SitesBLAST

Q8BN82 Sialin; H(+)/nitrate cotransporter; H(+)/sialic acid cotransporter; AST; Solute carrier family 17 member 5; Vesicular excitatory amino acid transporter; VEAT from Mus musculus (Mouse) (see paper)
26% identity, 60% coverage: 58:314/425 of query aligns to 115:386/495 of Q8BN82

query
sites
Q8BN82

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H183 (≠ L124) mutation to R: Abolishes sialic acid transporter activity. Does not affect L-aspartate and L-glutamate transporter activity.

Sites not aligning to the query:

39 R→C: Completely abolishes L-aspartate and L-glutamate transporter activity. Retains appreciable H(+)-coupled sialic acid transporter activity.

8u3gA Structure of naag-bound sialin (see paper)
25% identity, 60% coverage: 58:314/425 of query aligns to 54:325/427 of 8u3gA

query
sites
8u3gA

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binding aspartic acid: F118 (≠ M120)

Sites not aligning to the query:

8u3hA Structure of fmoc-leu-oh bound sialin (see paper)
25% identity, 60% coverage: 58:314/425 of query aligns to 52:323/425 of 8u3hA

query
sites
8u3hA

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binding leucine: M279 (= M284)
binding Fluorenylmethyloxycarbonyl chloride: H235 (≠ Y240), Y238 (≠ W243), Y243 (= Y248)

Sites not aligning to the query:

Q9NRA2 Sialin; H(+)/nitrate cotransporter; H(+)/sialic acid cotransporter; AST; Membrane glycoprotein HP59; Solute carrier family 17 member 5; Vesicular excitatory amino acid transporter; VEAT from Homo sapiens (Human) (see 8 papers)
25% identity, 60% coverage: 58:314/425 of query aligns to 115:386/495 of Q9NRA2

query
sites
Q9NRA2

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K136 (= K79) to E: in SD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; completely devoid of L-aspartate and L-glutamate transporter activity, but retains appreciable H(+)-coupled sialic acid transporter activity; dbSNP:rs80338795
H183 (≠ L124) to R: in ISSD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; abolishes H(+)-coupled sialic acid transporter activity; has normal L-aspartate and L-glutamate transporter activity; dbSNP:rs119491109
LL 198:199 (≠ AN 139:140) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
IL 266:267 (≠ LK 207:208) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
SSLR-N 268:272 (≠ AALDLE 209:214) natural variant: Missing (in ISSD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; abolishes H(+)-coupled sialic acid transporter activity; has normal L-aspartate and L-glutamate transporter activity)
G328 (= G270) to E: in ISSD; some patients may manifest a milder phenotype consistent with Salla disease; markedly decreases H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity; dbSNP:rs386833996
P334 (= P276) to R: in ISSD; does not affect intracellular localization, targeted to lysosomes; abolishes H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity; dbSNP:rs119491110
G371 (vs. gap) to V: in ISSD; abolishes H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity; dbSNP:rs777862172

Sites not aligning to the query:

22:23 Dileucine internalization motif; LL→AA: Targeted to plasma membrane.; LL→GG: Targeted to plasma membrane; sialic acid uptake strongly activated at acidic pH.
39 R → C: in SD; frequent variant in Finland; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; completely devoid of L-aspartate and L-glutamate transport activity, but retains appreciable H(+)-coupled sialic acid and nitrate transporter activity; dbSNP:rs80338794

