SitesBLAST
Comparing CCNA_01242 CCNA_01242 amino acid permease 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)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
44% identity, 96% coverage: 6:515/531 of query aligns to 1:455/456 of 5oqtA
- binding alanine: I38 (= I41), G40 (= G43), T41 (≠ A44), G42 (= G45), F226 (= F260), A227 (= A261), I229 (≠ V263)
- binding : E24 (≠ T27), G26 (= G29), F28 (≠ I31), D29 (≠ N32), M32 (≠ S35), A176 (= A202), R177 (≠ N203), A184 (≠ V210), A188 (≠ I214), L192 (≠ T218), Q294 (≠ L328), V297 (≠ L346)
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
44% identity, 96% coverage: 5:515/531 of query aligns to 2:457/458 of 6f34A
- binding arginine: I40 (= I41), G42 (= G43), T43 (≠ A44), G44 (= G45), E115 (= E116), Y116 (= Y117), A119 (= A120), F228 (= F260), A229 (= A261), I231 (≠ V263), V314 (= V361)
- binding cholesterol: W201 (≠ Q225), Y202 (= Y226)
- binding : G28 (= G29), F30 (≠ I31), D31 (≠ N32), M34 (≠ S35), A178 (= A202), R179 (≠ N203), A186 (≠ V210), I187 (= I211), A190 (≠ I214), L194 (≠ T218), Q296 (≠ L328), V299 (≠ L346)
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)
34% identity, 83% coverage: 8:450/531 of query aligns to 14:438/629 of P30825
- N226 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
25% identity, 83% coverage: 14:453/531 of query aligns to 8:396/461 of P76037
- Y110 (= Y117) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
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)
24% identity, 84% coverage: 9:455/531 of query aligns to 13:410/487 of P82251
- V40 (= V38) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ IIGAG 41:45) binding
- I44 (= I42) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ L49) to F: in CSNU; uncertain significance
- P52 (≠ T50) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (≠ I67) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y96) to H: in CSNU; uncertain significance
- G105 (= G102) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W111) to R: in CSNU; uncertain significance
- I120 (≠ E116) to L: in CSNU; uncertain significance
- T123 (≠ V119) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ L139) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ I141) modified: Interchain (with C-114 in SLC3A1)
- V170 (= V198) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ V210) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (= G223) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ R253) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (≠ G254) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (≠ I257) to D: in CSNU; decreased amino acid transport activity
- W230 (≠ F260) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (≠ V263) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ F265) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ A267) mutation to A: Reduces amino acid transport activity.
- G259 (≠ A289) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ I291) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ P316) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (= C366) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ Q369) to E: in CSNU; uncertain significance
- V330 (≠ T375) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ M376) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (= R378) 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 (≠ G399) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (= S424) mutation to A: Markedly reduces amino acid transport activity.
- A382 (≠ T427) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (≠ A428) mutation to A: Complete loss of amino acid transport activity.
- Y386 (≠ F431) mutation to A: Loss of amino acid transport activity.
- K401 (≠ P446) to E: in CSNU; uncertain significance; dbSNP:rs760264924
Sites not aligning to the query:
- 426 L → P: in CSNU; uncertain significance
- 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.
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)
25% identity, 81% coverage: 24:454/531 of query aligns to 35:421/531 of Q9QXW9
- Y130 (= Y117) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ A120) 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 (= F260) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
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)
24% identity, 85% coverage: 18:471/531 of query aligns to 40:446/507 of Q01650
- Y117 (= Y94) mutation to A: Strongly decreased leucine transport activity.
- C164 (≠ V164) modified: Interchain (with C-210 in SLC3A2)
- D223 (≠ N231) to V: in dbSNP:rs17853937
- N230 (≠ E238) to K: in dbSNP:rs1060250
- A246 (≠ G254) mutation to V: Nearly abolishes leucine transport activity.
- F252 (= F260) mutation to A: Nearly abolishes leucine transport activity.
- W257 (≠ F265) mutation to A: Nearly abolishes leucine transport activity.
- N258 (≠ E266) mutation to A: Decreased leucine transport activity.; mutation to D: Nearly abolishes leucine transport activity.
- Y259 (≠ A267) mutation to A: Strongly decreased leucine transport activity.
- E303 (≠ P316) mutation to K: Decreased leucine transport activity.
- P375 (≠ L398) mutation to L: Nearly abolishes leucine transport activity.
Sites not aligning to the query:
- 483:507 mutation Missing: Nearly abolishes leucine transport activity.
