SitesBLAST

Q86YT5 Na(+)/citrate cotransporter; NaCT; Sodium-coupled citrate transporter; Sodium-dependent citrate transporter; Solute carrier family 13 member 5 from Homo sapiens (Human) (see 5 papers)
31% identity, 32% coverage: 277:410/419 of query aligns to 411:542/568 of Q86YT5

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Q86YT5

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L420 (= L286) to P: loss of localization to plasma membrane; loss of function in citrate transport; dbSNP:rs150738356
S427 (≠ T293) to L: in DEE25; loss of localization to plasma membrane; loss of function in citrate transport; dbSNP:rs548065551
L485 (≠ A353) to R: no effect on localization to plasma membrane; reduced function in citrate transport; increased Km and Vmax values compared with that of wild type with citrate as substrate; dbSNP:rs148049520
L488 (≠ R356) to P: in DEE25; loss of function in citrate transport; loss of localization to plasma membrane; dbSNP:rs587777578
D524 (= D392) to H: in DEE25; loss of function in citrate transport; no effect on localization to plasma membrane; dbSNP:rs863225448

Sites not aligning to the query:

142 T → M: in DEE25; no loss of localization to plasma membrane; loss of function in citrate transport; dbSNP:rs761917087
219 G → E: loss of localization to plasma membrane; loss of function in citrate transport; dbSNP:rs150024888; G → R: in DEE25; loss of function in citrate transport; loss of localization to plasma membrane; dbSNP:rs144332569
227 T → M: in DEE25; loss of function in citrate transport; no effect on localization to plasma membrane; dbSNP:rs587777577
243 D → N: no effect on localization to plasma membrane; no effect on its function in citrate transport; dbSNP:rs142262032
341:568 natural variant: Missing (in DEE25; loss of localization to plasma membrane; loss of function in citrate transport)
409 G→Q: No effect on its function in citrate transport.
410 mutation I->A,F: Significant loss of function in citrate transport.; I→V: No effect on its function in citrate transport.
562 modified: carbohydrate, N-linked (GlcNAc...) asparagine

Q28615 Solute carrier family 13 member 2; Na(+)/dicarboxylate cotransporter 1; NaDC-1; Renal sodium/dicarboxylate cotransporter from Oryctolagus cuniculus (Rabbit) (see paper)
31% identity, 36% coverage: 256:407/419 of query aligns to 409:553/593 of Q28615

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Q28615

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Y432 (≠ L284) mutation to C: Does not affect cell membrane localization. Decreases succinate transport activity. Decreases Km value for succinate. More sensitive to inhibition by lithium.
T474 (= T328) mutation to C: Does not affect cell membrane localization. Abolishes succinate transport activity.
N525 (= N379) mutation to C: Decreases cell membrane expression. Decreases succinate transport activity.
M539 (≠ Y393) mutation to C: Does not affect cell membrane localization. Decreases succinate transport activity. Insensitive to inhibition by lithium.

Sites not aligning to the query:

83 L→C: Decreases cell membrane expression. Decreases succinate transport activity. Decreases Km value for succinate.
86 T→C: Does not affect cell membrane localization. Decreases succinate transport activity.
228 Y→C: Does not affect cell membrane localization. Decreases succinate transport activity.

Q10SY9 Silicon efflux transporter LSI2; Low silicon protein 2 from Oryza sativa subsp. japonica (Rice) (see paper)
25% identity, 37% coverage: 25:181/419 of query aligns to 295:456/472 of Q10SY9

query
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Q10SY9

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Sites not aligning to the query:

115 S→N: In lsi2; impairs silicon uptake. Reduced growth. Grain discoloration. Reduces grain yield 2.5-fold.

Query Sequence

>BWI76_RS04380 FitnessBrowser__Koxy:BWI76_RS04380
MSPVTITLSLLVFSIVMFVWEKIPLAVTAMIVCITLVVTGVFDVQTAFSGFINQNVILFV
AMFVVGGALFETGVTDKIGGIVTRYARSEKQLIVIIMLVCGLLSGVLSNTGTAAVLIPVV
IGAAIKSGYARSRLLMPLAFASALGGNLSLIGSPGNLIAQSALEQVGQSFGFFEYAKLGI
PMLACGILYFVTIGYRILPGKNTLQKHGAESIRTVDCPTYKQVIALSVLIATVLGMIFEK
RIGLPIAIIGSIGALSLVMTRVITEKQAYQAIDSQTIFLFGGTLALAKALETTGAGAIMA
RSIIDLLGHQASPFLLLSAVLIISCILTNFMSNTATAALLMPIGLSIAHSMGADPRAVLM
AIVIGCSCAYATPVGTPANMMIFSAGGYKFVDYVKVGLPLILISVIVSFILLPIFFPFY

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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