Q5Q0U0 Sialin; H(+)/nitrate cotransporter; H(+)/sialic acid cotransporter; AST; Solute carrier family 17 (Anion/sugar transporter), member 5; Vesicular excitatory amino acid transporter; VEAT from Rattus norvegicus (Rat) (see 2 papers)
26% identity, 60% coverage: 58:314/425 of query aligns to 115:386/495 of Q5Q0U0

query
sites
Q5Q0U0

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G

E
|
E

A
x
G

A

V

V

T

M
x
F

P
|
P

A

A

M

M

L
x
H

I

A

Y

M

I
x
W

S

S

N

S

W

W

F

A

T

P

K

P

N

L

E

E

R

R

S

S

R

K

A

L

N

L

T

T

F

I

L

S

I

Y

L

A

G

G

N

A

P

Q

V

L

T

G

V

T

L

V

W

I

M

S

S

L

V

P

L

L

S

S

G

G

Y

I

L

I

V

C

N

Y

S

Y

F

M

G

N

W

W

R

T

H

Y

M

V

M

F

I

Y

A

L

E

F

G

G

V

L

P

V

A

G

I

I

V

V

W

W

A

F

C

I

I

L

W

W

W

M

F

W

V

I

V

V

Q

S

D

D

K

T

P

P

A

E

E

T

S

H

T

K

W

T

L

I

Q

S

P

H

Q

Y

E

E

K

K

A

E

D

Y

L

I

K

V

A
x
S

L
|
L

D
x
K

L

-

E
x
N

Q

Q

V

L

G

S

M

S

K

Q

P

K

M

V

R

V

N

P

Y

W

A

V

E

S

A

I

F

L

K

K

S

S

P

L

A

P

V

L

I

W

K

A

L

I

C

V

A

V

Q

A

Y

H

F

F

C

S

W

Y

S

N

I

W

G

T

V

F

Y

Y

G

T

F

L

V

L

L

T

W

L

L

L

P

P

S

T

I

Y

L

M

K

K

N

E

A

I

A

L

N

R

I

F

S

N

M

V

V

Q

E

E

T

N

G

G

W

F

L

L

S

S

S

A

L

L

P
|
P

Y

Y

L

F

V

G

A

C

V

W

I

L

A

C

M

M

L

I

L

V

T

C

S

G

W

Q

A

A

S

A

D

D

K

Y

M

L

Q

R

-

V

-

K

-

W

-

N

-

F

-

S

-

T

-

I

-

S

N

V

R

R

K

R

L

I

F

F

-

S

-

L

-

I

-
x
G

-

M

V

V

W

G

P

P

A

A

L

V

L

F

I

L

G

V

A

A

L

A

A

G

F

F

L

I

G

G

K136 (= K79) mutation to E: Markedly decreases H(+)-coupled sialic acid transporter activity.
R168 (= R109) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
E171 (≠ L112) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
G172 (= G113) mutation to C: Decreases protein levels and alters subcellular localization.
E175 (= E116) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
G176 (≠ A117) mutation to C: Decreases protein levels and alters subcellular localization.
F179 (≠ M120) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
P180 (= P121) mutation to C: Decreases protein levels and alters subcellular localization.
H183 (≠ L124) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
W186 (≠ I127) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
SSLK-N 268:272 (≠ AALDLE 209:214) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
P334 (= P276) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
G371 (vs. gap) mutation to V: Remains in the endoplasmic reticulum.

Sites not aligning to the query:

22:23 Dileucine internalization motif; LL→AA: Targeted to plasma membrane; sialic acid uptake strongly activated at acidic pH.
39 R→C: Markedly decreases H(+)-coupled sialic acid transporter activity.

Q9JI12 Vesicular glutamate transporter 2; VGluT2; Differentiation-associated BNPI; Differentiation-associated Na(+)-dependent inorganic phosphate cotransporter; Solute carrier family 17 member 6 from Rattus norvegicus (Rat) (see 2 papers)
23% identity, 83% coverage: 50:401/425 of query aligns to 123:486/582 of Q9JI12