7dsqB Overall structure of the lat1-4f2hc bound with 3,5-diiodo-l-tyrosine (see paper)
25% identity, 84% coverage: 24:471/531 of query aligns to 3:403/464 of 7dsqB
7dsnB Overall structure of the lat1-4f2hc bound with jx-119 (see paper)
25% identity, 84% coverage: 24:471/531 of query aligns to 3:403/464 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 (≠ A40), I20 (= I41), G22 (= G43), S23 (≠ A44), G24 (= G45), I97 (≠ A125), I104 (≠ V132), F209 (= F260), A210 (= A261), G212 (≠ V263), I354 (≠ G420), N361 (≠ T427)
- binding cholesterol hemisuccinate: F109 (≠ H137), Y145 (≠ A188), K148 (≠ S191), V153 (= V204), Q326 (≠ K392)
Sites not aligning to the query:
7dslB Overall structure of the lat1-4f2hc bound with jx-078 (see paper)
25% identity, 84% coverage: 24:471/531 of query aligns to 3:403/464 of 7dslB
7dskB Overall structure of the lat1-4f2hc bound with jx-075 (see paper)
25% identity, 84% coverage: 24:471/531 of query aligns to 3:403/464 of 7dskB
- binding (2~{S})-2-azanyl-7-(naphthalen-1-ylmethoxy)-3,4-dihydro-1~{H}-naphthalene-2-carboxylic acid: T19 (≠ A40), I20 (= I41), S23 (≠ A44), G24 (= G45), I97 (≠ A125), S100 (≠ W128), S101 (= S129), F209 (= F260), G212 (≠ V263), Y216 (≠ A267), V353 (≠ L419), I354 (≠ G420), N361 (≠ T427)
- binding cholesterol hemisuccinate: K148 (≠ S191), A149 (= A192), V153 (= V204), F157 (≠ I208), H324 (= H390)
Sites not aligning to the query:
Q9UHI5 Large neutral amino acids transporter small subunit 2; L-type amino acid transporter 2; hLAT2; Solute carrier family 7 member 8 from Homo sapiens (Human) (see 3 papers)
25% identity, 81% coverage: 24:454/531 of query aligns to 36:422/535 of Q9UHI5
- I53 (= I41) binding
- Y93 (= Y80) mutation to A: Nearly complete reduction of glycine, L-alanine, and L-glutamine uptake. Minimal effect on the transport of L-isoleucine, L-histidine and L-tryptophan.
- N134 (≠ A120) Important for substrate specificity; binding ; mutation to Q: Reduces L-leucine uptake activity. Abolishes L-tryptophan uptake.; mutation to S: The substrate specificity changed dramatically reducing L-glutamine, glycine and L-alanine uptake activity thus mimicking the selectivity of SLC7A5.
- C154 (≠ V164) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ A184) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (= F260) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ V263) Important for substrate specificity; binding ; mutation to S: Strong decrease in the uptake of large substrates L-tryptophan, L-glutamine, and L-histidine but increases the uptake of small neutral amino acids glycine and L-alanine.
- V302 (≠ I319) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity
- N395 (vs. gap) binding ; mutation to Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- Y396 (vs. gap) mutation to A: Strongly reduces L-leucine uptake activity.
- T402 (≠ V434) to M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity
- R418 (= R450) to C: found in a patient with age-related hearing loss; decreases L-alanine transport activity. Decreases L-tyrosine transport activity
Sites not aligning to the query:
- 460 V → E: found in a patient with age-related hearing loss; strongly decreases L-alanine transport activity. Decreases L-tyrosine transport activity. Decreases cell membrane localization
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, 76% coverage: 68:471/531 of query aligns to 85:438/501 of Q9UPY5
- C86 (≠ A69) 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 (≠ G118) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (≠ P159) 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 (≠ N205) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ I211) 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 (= K212) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (≠ F260) binding
- F254 (≠ T270) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ L287) 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 (= C366) 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 (vs. gap) 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 (≠ H445) 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 (= C468) 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.
6irtB Human lat1-4f2hc complex bound with bch (see paper)
25% identity, 83% coverage: 31:471/531 of query aligns to 3:396/457 of 6irtB
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
23% identity, 76% coverage: 68:471/531 of query aligns to 41:394/455 of 7p9uB
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
23% identity, 82% coverage: 18:455/531 of query aligns to 2:387/438 of O34739
- C94 (≠ M109) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ S191) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ T218) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ V361) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
Sites not aligning to the query:
- 415 C→S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
23% identity, 76% coverage: 68:471/531 of query aligns to 41:394/453 of 7epzB
Sites not aligning to the query:
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
24% identity, 81% coverage: 28:455/531 of query aligns to 1:381/458 of 6li9B
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
24% identity, 71% coverage: 18:392/531 of query aligns to 2:328/469 of P46349
- G33 (≠ L49) mutation to D: Lack of activity.
- G42 (= G59) mutation to S: Lack of activity.
- G301 (≠ V361) mutation to V: Lack of activity.
Sites not aligning to the query:
- 338 G→E: Lack of activity.
- 341 F→S: Lack of activity.
- 414 G→R: Lack of activity.
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
25% identity, 71% coverage: 12:389/531 of query aligns to 1:339/489 of P25737
- M1 (≠ I12) modified: Initiator methionine, Removed
- Y102 (≠ L113) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ Y117) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K212) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F260) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E266) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E274) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ A322) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-278.
- D278 (≠ R325) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-275.
Sites not aligning to the query:
- 438 E→A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 443 D→A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 446 D→A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.
Query Sequence
>CCNA_01242 CCNA_01242 amino acid permease
MAGNRLFLKKSIASIQKEAAHSQLKRTLGPINLMSLGVGAIIGAGIFVLTGQVASANAGP
AIMLSFIVAGIACALAGLCYAELASTMPVSGSAYTYAYGTLGEVFAWIMGWLLVLEYGVA
ASTVAVGWSGYVVSTLHALGINFPMIQVAGADAPMWATPLIQAVAAPGGGTMFAMTGTLN
LVAAIGIAMVSALLVVGVSESANVNNAIVVIKVIVLVTFIAVGAQYINPANWHPFIPEPT
GQPGEFGIGGIFRGAAIIFFAYVGFEAVSTAAAEAKNPSRDVPIGILGALIICTLIYMAV
AAVMTGVVPFRELASPAPIAVAIDRMGLEWADIPYAAAEGGKLNLLSFAIKIGAITGLSS
VMLVLCYGQTRIFYTMARDGLLPKVFAEIHPKFRTPWLGTILLGVVIAIAASFLPISLLG
DLVSLGTAVAFSIVCLSVIYLRIKHPDLPRPFKVPGGIFTAAAGIAACLFLPYQNFQPMI
VHAMNDNPLPLMILGGYAAVGAIIYIAYGYWHSKLAKGIDITEETDPNSPA
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