SitesBLAST
Comparing CA265_RS17395 FitnessBrowser__Pedo557:CA265_RS17395 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)
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
46% identity, 98% coverage: 2:475/483 of query aligns to 6:458/458 of 6f34A
- binding arginine: I40 (≠ T37), G42 (= G39), T43 (≠ A40), G44 (= G41), E115 (= E112), Y116 (= Y113), A119 (≠ G116), F228 (= F244), A229 (≠ V245), I231 (= I247), V314 (= V331)
- binding cholesterol: W201 (≠ Q209), Y202 (= Y210)
- binding : G28 (= G25), F30 (≠ I27), D31 (≠ N28), M34 (≠ L31), A178 (= A186), R179 (≠ I187), A186 (≠ F194), I187 (≠ L195), A190 (≠ G198), L194 (≠ V202), Q296 (≠ Y313), V299 (≠ L316)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
46% identity, 98% coverage: 2:475/483 of query aligns to 4:456/456 of 5oqtA
- binding alanine: I38 (≠ T37), G40 (= G39), T41 (≠ A40), G42 (= G41), F226 (= F244), A227 (≠ V245), I229 (= I247)
- binding : E24 (≠ T23), G26 (= G25), F28 (≠ I27), D29 (≠ N28), M32 (≠ L31), A176 (= A186), R177 (≠ I187), A184 (≠ F194), A188 (≠ G198), L192 (≠ V202), Q294 (≠ Y313), V297 (≠ L316)
P30825 High affinity cationic amino acid transporter 1; CAT-1; CAT1; Ecotropic retroviral leukemia receptor homolog; Ecotropic retrovirus receptor homolog; Solute carrier family 7 member 1; System Y+ basic amino acid transporter from Homo sapiens (Human) (see paper)
33% identity, 83% coverage: 17:417/483 of query aligns to 25:435/629 of P30825
- N226 (= N215) modified: carbohydrate, N-linked (GlcNAc...) asparagine
Q7YQK4 Large neutral amino acids transporter small subunit 1; 4F2 light chain; 4F2 LC; 4F2LC; L-type amino acid transporter 1; LAT1; Solute carrier family 7 member 5 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
26% identity, 97% coverage: 2:470/483 of query aligns to 23:477/503 of Q7YQK4
- C88 (= C69) mutation to S: No significant effect on inhibition by HgCl(2). Decreased KM and Vmax for Phe. Similar affect on KM and Vmax for Phe; when associated with S-183.
- C98 (= C75) mutation to S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe. Slightly less decreased KM and Vmax for Phe; when associated with S-183.
- C160 (≠ L145) mutation to S: No change to KM or Vmax for Phe.
- C172 (≠ A168) mutation to S: No change to KM or Vmax for Phe.
- C174 (≠ V170) mutation to S: No change to KM or Vmax for Phe.
- C183 (≠ I179) mutation to S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe. Similar affect on KM and Vmax for Phe; when associated with S-88. Slightly less decreased KM and Vmax for Phe; when associated with S-98.
- G219 (≠ N215) mutation to D: Decreased KM and Vmax for Trp. Increased KM and Vmax for Phe; when associated with L-234.
- W234 (≠ G228) mutation to L: Decreased KM and Vmax for Trp. Increased KM but decreased Vmax for Phe. Increased KM and Vmax for Phe; when associated with D-219.
- C331 (≠ S330) mutation to S: No significant effect on inhibition by HgCl(2). Increased KM and Vmax for Phe.
- C377 (= C374) mutation to S: No significant effect on inhibition by HgCl(2).
- C403 (≠ A400) mutation to S: No significant effect on inhibition by HgCl(2).
- C439 (= C438) mutation to S: Prevents insertion into the plasma membrane and possibly protein folding.
- C454 (≠ L453) mutation to S: No significant effect on inhibition by HgCl(2). Slightly increased KM but slightly decreased Vmax for Phe.
Sites not aligning to the query:
- 492 C→S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe.
Q01650 Large neutral amino acids transporter small subunit 1; 4F2 light chain; 4F2 LC; 4F2LC; CD98 light chain; Integral membrane protein E16; E16; L-type amino acid transporter 1; hLAT1; Solute carrier family 7 member 5; y+ system cationic amino acid transporter from Homo sapiens (Human) (see 3 papers)
27% identity, 95% coverage: 10:470/483 of query aligns to 36:481/507 of Q01650
- Y117 (= Y90) mutation to A: Strongly decreased leucine transport activity.
- C164 (≠ L143) modified: Interchain (with C-210 in SLC3A2)
- D223 (= D212) to V: in dbSNP:rs17853937
- N230 (≠ Q229) to K: in dbSNP:rs1060250
- A246 (vs. gap) mutation to V: Nearly abolishes leucine transport activity.
- F252 (= F244) mutation to A: Nearly abolishes leucine transport activity.
- W257 (≠ F249) mutation to A: Nearly abolishes leucine transport activity.
- N258 (≠ D250) mutation to A: Decreased leucine transport activity.; mutation to D: Nearly abolishes leucine transport activity.
