SitesBLAST
Comparing WP_012406249.1 NCBI__GCF_000020045.1:WP_012406249.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 6 hits to proteins with known functional sites (download)
P07117 Sodium/proline symporter; Proline carrier; Proline permease; Propionate transporter from Escherichia coli (strain K12) (see 4 papers)
23% identity, 80% coverage: 34:480/557 of query aligns to 3:442/502 of P07117
- R257 (= R287) mutation to C: Sodium-independent binding affinity for proline.
- C281 (≠ M316) mutation to S: Does not affect proline uptake activity. Confers resistance to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
- C344 (≠ G380) mutation to S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
- C349 (≠ G385) mutation to S: Does not affect proline uptake activity. Sensitive to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
- R376 (≠ S416) mutation R->E,Q: No change in activity.; mutation to K: Loss of activity.
Q9NY91 Probable glucose sensor protein SLC5A4; Solute carrier family 5 member 4 from Homo sapiens (Human) (see paper)
21% identity, 89% coverage: 20:517/557 of query aligns to 8:535/659 of Q9NY91
- E457 (≠ F443) mutation to Q: Confers sugar transport activity not found in the wild-type protein. Increased sensitivity to inhibitor phlorizin.
P11170 Sodium/glucose cotransporter 1; Na(+)/glucose cotransporter 1; High affinity sodium-glucose cotransporter; Solute carrier family 5 member 1 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
21% identity, 68% coverage: 132:510/557 of query aligns to 124:522/662 of P11170
- C255 (≠ L260) modified: Disulfide link with 608
- Q457 (≠ F443) mutation to W: Drasticly decreased affinity for glucose and phlorizin.
- T460 (≠ A446) mutation to W: Decreased affinity for glucose and phlorizin.
Sites not aligning to the query:
- 608 modified: Disulfide link with 255
P13866 Sodium/glucose cotransporter 1; Na(+)/glucose cotransporter 1; High affinity sodium-glucose cotransporter; Solute carrier family 5 member 1 from Homo sapiens (Human) (see 6 papers)
22% identity, 78% coverage: 35:468/557 of query aligns to 25:485/664 of P13866
- N51 (= N61) to S: in GGM; slightly decreased activity; dbSNP:rs17683011
- W67 (≠ G75) mutation to A: Strong reduction in D-glucose transporter activity.
- S77 (≠ D85) mutation to A: Loss of activity.
- H83 (≠ A91) mutation to L: Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with A-287 and C-290.; mutation to Q: Loss of D-glucose transporter activity.
- R135 (= R143) to W: in GGM; loss of activity
- S159 (≠ V167) to P: in GGM; loss of activity; dbSNP:rs933026071
- A166 (≠ Q174) to T: in GGM; about 90% reduction in activity
- D204 (≠ Q211) mutation to A: Loss of activity.
- N248 (≠ G253) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to Q: Loss of N-glycosylation.
- C255 (≠ L260) modified: Disulfide link with 511
- W276 (vs. gap) to L: in GGM; about 95% reduction in activity
- T287 (≠ M286) mutation to A: Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with L-83 and C-290.; mutation to N: Loss of D-glucose transporter activity. Has strict selectivity for D-galactose.; mutation T->S,A: Has normal D-glucose and D-galactose transporter activity.
- Y290 (≠ F289) mutation to C: Loss of D-galactose transporter activity. Has strict selectivity for D-glucose. Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with A-287 and L-83.
- W291 (≠ T290) mutation to A: Loss of D-glucose transporter activity.
- C292 (≠ V291) to Y: in GGM; loss of activity; dbSNP:rs765502638; mutation to A: Has no effect on water permeability.
- Q295 (vs. gap) to R: in GGM; loss of activity; dbSNP:rs779428134
- R300 (vs. gap) to S: in GGM; loss of activity
- A304 (= A297) to V: in GGM; impairs trafficking to the plasma membrane
- K321 (vs. gap) mutation to Q: Acquires D-mannose and D-allose transporter activity comparable to glucose and galactose.
- C345 (≠ I325) modified: Disulfide link with 351
- C351 (≠ G335) modified: Disulfide link with 345
- C355 (≠ G339) modified: Disulfide link with 361
- C361 (≠ G345) modified: Disulfide link with 355
- N363 (= N347) mutation to A: Loss of water permeation.
- L369 (= L353) to S: in GGM; loss of activity
- R379 (≠ L363) to Q: in GGM; loss of activity; dbSNP:rs747215838
- A388 (= A372) to V: in GGM; loss of activity
- S396 (≠ G380) mutation to A: Loss of activity.
