384), F453 (≠ I385)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: Q156 (≠ K110), W421 (= W349), V432 (≠ I364), F433 (≠ I365), F455 (vs. gap)
- binding 2-{[3-(trifluoromethyl)phenyl]amino}nicotinic acid: Y65 (≠ F37), F101 (≠ P66), T173 (≠ V127), E252 (≠ I189), I312 (≠ V244), L356 (≠ I292), S357 (≠ A293), V402 (= V330), N406 (≠ A334)
8sgwC Pendrin in complex with chloride
22% identity, 96% coverage: 1:491/511 of query aligns to 25:587/613 of 8sgwC
- binding Lauryl Maltose Neopentyl Glycol: G198 (= G155), S296 (≠ L228), T300 (≠ K232), F303 (= F235)
- binding cholesterol: I228 (≠ V169), V255 (= V192), I262 (≠ F199), Y272 (vs. gap), K408 (≠ V336), F411 (≠ M339), M412 (= M340), M412 (= M340), V414 (= V342), C415 (≠ A343), V417 (≠ G345), I439 (≠ V371)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: F159 (≠ K113), Y163 (≠ L117), F284 (= F216), P286 (= P218), I289 (= I221), F343 (≠ A279), F346 (= F282), W421 (= W349), F433 (≠ I365), I436 (≠ L368), F455 (vs. gap), F464 (≠ V393), P465 (≠ F394)
A0FKN5 Prestin; Solute carrier family 26 member 5 from Gallus gallus (Chicken) (see paper)
22% identity, 65% coverage: 19:351/511 of query aligns to 84:462/742 of A0FKN5
- S404 (≠ A293) 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 (≠ Q294) mutation to C: Fully abolishes anion transport.
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, 72% coverage: 26:393/511 of query aligns to 100:503/759 of Q9BXS9
- N167 (vs. gap) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- N172 (≠ K85) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- V206 (≠ F114) 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)
22% identity, 72% coverage: 26:393/511 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.
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
23% identity, 65% coverage: 19:351/511 of query aligns to 83:456/744 of P58743
- F101 (= F37) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ A293) binding
7lguA Structure of human prestin in the presence of nacl (see paper)
23% identity, 65% coverage: 19:351/511 of query aligns to 71:444/680 of 7lguA
Sites not aligning to the query:
D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
22% identity, 65% coverage: 19:351/511 of query aligns to 83:456/741 of D7PC76
- GG 274:275 (vs. gap) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ A293) binding
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
22% identity, 65% coverage: 19:351/511 of query aligns to 83:456/744 of Q9JKQ2
- 158:168 (vs. 82:89, 18% identical) Involved in motor function
- S398 (≠ A293) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (≠ Q294) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
Query Sequence
>CA265_RS24540 FitnessBrowser__Pedo557:CA265_RS24540
MKPYLQLFDFSKKVNYKTEILAGLTVAMTMIPESLSFAILAGFPPLTGLYAAFIMGLVTA
ILGGRPGLVSGGAGATVIVLIALMKTQGIEYVFAAVALAGLIQIMVGLFKLGKFVRLVPQ
PVMFGFVNGLAVIIFMSQLEQFKTLVDGRITWLSGTPLYVMLALVLLTVAIVIILPKITK
AVPASLVAIIVVFLIVLCFGIDTKLVKNIASVNGGFPPFHIPKVPLNLDMLKIIFPYSLI
MAGVGLTEGLLTLNLVDEITASKGNRNRESIAQGIANIANGFFTGMGGCPMIAQTLVNLS
AGARARLSGIIAALTILLIILVGAPVIDRVPMAALVGVMMMVAIGTFEWMSFKVINKMPA
QDIIIGILVAVITVWLHNLALAVLIGVILSALVFAWESSKRIRASKHTDASGVKTYEIFG
PLFFGSIANFNELFDVAHDPQHIVIDFKHSRVFDMSGIDALNKLTERYRSLDKKLQLKHL
SNDCKRLLKNADQIIEVNIIEDPIYQVATER
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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