SitesBLAST

S189 (= S101) to L: no changes in MPP(+) uptake; dbSNP:rs34104736
G220 (≠ A140) to V: affects transporter activity; reduction of MPP(+) uptake when associated with V-408; dbSNP:rs36103319
Y240 (≠ P160) mutation to F: Decreased TEA uptake.
P283 (= P195) to L: in dbSNP:rs4646277; mutation to A: Decreased TEA uptake.
R287 (vs. gap) to G: in dbSNP:rs4646278
P341 (≠ H240) to L: affects transporter activity; reduction of TEA uptake; reduction o MPP(+) uptake when associated with V-408; largely localized to the plasma membrane; dbSNP:rs2282143
R342 (≠ K241) to H: no changes in MPP(+) uptake when associated with V-408; dbSNP:rs34205214
Y361 (= Y275) mutation to F: Decreased TEA uptake.
Y376 (≠ F290) mutation to F: Decreased TEA uptake.
G401 (= G306) to S: affects transporter activity; reduction of MPP(+), serotonin and TEA uptake; no MPP(+) uptake when associated with L-160; dbSNP:rs34130495
M408 (≠ I313) to V: does not affect transporter activity; no changes in MPP(+) uptake when associated with F-14; no changes in MPP(+) uptake when associated with F-85; no changes in MPP(+) uptake when associated with L-189; no changes in MPP(+) uptake when associated with H-342; no changes in MPP(+) uptake when associated with M-420 del; no changes in MPP(+) uptake when associated with I-440; no changes in MPP(+) uptake when associated with I-461; no changes in MPP(+) uptake when associated with M-488; reduction of MPP uptake when associated with C-61; no MPP(+) uptake when associated with V-220; reduction of MPP(+) uptake when associated with L-341; no MPP(+) uptake when associated with S-401; no MPP(+) uptake when associated with R-465; dbSNP:rs628031
M420 (= M325) natural variant: Missing (reduction of serum O-isobutanoyl-(R)-carnitine levels; no change in MPP(+) uptake; no changes in MPP(+) uptake when associated with V-408; dbSNP:rs72552763)
M440 (= M347) to I: in dbSNP:rs35956182
V461 (= V366) to I: no changes in MPP(+) uptake when associated with V-408; dbSNP:rs34295611
G465 (= G370) to R: reduction of the localization to the basolateral membrane; no MPP(+) uptake when associated with V-408; dbSNP:rs34059508; mutation to A: No changes in MPP(+) uptake.

Sites not aligning to the query:

14 S → F: exclusively found in the African American population; increased MPP(+) uptake when associated with V-408; dbSNP:rs34447885
24 I→L: No change in fenoterol uptake. No change in trospium uptake. No change in terbutaline uptake.
28 L→I: No change in fenoterol uptake. No change in trospium uptake. No change in terbutaline uptake.
31 A→S: No change in fenoterol uptake. No change in trospium uptake. No change in terbutaline uptake.
32 F→L: No change in fenoterol uptake. Decreased trospium uptake. Decreased trospium affinity.
36 C→Y: Increased fenoterol uptake. Increased fenoterol affinity. No change in trospium uptake. No change in terbutaline uptake. No change in terbutaline affinity.
41 F → L: in dbSNP:rs2297373
61 R → C: affects transporter activity; reduction of MPP(+) uptake; reduction of serum O-isobutanoyl-(R)-carnitine levels; reduction of MPP(+) uptake when associated with V-408; dbSNP:rs12208357
85 L → F: no changes in MPP(+) uptake; when associated with V-408; dbSNP:rs35546288
88 C → R: affects transporter activity; reduction of MPP(+), serotonin and TEA uptake; dbSNP:rs55918055
160 L → F: no changes in both MPP(+) and TEA uptake; abolishes MPP(+) uptake when associated with S-401; largely localized to the plasma membrane; dbSNP:rs683369
488 R → M: no changes in MPP(+) uptake when associated with V-408; dbSNP:rs35270274