- Y259 (≠ A251) mutation to A: Strongly decreased leucine transport activity.
- E303 (≠ S300) mutation to K: Decreased leucine transport activity.
- P375 (≠ K368) mutation to L: Nearly abolishes leucine transport activity.
Sites not aligning to the query:
- 483:507 mutation Missing: Nearly abolishes leucine transport activity.
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
24% identity, 96% coverage: 4:467/483 of query aligns to 2:440/461 of P76037
- Y110 (= Y113) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
7dsqB Overall structure of the lat1-4f2hc bound with 3,5-diiodo-l-tyrosine (see paper)
26% identity, 94% coverage: 19:470/483 of query aligns to 2:438/464 of 7dsqB
7dsnB Overall structure of the lat1-4f2hc bound with jx-119 (see paper)
26% identity, 94% coverage: 19:470/483 of query aligns to 2:438/464 of 7dsnB
- binding (2~{S})-2-azanyl-7-[[2-(1,3-benzoxazol-2-yl)phenyl]methoxy]-3,4-dihydro-1~{H}-naphthalene-2-carboxylic acid: T19 (≠ L36), I20 (≠ T37), G22 (= G39), S23 (≠ A40), G24 (= G41), I97 (≠ E112), I104 (≠ T119), F209 (= F244), A210 (≠ V245), G212 (≠ I247), I354 (≠ G390), N361 (≠ T397)
- binding cholesterol hemisuccinate: F109 (≠ W124), Y145 (≠ R180), K148 (= K183), V153 (= V188), Q326 (≠ K362)
Sites not aligning to the query:
7dslB Overall structure of the lat1-4f2hc bound with jx-078 (see paper)
26% identity, 94% coverage: 19:470/483 of query aligns to 2:438/464 of 7dslB
7dskB Overall structure of the lat1-4f2hc bound with jx-075 (see paper)
26% identity, 94% coverage: 19:470/483 of query aligns to 2:438/464 of 7dskB
- binding (2~{S})-2-azanyl-7-(naphthalen-1-ylmethoxy)-3,4-dihydro-1~{H}-naphthalene-2-carboxylic acid: T19 (≠ L36), I20 (≠ T37), S23 (≠ A40), G24 (= G41), I97 (≠ E112), S100 (≠ V115), S101 (≠ G116), F209 (= F244), G212 (≠ I247), Y216 (≠ A251), V353 (= V389), I354 (≠ G390), N361 (≠ T397)
- binding cholesterol hemisuccinate: K148 (= K183), A149 (≠ G184), V153 (= V188), F157 (≠ I192), H324 (= H360)
Sites not aligning to the query:
6irtB Human lat1-4f2hc complex bound with bch (see paper)
26% identity, 92% coverage: 27:470/483 of query aligns to 3:431/457 of 6irtB
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
24% identity, 90% coverage: 34:470/483 of query aligns to 14:430/433 of 6f2wA
P82251 b(0,+)-type amino acid transporter 1; b(0,+)AT1; Glycoprotein-associated amino acid transporter b0,+AT1; Solute carrier family 7 member 9 from Homo sapiens (Human) (see 11 papers)
23% identity, 95% coverage: 11:467/483 of query aligns to 17:454/487 of P82251
- V40 (= V34) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ TLGAG 37:41) binding
- I44 (≠ L38) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (vs. gap) to F: in CSNU; uncertain significance
- P52 (≠ S44) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (vs. gap) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y92) to H: in CSNU; uncertain significance
- G105 (= G98) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W107) to R: in CSNU; uncertain significance
- I120 (≠ E112) to L: in CSNU; uncertain significance
- T123 (≠ V115) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ I137) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ Y138) modified: Interchain (with C-114 in SLC3A1)
- V170 (≠ T182) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ F194) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (= G207) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ R237) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (≠ G238) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (≠ L241) to D: in CSNU; decreased amino acid transport activity
- W230 (≠ F244) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (≠ I247) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ F249) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ A251) mutation to A: Reduces amino acid transport activity.
- G259 (≠ S273) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ L275) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (= S300) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ L336) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ Q339) to E: in CSNU; uncertain significance
- V330 (≠ S345) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ I346) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (≠ K348) to Q: in CSNU; decreased amino acid transport activity; dbSNP:rs769576205; to W: in CSNU; severe loss of amino acid transport activity; dbSNP:rs121908484
- A354 (≠ S369) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (= S394) mutation to A: Markedly reduces amino acid transport activity.
- A382 (≠ T397) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (≠ L398) mutation to A: Complete loss of amino acid transport activity.
- Y386 (≠ F401) mutation to A: Loss of amino acid transport activity.
- K401 (≠ P416) to E: in CSNU; uncertain significance; dbSNP:rs760264924
- L426 (≠ F444) to P: in CSNU; uncertain significance
Sites not aligning to the query:
- 482 P → L: in CSNU; severe loss of amino acid transport activity; no effect on localization to the apical membrane; dbSNP:rs146815072; mutation P->A,G,S,V: No effect on amino acid transport activity.; mutation P->F,I,M,W: Decreased amino acid transport activity.