query
sites
Q9JI12

T

T

S

V

S

G

L

M

I

I

G
x
H

A

G

L

S

F

F

I

W

G

G

Y

Y

F

I

F

T

Q

Q

I

I

P

P

G

G

A

G

I

Y

Y

I

A

A

E

S

R

R

R

L

S

A

V

A

K

N

K

R

M

V

I

F

F

G

W

A

S

A

L

I

V

L

L

L

W

T

G

S

S

T

C

L

A

N

A

M

L

L

T

I

G

P

V

S

I

A

S

A

N

R

I

V

P

H

M

Y

L

G

M

C

V

V

I

I

-

F

-

V

R
|
R

F

I

S

L

L

Q

G

G

V

L

V

V

E
|
E

A

G

A

V

V

T

M

Y

P

P

A

A

M

C

L

H

I

G

Y

I

I

W

S

S

N

K

W

W

F

A

T

P

K

P

N

L

E

E

R

R

S

S

R

R

A

L

N

A

T

T

F

T

L

S

I

F

L

C

G

G

N

S

P

Y

V

A

T

G

V

A

L

V

W

I

M

A

S

M

V

P

L

L

S

A

G

G

Y

I

L

L

V

V

N

Q

S

Y

F

T

G

G

W

W

R

S

H

S

M

V

M

F

I

Y

A

V

E

Y

G

G

V

S

P

F

A

G

I

M

V

V

W

W

A

Y

C

M

I

F

W

W

W

L

F

L

V

V

V

S

Q

Y

D

E

K

S

P

P

A

A

E

K

S

H

T

P

W

T

L

I

Q

T

P

D

Q

E

E

E

K

R

A

R

D

Y

L

I

K

E

A

E

A

S

L

I

D

G

L

E

E

S

Q

A

V

N

G

L

M

L

K

G

P

A

M

M

R

E

N

K

Y

F

A

K

-

T

-

P

-

W

-

R

E

K

A

F

F

F

K

T

S

S

P

M

A

P

V

V

I

Y

K

A

L

I

C

I

A

V

Q

A

Y

N

F

F

C

C

W
x
R

S

S

I

W

G

T

V

F

Y

Y

G

L

F

L

V

L

L

I

W

S

L

Q

P

P

S

A

I

Y

L

F

K

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N

E

A

V

A

F

N

G

I

F

S

E

M

I

V

S

E

K

T

V

G

G

W

M

L

L

S

S

S

A

L

V

P

P

Y

H

L

L

V

V

A

M

V

T

I

I

A

I

M

V

L

P

L

I

T

G

S

G

W

Q

A

I

S

A

D

D

K

F

M

L

Q

R

N

S

R

K

K

Q

L

I

F

L

-

S

-

T

V

V

W

R

P

K

A

I

L

M

L

N

I

C

G

G

A

G

L

F

A

G

F

M

L

E

G

A

S

T

Y

L

L

L

-

V

-

G

G

Y

S

S

S

H

N

T

F

R

W

G

L

V

S

A

Y

I

S

S

L

F

L

L

V

V

I

L

A

A

-

V

G

G

A

F

A

S

M

G

Y

F

A

A

P

I

Y

S

G

G

P

-

F

-

F

F

A

N

I

V

I

N

P

H

E

L

L

D

L

I

P

A

K

P

N

R

V

Y

A

A

G

S

G

I

A

L

M

M

A

G

L

I

I

S

N

N

S

G

M

V

G

G

A

T

L

L

G

S

S

G

F

M

L

V

G

C

S

P

Y

I

V

I

V

V

G

G

Y

A

L

M

N

T

G

K

A

N

T

K

G

S

S

R

P

E

S

E

A

W

S

Q

Y

Y

L

V

F

F

M

L

A

I

S

A

G

A

L

L

L

V

H128 (≠ G55) mutation to A: Greatly lowers L-glutamate transport.
R184 (= R109) mutation R->A,E,K: Greatly lowers L-glutamate transport.
E191 (= E116) mutation to A: Greatly lowers L-glutamate transport.; mutation E->D,Q: Lowers L-glutamate transport.
R322 (≠ W243) mutation to A: Loss of L-glutamate release. Abolishes the chloride ion conductance.