8sc2A Human oct1 bound to diltiazem in inward-open conformation (see paper)
26% identity, 73% coverage: 79:389/426 of query aligns to 149:422/453 of 8sc2A

query
sites
8sc2A

G

G

H

Y

F

F

G

A

D

D

K

R

I

F

G

G

R

R

K

K

A

L

T

C

L

L

V

L

A

G

A

T

L

V

M

L

T

V

M

N

G

A

L

V

S

S

T

G

V

V

A

L

I

M

G

A

F

F

L

S

P

P

T

N

Y

Y

A

M

S

S

I

-

G

-

V

-

A

-

P

-

L

-

L

M

A

L

L

L

C

F

R

R

L

L

G

L

Q

Q

G

G

L

L

G

V

L

S

G

K

G

G

E

N

W
|
W

G

M

G

A

A

G

V

Y

L

T

L

L

A

I

T

T

E

E

N

F

A

V

P

G

E

S

G

G

K

S

R

R

T

R

W

T

Y

V

G

A

M

I

F

M

P

Y

Q
|
Q

L

M

G

A

A
x
F

P

T

A

V

G

G

F

L

I

V

L

A

A

L

T

T

G

G

I

L

-

A

-

Y

-

A

-

L

-

P

-

H

-

W

-

R

F

W

L

L

L

Q

L

L

A

A

E

V

T

S

M

L

T

P

E

T

E

F

Q

L

F

F

F

L

A

L

Y

Y

G

Y

W

W

R

C

V

V

P

P

F

-

I

-

A

-

S

-

A

-

I

-

L

-

V

-

A

-

V

-

G

-

L

-

F

-

I

-

R

-

L

-

R

E

I

S

A

P

E

R

T

S

P

P

E

S

F

F

Q

-

K

-

A

-

I

-

D

-

K

-

A

-

E

-

R

-

V

-

A

-

V

-

P

-

A

-

A

A

Q

D

L

L

F

F

R

R

H

T

H

P

K

R

M

L

N

R

L

-

F

-

L

-

G

-

T

-

I

-

G

-

T

-

M

K

A

R

T

T

F

F

V

I

L

L

F

M

Y

Y

L

L

M

-

T

-

V

-

F

-

S

-

L

-

G

-

W
|
W

G

F

T

T

R

D

A
x
S

L

V

G

L

Y

Y

S

-

R

-

E

-

E

Q

F

G

L

L

V

I

L

L

Q

H

M

M

-

G

-

A

-

T

I

S

G

G

V

N

I

L

F

Y

F

L

G

D

-

F

-

L

-

Y

-

S

-

A

-

L

L

V

T

E

I

I

P

P

-

G

-

A

-

F

L

I

S

A

A

L

L

I

L

T

S

I

D

D

R

R

Y

V

G

G

M

R

R

I

T

Y

I

P

M

M

V

A

I

M

V

S

T

N

V

L

L

L

I

A

G

G

L

A

Y

A

G

C

F

L

I

V

M

M

A

-

P

-

L

I

F

F

A

I

A

S

G

P

T

D

A

L

G

H

V

W

L

L

G

N

F

I

L

I

I

I

I

M

G

C

F

V

G

G

L

R

M

M

G

G

M

I

T

T

Y

I

G

A

-
x
I

-

Q

P

M

I

I

G

C

A

L

V

V

L

N

A

A

E

E

P

L

F

Y

P

P

T

T

S

F

V

V

R

R

Y

N

T

L

G

G

A

V

S

M

L

V

A

C

F

S

N

S

L

L

A

C

G

D

I

I

L

-

G

G

A

G

S

I

L

I

A

T

P

P

Y

F

I

I

binding Diltiazem: W199 (= W137), Q223 (= Q161), F226 (≠ A164), W293 (= W268), S297 (≠ A272), I385 (vs. gap)

Sites not aligning to the query:

binding Diltiazem: 18

Q9VCA2 Organic cation transporter protein from Drosophila melanogaster (Fruit fly) (see paper)
26% identity, 75% coverage: 73:390/426 of query aligns to 143:475/548 of Q9VCA2