- F405 (≠ I389) to S: in GGM; loss of activity
- A411 (= A395) to T: in GGM; slightly decreased activity; dbSNP:rs17683430
- G426 (≠ S412) to R: in GGM; loss of activity; dbSNP:rs1304151494
- Q451 (≠ F437) mutation to A: Strong reduction in water permeation.
- L452 (= L438) mutation to A: Loss of water permeation.
- D454 (≠ A440) mutation to A: Has no effect on water permeation.
- Q457 (≠ F443) mutation to A: Loss of D-glucose transporter activity.; mutation to C: Strong reduction in D-glucose transporter activity.
- T460 (≠ A446) mutation to A: Loss of D-glucose transporter activity.
- V470 (vs. gap) to N: in GGM; about 90% reduction in activity; requires 2 nucleotide substitutions
Sites not aligning to the query:
- 191:664 natural variant: Missing (in GGM; loss of activity)
- 379:664 natural variant: Missing (in GGM; loss of activity)
- 499 R → H: in GGM; impairs trafficking to the plasma membrane; decreases the sugar affinity; dbSNP:rs927157864
- 511 modified: Disulfide link with 255
- 517 modified: Disulfide link with 522
- 522 modified: Disulfide link with 517
- 615 H → Q: in GGM; slightly decreased activity; dbSNP:rs33954001
- 641 W→A: Slightly reduced D-glucose transporter activity.
- 660:661 HA→WG: Loss of D-glucose transporter activity.
7wmvA Structure of human sglt1-map17 complex bound with lx2761 (see paper)
22% identity, 78% coverage: 35:468/557 of query aligns to 8:468/602 of 7wmvA
- binding N-[2-(dimethylamino)ethyl]-2-methyl-2-[4-[4-[[2-methyl-5-[(2S,3R,4R,5S,6R)-6-methylsulfanyl-3,4,5-tris(oxidanyl)oxan-2-yl]phenyl]methyl]phenyl]butanoylamino]propanamide: N61 (≠ Y86), H66 (≠ A91), L70 (= L95), I81 (≠ F101), F84 (≠ Y104), L257 (vs. gap), M266 (≠ T278), L269 (= L285), T270 (≠ M286), Y273 (≠ F289), W274 (≠ T290), F436 (≠ V439), D437 (≠ A440), Q440 (≠ F443)
Sites not aligning to the query:
Q92911 Sodium/iodide cotransporter; Na(+)/I(-) cotransporter; Natrium iodide transporter; Sodium-iodide symporter; Na(+)/I(-) symporter; Solute carrier family 5 member 5 from Homo sapiens (Human) (see 3 papers)
21% identity, 32% coverage: 41:221/557 of query aligns to 19:201/643 of Q92911
- A102 (≠ M121) natural variant: A -> P
Sites not aligning to the query:
- 226 mutation H->A,D,E,K: Significant loss of iodide transport activity but no effect on its localization to the cell membrane.
- 237 D→A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization.
- 242 Required for homodimerization; Y→A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471. Loss of iodide transport activity; when associated with F-535.
- 243 Required for homodimerization; T→A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471.
- 471 Required for homodimerization; Q→A: No effect on localization to the cell membrane, iodide transport activity and homodimerization. Significant loss of homodimerization; when associated with A-242 or A243.
- 525 A→F: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Loss of iodide transport activity; when associated with A-242.
- 536 T → Q: requires 2 nucleotide substitutions
- 556 S → Q: requires 2 nucleotide substitutions
Query Sequence
>WP_012406249.1 NCBI__GCF_000020045.1:WP_012406249.1
MKRIVTLIGFALASCIARAATAAETFGKVQKQPLNTTAIAMFLAFVVATLGITYWSASKT
NSMKDFYNAGGGISGFQNGLALAGDYMSAAALLGLTSMIFFNGYDGMLYAVSFFVAWPLL
MFLFAERIRNLGQVTIADIASFRLDQQRIRTLMAFGSLTVVCFYLVVQMVGAGQLIQLLF
GLQYNYAVVVVGVLMAVYVTFGGMVATTWVQIVKAVLMLFGASLLALLALSQFGFSLNDM
FAQAIATHKSGAGIMLPSKLVADPFAMLSLSVGLVFGTSGLPHILMRFFTVPDAKAARKS
VFVATGFIGYFFLVVMVLGTAAIVIVGRNPTFFEGGVAGGKLIGGGNMPVMHLAKAMGGD
LVLGFLSAVAFATILAVVAGLTMAGTSAISHDLYAMVLKRNQADHAKEKRVSRIASVAIA
GVAIVLGILFKDQNVAFLVALTFSVAASVNFPILTLSIYWKGLTTRGALMGGIAGLVSAV
GLVVLSPAVWVRVLGHVTAIFPYDYPAIISMSIAFFFTWIGSITDRSARAASERDQFDHQ
FVRAQTGIGASPAATHS
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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