Sites not aligning to the query:

88 R→A: Impairs synaptic transmission. Abolishes the chloride ion conductance.

7t3nA R184q/e191q mutant of rat vesicular glutamate transporter 2 (vglut2)
22% identity, 83% coverage: 50:401/425 of query aligns to 65:428/452 of 7t3nA

query
sites
7t3nA

T

T

S

V

S

G

L

M

I

I

G

H

A

G

L

S

F

F

I

W

G

G

Y
|
Y

F

I

F

T

Q

Q

I

I

P

P

G

G

A

G

I

Y

Y

I

A

A

E

S

R

R

R

L

S

A

V

A

K

N

K

R

M

V

I

F

F

G

W

A

S

A

L

I

V

L

L

L

W

T

G

S

S

T

C

L

A

N

A

M

L

L

T

I

G

P

V

S

I

A

S

A

N

R

I

V

P

H

M

Y

L

G

M

C

V

V

I

I

R

F

F

V

S

Q

L

I

-

L

-

Q

G

G

V

L

V

V

E

Q

A

G

A

V

V

T

M
x
Y

P

P

A

A

M

C

L

H

I

G

Y

I

I

W

S

S

N

K

W

W

F

A

T

P

K

P

N

L

E
|
E

R

R

S

S

R

R

A

L

N

A

T

T

F

T

L

S

I

F

L

C

G
|
G

N

S

P
x
Y

V

A

T

G

V

A

L

V

W

I

M

A

S

M

V

P

L

L

S

A

G

G

Y

I

L

L

V

V

N

Q

S

Y

F

T

G

G

W

W

R

S

H

S

M

V

M

F

I

Y

A

V

E

Y

G

G

V

S

P

F

A

G

I

M

V

V

W

W

A

Y

C

M

I

F

W

W

W

L

F

L

V

V

V

S

Q

Y

D

E

K

S

P

P

A

A

E

K

S

H

T

P

W

T

L

I

Q

T

P

D

Q

E

E

E

K

R

A

R

D

Y

L

I

K

E

A

E

A

S

L

I

D

G

L

E

E

S

Q

A

V

N

G

L

M

L

K

G

P

A

M

M

R

E

N

K

Y

F

A

K

-

T

-

P

-

W

-

R

E

K

A

F

F

F

K

T

S

S

P

M

A

P

V

V

I

Y

K

A

L

I

C

I

A

V

Q

A

Y

N

F

F

C

C

W
x
R

S

S

I

W

G

T

V
x
F

Y
|
Y

G

L

F

L

V

L

L

I

W

S

L

Q

P

P

S

A

I

Y

L

F

K

E

N

E

A

V

A

F

N

G

I

F

S

E

M

I

V

S

E

K

T

V

G

G

W

M

L

L

S

S

S

A

L

V

P

P

Y

H

L

L

V

V

A

M

V

T

I

I

A

I

M

V

L

P

L

I

T

G

S

G

W

Q

A

I

S

A

D

D

K

F

M

L

Q

R

N

S

R

K

K

Q

L

I

F

L

-

S

-

T

V

V

W

R

P

K

A

I

L

M

L

N

I

C

G

G

A

G

L

F

A

G

F

M

L

E

G

A

S

T

Y

L

L

L

-

V

-

G

G

Y

S

S

S

H

N

T

F

R

W

G

L

V

S

A

Y

I

S

S

L

F

L

L

V

V

I

L

A

A

-

V

G

G

A

F

A

S

M

G

Y

F

A

A

P

I

Y

S

G

G

P

-

F

-

F

F

A

N

I

V

I

N

P

H

E

L

L

D

L

I

P

A

K

P

N

R

V

Y

A

A

G

S

G

I

A

L

M

M

A

G

L

I

I

S

N

N

S

G

M

V

G

G

A

T

L

L

G

S

S

G

F

M

L

V

G

C

S

P

Y

I

V

I

V

V

G

G

Y

A

L

M

N

T

G

K

A

N

T

K

G

S

S

R

P

E

S

E

A

W

S

Q

Y

Y

L

V

F

F

M

L

A

I

S

A

G

A

L

L

L

V

binding (1s,3r)-1-aminocyclopentane-1,3-dicarboxylic acid: Y77 (= Y62), Y137 (≠ M120), Y165 (≠ P148), R264 (≠ W243), F268 (≠ V247), Y269 (= Y248)
binding (2R)-2-(methoxymethyl)-4-{[(25R)-spirost-5-en-3beta-yl]oxy}butyl 4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside: E152 (= E135), G163 (= G146)

Sites not aligning to the query:

binding (2R)-2-(methoxymethyl)-4-{[(25R)-spirost-5-en-3beta-yl]oxy}butyl 4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside: 12, 13

P53322 High-affinity nicotinic acid transporter; Nicotinic acid permease from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
22% identity, 76% coverage: 1:323/425 of query aligns to 80:411/534 of P53322