query
sites
Q9VCA2

V

L

G

G

A

S

A

L

I

I

F

F

G

G

H

Q

F

M

G

S

D

D

K

K

I

L

G

G

R

R

K

K

A

P

T

T

L

F

V

F

A

A

A

S

L

L

M

V

T

L

M

Q

G

L

L

I

S

F

T

G

V

V

A

L

I

A

G

A

F

V

L

A

P

P

T

E

Y

Y

A

F

S

S

I

Y

G

T

V

I

A

S

A

-

P

-

L

-

A

-

L

-

C

-

R

R

L

M

G

I

Q

V

G

G

L

A

G

T

L

T

G

S

G

G

E

V

W

F

G

L

G

V

A

A

V

Y

L

V

L

I

A

A

T

L

E

E

N

M

A

V

P

G

E

S

G

S

K

Y

R

R

T

L

W

F

Y

A

G

G

M

V

F

A

P

M

Q

Q

L

M

G

F

A

F

P

S

A

V

G

G

F

F

I

M

L

L

A

T

T

A

G

G

I

F

-

A

-

Y

-

F

-

I

-

H

-

D

-

W

-

R

F

W

L

L

L

Q

L

I

A

A

E

I

T

T

M

L

T

P

E

G

E

L

Q

L

F

F

F

L

A

C

Y

Y

G

Y

W

W

R

I

V

I

P

P

F

E

I

S

A

A

S

R

A

W

I

L

L

L

-

M

-

K

-

G

-

R

-

K

-

D

-

E

-

A

-

F

V

V

A

I

V

I

G

E

L

K

F

A

I

A

R

K

L

E

R

N

I

K

A

V

E

E

T

V

P

P

E

N

-

E

-

I

F

Y

Q

E

K

Q

A

L

I

V

D

D

K

E

-

V

A

A

E

E

R

K

-

K

-

Q

-

D

-

E

-

M

-

A

V

A

A

S

V

Q

P

P

A

A

Q

T

L

V

F

F

-

D

-

L

R

R

H

Y

H

P

K

N

M

L

N

R

L

R

F

-

L

-

G

-

T

-

I

-

G

K

T

T

M

L

A

L

T

I

F

F

V

F

L

D

F

W

Y

F

L

V

M

N

T

S

-

G

-

V

V

Y

F

Y

S

G

L

L

G

S

W

W

G

N

T

T

R

N

A

N

L

L

G

G

Y

G

S

N

R

Q

E

-

F

-

L

L

V

V

L

N

Q

F

M

M

I

I

G

S

-

G

-

A

V

V

I

E

F

I

F

P

G

G

L

Y

T

T

I

L

P

L

L

L

S

F

A

T

L

L

L

-

S

-

D

N

R

R

Y

W

G

G

M

R

R

R

T

S

I

I

M

L

V

C

I

G

V

T

T

M

V

M

L

V

I

A

G

G

L

I

Y

S

G

-

F

-

I

L

M

L

A

A

P

T

L

I

F

F

A

V

A

P

G

S

T

D

A

-

G

-

V

-

L

M

G

N

F

W

L

L

I

I

I

V

G

A

F

C

G

A

L

M

M

I

G

G

M

K

-

L

-

A

-

I

-

T

-

S

T

S

Y

Y

G

G

P

T

I

I

G

Y

A

I

V

F

L

S

A

A

E

E

P

Q

F

F

P

P

T

T

S

V

V

V

R

R

Y

N

T

V

G

G

A

L

S

G

L

-

A

A

F

S

N

S

L

M

A

V

G

A

I

R

L

V

G

G

A

G

S

I

L

L

A

A

P

P

Y

Y

I

L

A

K

Sites not aligning to the query:

97 modified: carbohydrate, N-linked (GlcNAc...) asparagine

Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) (see paper)
26% identity, 49% coverage: 16:222/426 of query aligns to 39:228/444 of Q8NLB7

query
sites
Q8NLB7

R

R

V

R

L

L

T

A

A

A

S

V

M

L

I

I

G

G

T

W

T

F

I

F

E

V

F

I

F

F

D
|
D

F

G

Y

Y

-
x
D

-

L

-

I

I

V

Y

Y

A

G

T

T

A

V

A

Q

V

S

I

A

V

L

F

-

P

-

H

-

L

-

F

-

P

-

A

A

S

K

D

E

G

W

N

N

-

L

-

S

S

S

A

A

L

T

L

L

Q

G

S

T

F

I

A

G

T

S

F

-

A

-

I

T

A

A

F

F

A

G

R

M

P

A

V

I

G

G

A

A

A

V

I

F

F

I

G

G

H

R

F

L

G

S

D

D

K
x
R

I

V

G

G

R

R

K

K

A

A

T

A

L

V

V

I

A

G

A

S

L

V

M

L

T

I

M

L

G

S

L

V

S

F

T

T

V

M

A

L

I

C

G

A

F

F

L

A

P

P

T

N

Y

-

A

-

S

-

I

-

G

-

V

-

A

-

P

P

L

W

L

V

L

F

A

G

L

A

C

F

R

R

L

F

G

I

Q

A

G

G

L

L

G

G

L

L

G

G

E

L

W

V

G

P

G

S

A

V

V

N

L

A

L

M

A

T

T

S

E

D

N

L

A

V

P

P

E

R

G

K

K

T

R

M

T

S

W

A

Y

W

G

A

M

T

F

V

P

M

Q

M

L

S

G

G

A

V

P

P

A

I

G

G

F

G

I

S

L

I

A

A

T

A

G

V

I

L

F

A

L

L

L

V

A

V

E

P

T

S

M

S

T

E

E

E

E

-

Q

-

F

-

A

-

Y

W

G

G

W

W

R

R

V

F

P

M

F

F

I

L

A

I

S

A

A

L

I

I

L

P

V

L

A

V

V

V

G

G

L

L

F

P

I

I

R

A

L

M

R

K

I

V

A

I

E

P

T

S

P

D

E

K

F

A

Q

I

K

K

A

A

D54 (= D31) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
D57 (vs. gap) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
R103 (≠ K84) mutation to A: Loss of transport activity.