Q9UPY5 Cystine/glutamate transporter; Amino acid transport system xc-; Calcium channel blocker resistance protein CCBR1; Solute carrier family 7 member 11; xCT from Homo sapiens (Human) (see 4 papers)
24% identity, 77% coverage: 69:442/483 of query aligns to 86:439/501 of Q9UPY5
- C86 (= C69) mutation to S: Does not affect L-cystine transport activity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- R135 (≠ Y113) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (≠ L135) modified: Interchain (with C-210 in SLC3A2); mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- Q191 (≠ N189) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ L195) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435.
- K198 (= K196) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (≠ L236) binding
- F254 (= F246) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ I271) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- C327 (≠ Y328) mutation to A: Does not affect L-glutamate transport activity. Does not affect location at cell membrane Does not affect expression level.; mutation to L: Loss of L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.; mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Loss of inhibitio nof L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid. Decrease L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.; mutation to T: Does not affect L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.
- F336 (≠ M337) mutation to A: Decreases L-cystine transport activity about 50%. Increases sensitivity to erastin-induced ferroptosis. Significantly decreases the L-cystine transport activity.; mutation to Y: Does not affect L-cystine transport activity.
- R396 (vs. gap) mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.; mutation to N: Loss of L-cystine transport activity.
- C414 (≠ N415) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- C435 (= C438) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
25% identity, 77% coverage: 69:442/483 of query aligns to 42:395/453 of 7epzB
Sites not aligning to the query:
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
25% identity, 77% coverage: 69:442/483 of query aligns to 42:395/455 of 7p9uB
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
23% identity, 92% coverage: 24:467/483 of query aligns to 1:425/458 of 6li9B
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
22% identity, 95% coverage: 14:473/483 of query aligns to 2:436/438 of O34739
- C94 (≠ I105) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ T175) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ V202) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ V331) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
- C415 (≠ L453) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
Q9QXW9 Large neutral amino acids transporter small subunit 2; L-type amino acid transporter 2; mLAT2; Solute carrier family 7 member 8 from Mus musculus (Mouse) (see paper)
23% identity, 96% coverage: 4:465/483 of query aligns to 18:463/531 of Q9QXW9
- Y130 (= Y113) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ G116) mutation to S: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake. Increases the export of both L-leucine and L-phenylalanine.
- F242 (= F244) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
22% identity, 91% coverage: 3:442/483 of query aligns to 2:421/458 of P24207
- R26 (≠ I27) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P56) mutation to A: 50% of wild-type phenylalanine transport activity.; mutation to G: No change in phenylalanine transport activity.; mutation to L: 26% of wild-type phenylalanine transport activity.
- F87 (≠ A89) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y92) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (= Y94) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ T96) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ M97) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ L100) mutation to L: No effect on phenylalanine transport activity.
- F101 (≠ W103) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W107) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (≠ L109) mutation to L: No effect on phenylalanine transport activity.
- W108 (vs. gap) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ E112) mutation to L: 60% of wild-type phenylalanine transport activity.; mutation to Y: Enables the transport of tryptophan to almost the same steady-state level as that of phenylalanine.
- E118 (≠ T119) mutation E->G,L,V,N: Loss of activity.
- K168 (≠ V171) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (≠ D250) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (≠ T278) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P366) mutation to A: 5% of wild-type phenylalanine transport activity.; mutation P->G,Q,K,R: Loss of activity.; mutation to S: 3% of wild-type phenylalanine transport activity.; mutation to T: 17% of wild-type phenylalanine transport activity.
Sites not aligning to the query:
- 442 P→A: 46% of wild-type phenylalanine transport activity.; P→G: 52% of wild-type phenylalanine transport activity.; P→L: 43% of wild-type phenylalanine transport activity.
Query Sequence
>CA265_RS17395 FitnessBrowser__Pedo557:CA265_RS17395
MKKSIASIVAEANESGEGSLKRTLGPINLILIGVGLTLGAGLFSITGLAAANHSGPAVTL
SFVIAALGCGFAALCYAEFASMIPVAGSAYTYSYATMGELFAWIIGWDLVLEYSVGCATV
AISWSQYLTKFLASLHIYLPPQLTLSPFETAKLADGSTVNGIINIPAALVVVLMTAILIR
GTKGSAIVNGIIVFLKVGVVLVFIALGWQYIDPANYHPYIPENTGTFGQFGWSGVLRGAG
LVFFVFIGFDAVAASAQETKNPARDLPIGIIGSLLVCTVLFGLFGHVMTGLANYKEFANS
GAPVAIAIEKTPYAWLSQAIILAILIGYTSVILIDLMAQSRMFYSISKDGLLPKMFSDVH
AKFKTPYKSNIILCVFIGLFAAFVPMNVVGEMTSIGTLLAFLMVCVGILILRKTNPEAKR
PFKVPFVPLIPILGILTCIAMMVFLPWETWLRLAVWLIIGLAIYFWYGKKNSKLKAQEEQ
TKL
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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