query
sites
P53322

M

M

E

E

T

K

R

R

K

V

L

L

A

R

M

K

R

M

R

D

W

I

W

Y

F

L

I

I

M

-

P

P

I

L

V

M

F

G

I

M

T

L

Y

Y

S

F

L

L

A

S

Y

N

L

L

D

D

R

K

A

S

N

N

F

I

G

G

F

N

A

A

S

E

A

V

A

A

G

G

I

L

N

S

H

K

D

D

L

I

G

H

I

L

T

V

Q

G

G

T

T

Q

S

Y

S

N

L

T

I

C

G

V

A

T

L

V

F

F

I

A

G

T

Y

Y

F

V

F

L

F

F

Q

D

I

P

P

I

G

G

A

T

I

N

Y

L

A

L

E

K

R

I

R

M

S

G

V

P

K

P

K

L

M

M

I

M

F

S

W

I

S

C

L

L

V

T

L

C

W

F

G

G

S

A

C

I

A

S

A

L

L

G

T

T

G

A

V

W

I

V

S

K

N

N

I

Y

P

A

M

Q

L

L

M

I

V

V

I

V

R

R

F

L

S

L

L

L

G

G

V

A

V

F

E

E

A

G

A

M

V

I

M

Y

P

P

A

A

M

I

L

N

I

M

Y

Y

I

L

S

S

N

V

W

C

F

Y

T

R

K

R

N

E

E

Q

R

Y

S

A

R

L

A

R

N

F

T

A

F

F

L

V

I

F

L

S

G

A

N

A

P

C

V

L

T

S

V

S

L

S

W

F

-

G

-

L

-

I

-

A

-

Y

-

G

M

C

S

S

V

K

L

I

S

S

G

G

Y

S

L

L

V

K

N

D

S

-

F

-

G

-

W

W

R

Q

H

Y

M

I

M

Y

I

I

A

V

E

E

G

G

V

C

P

I

A

S

I

L

V

G

W

F

A

V

C

P

I

F

W

Y

W

A

F

F

V

G

V

L

Q

S

D

-

K

K

P

N

A

L

E

E

S

D

T

S

W

W

L

F

Q

F

P

N

Q
x
K

E

E

K

E

A

K

D

E

L

Y

K

I

A

S

A

E

L

R

D

Y

L

K

E

T

Q

M

V

N

G

T

M

F

K

D

P

P

M

D

R

E

N

K

Y

F

A

E

-

W

-

F

-

Q

-

V

-

W

E

Q

A

A

F

V

K

K

S

D

P

V

A

K

V

T

I

W

K

A

L

S

C

A

A

V

Q

A

Y

L

F

F

C

G

W

I

S

D

I

L

G

T

V

T

Y

F

G

G

F

L

V

T

L

V

W

F

L

L

P

P

S

I

I

I

L

I

K

T

N

S

A

M

A

G

N

F

I

T

S

N

M

V

V

R

E

A

T

Q

G

L

W

M

L

T

S

V

S

P

L

I

P

Y

Y

F

L

L

V

T

A

A

V

I

I

V

A

F

M

F

L

I

L

C

T

A

S

V

W

W

A

-

S

S

D

D

K

R

M

I

Q

K

N

L

R

R

K

S

L

P

F

F

V

I

W

L

P

G

A

A

L

C

L

L

-

T

-

S

I

I

G

G

A

I

L

A

A

I

F

V

L

L

G

G

S

S

Y

Q

L

V

L

H

G

G

S

V

S

R

N

Y

F

F

K283 (≠ Q202) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Q51955 4-hydroxybenzoate transporter PcaK from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
20% identity, 87% coverage: 9:377/425 of query aligns to 25:406/448 of Q51955