Sites not aligning to the query:

309 W→V: Loss of transport activity.
312 D→A: Loss of transport activity.
313 R→A: Loss of transport activity.
317 mutation I->H,Y: Loss of transport activity.
386 R→A: Loss of transport activity.

8sc6A Human oct1 bound to thiamine in inward-open conformation (see paper)
26% identity, 73% coverage: 79:389/426 of query aligns to 149:415/447 of 8sc6A

query
sites
8sc6A

G

G

H

Y

F

F

G

A

D

D

K

R

I

F

G

G

R

R

K

K

A

L

T

C

L

L

V

L

A

G

A

T

L

V

M

L

T

V

M

N

G

A

L

V

S

S

T

G

V

V

A

L

I

M

G

A

F

F

L

S

P

P

T

N

Y

Y

A

M

S

S

I

-

G

-

V

-

A

-

P

-

L

-

L

M

A

L

L

L

C

F

R

R

L

L

G

L

Q

Q

G

G

L

L

G

V

L

S

G

K

G

G

E

N

W

W

G

M

G

A

A

G

V

Y

L

T

L

L

A

I

T

T

E

E

N

F

A

V

P

G

E

S

G

G

K

S

R

R

T

R

W

T

Y

V

G

A

M

I

F

M

P

Y

Q
|
Q

L

M

G

A

A
x
F

P

T

A

V

G

G

F

L

I

V

L

A

A

L

T

T

G

G

I

L

F

A

L

Y

L

A

L

L

A

P

E

H

T

-

M

-

T

-

E

-

Q

-

F

-

A

-

Y

-

G

-

W

W

R

R

V

W

P

L

F

Q

I

L

A

A

S

-

A

-

I

-

L

-

V

V

A

S

V

L

G

P

L

T

F

F

I

L

R

F

L

L

R

L

I

Y

A

Y

E

W

T

S

P

P

E

S

F

F

Q

-

K

-

A

-

I

-

D

-

K

-

A

-

E

-

R

-

V

-

A

-

V

-

P

-

A

-

A

A

Q

D

L

L

F

F

R

R

H

T

H

P

K

R

M

L

N

R

L

-

F

-

L

-

G

-

T

-

I

-

G

-

T

-

M

K

A

R

T

T

F

F

V

I

L

L

F

M

Y

Y

L

L

M

-

T

-

V

-

F

-

S

-

L

-

G

-

W

W

G

F

T

T

R

D

A

S

L

V

G

L

Y
|
Y

S

-

R

-

E

-

E
x
Q

F

G

L

L

V

I

L

L

Q

H

M

M

-

G

-

A

-

T

I

S

G

G

V

N

I

L

F

Y

F

L

G

D

-

F

-

L

-

Y

-

S

-

A

-

L

L

V

T
x
E

I

I

P

P

-

G

-

A

-

F

L

I

S

A

A

L

L

I

L

T

S

I

D

D

R

R

Y

V

G

G

M

R

R

I

T

Y

I

P

M

M

V

A

I

M

V

S

T

N

V

L

L

L

I

A

G

G

L

A

Y

A

G

C

F

L

I

V

M

M

A

-

P

-

L

I

F

F

A

I

A

S

G

P

T

D

A

L

G

H

V

W

L

L

G

N

F

I

L

I

I

I

I

M

G

C

F

V

G

G

L

R

M

M

G

G

M

I

T

T

Y

I

G

A

-
x
I

-
x
Q

P

M

I

I

G

C

A

L

V

V

L

N

A

A

E

E

P

L

F

Y

P

P

T

T

S

F

V

V

R

R

Y

N

T

L

G

G

A

V

S

M

L

V

A

C

F

S

N

S

L

L

A

C

G

D

I

I

L

-

G

G

A

G

S

I

L

I

A

T

P

P

Y

F

I

I

binding 3-(4-amino-2-methyl-pyrimidin-5-ylmethyl)-5-(2-hydroxy-ethyl)-4-methyl-thiazol-3-ium: Q223 (= Q161), F226 (≠ A164), Y293 (= Y275), Q294 (≠ E279), E318 (≠ T294), I378 (vs. gap), Q379 (vs. gap)