query
sites
Q51955

R

R

R

Y

W

Q

W

W

F

R

I

V

M

V

P

L

I

L

V

C

F

F

I

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I

Y

V

S

F

L

L

A
x
D

Y

G

L

L

D
|
D

R

T

A

A

N

A

F

M

G

G

F

F

A

I

S

A

A

P

A

A

G

-

I

L

N

S

H

Q

D

E

L

W

G

G

I

I

T

D

Q

R

G

A

T

S

S

L

S

G

L

P

I

V

G

M

A

S

L

A

F

A

F

L

I

I

G

G

Y

M

F

V

F

F

F

G

Q

A

I

L

P

G

G

S

A
x
G

I

P

Y

L

A

A

E
x
D

R

R

R

F

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x
G

V

R

K

K

K

G

M

V

I

L

F

V

W

G

S

A

L

V

V

L

L

V

W

F

G

G

S

G

C

F

A

S

A

L

L

A

T

S

G

A

V

Y

I

A

S

T

N

N

I

V

P

D

M

Q

L

L

M

L

V

V

I

L

R
|
R

F

F

S

L

L

T

G

G

V

L

V

G

E

L

A

G

A

A

V

G

M

M

P

P

A

N

M

A

L

T

I

T

Y

L

I

L

S

S

N
x
E

W

Y

F

T

T

P

K

E

N

R

E

L

R

K

S

S

R

L

A

L

N

V

T

T

F

S

L

M

I

F

L

C

G

G

N

F

P

N

V

L

T

G

V

M

L

A

W

G

M

G

S

G

V

F

L

I

S

S

G

A

Y

K

L

M

V

I

N

P

S

A

F

Y

G

G

W

W

R
x
H

H

S

M

L

I

V

A

I

E

G

G

G

V

V

P

L

A

P

I

L

V

L

W

L

A

A

C

L

I

V

W

L

-

M

-

V

-

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-

L

-

P

-

E

-

S

-

A

-

R

W

F

F

L

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V

Q

R

D

N

K

R

P

G

A

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E

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-

I

-

R

-

K

-

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-

L

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P

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A

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Q

E

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A

A

D

E

L

A

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A

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A

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E

E

Q

Q

V

K

G

A

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V

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A

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A

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N

V

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F

A

A

E

V

A

I

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S

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P

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-

Y

-

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-

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A

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A

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Y

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D

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-

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V

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A

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G

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D
|
D

K

R

M

Y

Q

N

N

P

R
x
H

K

K

L

V

F

I

V

G

W

I

P

F

A

Y

L

L

I

A

G

G

A

V

L

F

A

A

F

Y

L

A

G

V

S

G

Y

Q

L

S

L

L

G

G

S

-

N

N

F

I

W

T

L

V

S

L

Y

A

S

T

L

L

L

V

V

L

I

I

A

A

G

G

A

M

A

C

M

V

Y

N

A

G

P

A

Y

Q

G

S

P

A

F

M

F

P

A

S

I

L

I

A

P

A

E

R

L

F

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Y

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P

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N

Q

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A
x
R

G

A

G

T

A

G

M

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A

S

L

W

I

M

N

L

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G

M

I

G

G

A
x
R

L

F

G

G

S

A

F

I

L

L

G

G

S

A

Y

W

D41 (≠ A25) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
D44 (= D28) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
G85 (≠ A70) mutation to V: Abolishes 4-HBA transport and chemotaxis.
D89 (≠ E74) mutation to N: Abolishes 4-HBA transport and chemotaxis.
G92 (≠ S77) mutation to A: Decrease in 4-HBA transport and chemotaxis.; mutation to C: No change in 4-HBA transport and chemotaxis.; mutation G->L,V: Abolishes 4-HBA transport and chemotaxis.; mutation to Q: Decrease in 4-HBA transport and strong decrease in chemotaxis.
R124 (= R109) mutation to A: Abolishes 4-HBA transport.
E144 (≠ N129) mutation to A: Strong decrease in 4-HBA transport.
H183 (≠ R168) mutation to A: Decrease in 4-HBA transport and chemotaxis.
D323 (= D292) mutation to N: Abolishes 4-HBA transport and chemotaxis.
H328 (≠ R297) mutation to A: Decrease in 4-HBA transport and chemotaxis.; mutation to R: Decrease in 4-HBA transport and loss of chemotaxis.
R386 (≠ A357) mutation to A: Strong decrease in 4-HBA transport.
R398 (≠ A369) mutation to A: Abolishes 4-HBA transport.

Sites not aligning to the query:

444 H→A: No change in 4-HBA transport and chemotaxis.

Q9C0U9 Uncharacterized transporter PB1C11.03 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
25% identity, 42% coverage: 26:204/425 of query aligns to 114:296/570 of Q9C0U9

query
sites
Q9C0U9

Y

F

L

I

D

G

R

K

A

A

N

T

F

L

G

S

F

Y

A

S

S

T

A

I

A

L

G

G

I

L

N

F

H

D

D

D

L

V

G

H

I

I

T

T

Q

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G

N

T

Q

S

Y

S

N

L

N

I

L

G

N

A

T

L

L

F

F

F

Y

I

V

G

G

Y

Y

F

I

F

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F

G

Q

Q

I

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P

G

G

A

H

I

Y

Y

I

A

M

E

Q

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R

F

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L

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G

K

K

M

F

I

V

-

G

-

L

-

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T

-

F

F

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W

W

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L

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V

I

L

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W

F

G

L

S

H

C

C

A

C

A

A

L

Y

T

-

G

-

V

-

I

-

S

-

N

N

I

Y

P

G

M

G

L

L

M

I

V

A

I

L

R

R

F

F

S

F

L

L

G

G

V

F

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T

E

E

A

S

A

C

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L

M

L

P

P

A

A

M

M

L

E

I

A

Y

T

I

M

S

G

N

M

W

F

F

F

T

T

K

H

N

Q

E

E

R

Q

S

A

R

-

A

-

N

-

T

-

F

F

L

L

I

-

L

-

G

-

N

Q

P

P

V

-

T

-

V

V

L

F

W

W

M

I

S

S

V

C

L

L

S

S

-

C

-

G

-

I

-

P

-

A

-

G

-

F

-

I

-

A

-

Y

-

G

-

L

G

E

Y

F

L

V

V

T

N

K

S

S

F

I

G

A

-

P

W

W

R

K

H

L

M

F

M

M

I

I

A

I

E

T

G

G

V

G

P

I

A

T

I

F

V

F

W

L

A

S

C

I

I

F

W

L

W

F

F

F

V

Y

Q

P

D

D

K

N

P

P

A

S

E

K

S

A

T

R

W

F

L

L

Q

T

P

D

Q

E

E

E

K

K

Sites not aligning to the query:

14 modified: Phosphoserine

Q9Y2C5 Probable small intestine urate exporter; Solute carrier family 17 member 4 from Homo sapiens (Human) (see 2 papers)
21% identity, 47% coverage: 100:299/425 of query aligns to 161:360/497 of Q9Y2C5

query
sites
Q9Y2C5

S

A

N

G

I

V

P

A

M

L

L

L

M

I

V

V

I

L

R

R

F

I

S

V

L

Q

G

G

V

I

V

A

E

Q

A

V

A

M

V

V

M

L

P

T

A

G

M

Q

L

Y

I

S

Y

I

I

W

S

V

N

K

W

W

F

A

T

P

K

P

N

L

E

E

R

R

S

S

R

Q

A

L

N

T

T

T

F

I

L

A

I

G

L

S

G

G

N

S

P

M

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L

T

G

V

S

L

F

W

I

M

V

S

L

V

L

L

A

S

G

G

G

Y

L

L

L

V

C

N

Q

S

T

F

I

G

G

W

W

R

P

H

Y

M

V

M

F

I

Y

A

I

E

F

G

G

V

G

P

I

A

G

I

C

V

A

W

C

A

C

C

P

I

L

W

W

W

F

F

P

V

L

V

I

Q

Y

D

D

K

D

P

P

A

V

E

N

S

H

T

P

W

F

L

I

Q

S

P

A

Q

G

E

E

K

K

A

R

D

Y

L

I

K

V

A

C

A

S

L

L

D

A

L

Q

E

Q

Q

D

V

C

G

S

M

P

K

G

-

W

-

S

-

L

P

P

M

I

R

R

N

-

Y

-

A

-

E

A

A

M

F

I

K

K

S

S

P

L

A

P

V

L

I

W

K

A

L

I

C

L

A

V

Q

S

Y

Y

F

F

C

C

W

E

S

Y

I

W

G

L

V

F

Y

Y

G

T

F

I

V

M

L

A

W

Y

L

T

P

P

S

T

I

Y

L

I

K

S

N

S

A

V

A

L

N

Q

I

A

S

N

M

L

V

R

E

D

T

S

G

G

W

I

L

L

S

S

S

A

L

L

P

P

Y

F

L

V

V

V

A

G

V

C

I

I

A

C

M

I

L

I

L

L

T

G

S

G

W

L

A

L

S

A

D

D

K

F

M

L

Q

L

N

S

R

R

K

K

L

I

Sites not aligning to the query:

66 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: Loss of glycosylation and significant reduction in the transport of thyroid hormones T3 and T4; when associated with A-75 and A-90.
75 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: Loss of glycosylation and significant reduction in the transport of thyroid hormones T3 and T4; when associated with A-66 and A-90.
90 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: Loss of glycosylation and significant reduction in the transport of thyroid hormones T3 and T4; when associated with A-75 and A-90.
372 A → T: in dbSNP:rs11754288

Query Sequence

>WP_061941349.1 NCBI__GCF_001584185.1:WP_061941349.1
METRKLAMRRWWFIMPIVFITYSLAYLDRANFGFASAAGINHDLGITQGTSSLIGALFFI
GYFFFQIPGAIYAERRSVKKMIFWSLVLWGSCAALTGVISNIPMLMVIRFSLGVVEAAVM
PAMLIYISNWFTKNERSRANTFLILGNPVTVLWMSVLSGYLVNSFGWRHMMIAEGVPAIV
WACIWWFVVQDKPAESTWLQPQEKADLKAALDLEQVGMKPMRNYAEAFKSPAVIKLCAQY
FCWSIGVYGFVLWLPSILKNAANISMVETGWLSSLPYLVAVIAMLLTSWASDKMQNRKLF
VWPALLIGALAFLGSYLLGSSNFWLSYSLLVIAGAAMYAPYGPFFAIIPELLPKNVAGGA
MALINSMGALGSFLGSYVVGYLNGATGSPSASYLFMASGLLAAVVLTISIKPEAQAMPLA
QSVTQ

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