8et8A Cryo-em structure of the organic cation transporter 1 in complex with verapamil (see paper)
24% identity, 73% coverage: 79:389/426 of query aligns to 166:482/532 of 8et8A

query
sites
8et8A

G

G

H

Y

F

I

G

A

D

D

K

R

I

F

G

G

R

R

K

K

A

L

T

C

L

L

V

L

A

A

A

T

L

T

M

L

T

I

M

S

G

A

L

V

S

S

T

G

V

V

A

L

I

M

G

A

F

V

L

A

P

P

T

D

Y

Y

A

T

S

S

I

-

G

-

V

-

A

-

P

-

L

-

L

M

A

L

L

L

C

F

R

R

L

L

G

L

Q

Q

G

G

L

L

G

V

L

S

G
x
K

G

G

E

S

W
|
W

G

M

G

S

A

G

V

Y

L

T

L

L

A

I

T

T

E

E

N

F

A

V

P

G

E

S

G

G

K

Y

R

R

T

R

W

T

Y

V

G

A

M

I

F

L

P

Y

Q
|
Q

L

M

G

A

A

F

P

T

A

V

G

G

F

L

I

V

L

L

A

L

T

S

G

G

I

V

-

A

-

Y

-

A

-

I

-

P

-

H

-

W

-

R

F

W

L

L

L

Q

L

L

A

A

E

V

T

S

M

L

T

P

E

T

E

F

Q

L

F

F

F

L

A

L

Y

Y

G

Y

W

W

R

C

V

V

P

P

-

E

-

S

-

P

-

R

F

W

I

L

A

L

S

S

A

Q

I

K

L

R

V

N

A

T

V

Q

G

A

L

I

F

K

I

I

R

M

L

D

R

H

I

I

A

A

E

Q

T

K

-

N

-

G

-

K

-

L

-

P

P

P

E

A

F

D

Q

L

K

K

A

M

I

L

-

S

-

L

-

K

-

E

D

D

K

S

A

T

E

E

R

K

V

L

A

S

V

P

P

S

A

F

A

A

Q

D

L

L

F

F

R

R

H

T

H

P

K

Q

M

L

N

R

L

-

F

-

L

-

G

-

T

-

I

-

G

-

T

-

M

K

A

H

T

T

F

F

V

I

L

L

F

M

Y

Y

L

L

M

-

T

-

V

-

F

-

S

-

L

-

G

-

W
|
W

G

F

T

T

R

S

A

S

L

V

G

L

Y
|
Y

S

-

R

-

E

-

E

Q

F

G

L

L

V

I

L

M

Q

H

M

M

I

G

G

A

V

T

-

G

-

N

-

L

-

Y

-

L

-

D

I
x
F

F

F

F

Y

G
x
S

L

A

T

L

I

V

P
x
E

L

F

S

P

A

A

-

A

-

F

-

I

-

L

L

V

L

T

S

I

D

D

R

R

Y

V

G

G

M

R

R

I

T

Y

I

P

M

L

V

A

I

V

V

S

T

N

V

L

L

V

I

A

G

G

L

A

Y

A

G

C

F

L

I

I

M

M

A

-

P

-

L

I

F

F

A

I

A

S

G

Q

T

D

A

L

G

H

V

W

L

L

G

N

F

I

L

T

I

V

I

A

G

C

F

V

G

G

L

R

M

M

G

G

M

I

T

T

-

I

-

V

Y

F

G

Q

P

M

I

V

G
x
C

A

L

V

V

L

N

A

A

E

E

P

L

F

Y

P

P

T

T

S

F

V

I

R

R

Y

N

T

L

G

G

A

V

S

M

L

V

A

C

F
x
S

N

S

L

L

A

C

G

D

I

-

L

L

G

G

A

G

S

I

L

I

A

T

P

P

Y

F

I

L

binding (2S)-2-(3,4-dimethoxyphenyl)-5-{[2-(3,4-dimethoxyphenyl)ethyl](methyl)amino}-2-(propan-2-yl)pentanenitrile: K213 (≠ G134), W216 (= W137), Q240 (= Q161), W353 (= W268), Y360 (= Y275), F378 (≠ I289), S381 (≠ G292), E385 (≠ P296), C449 (≠ G355), S469 (≠ F375)

Sites not aligning to the query:

binding (2S)-2-(3,4-dimethoxyphenyl)-5-{[2-(3,4-dimethoxyphenyl)ethyl](methyl)amino}-2-(propan-2-yl)pentanenitrile: 31, 35

8et7A Cryo-em structure of the organic cation transporter 1 in complex with diphenhydramine (see paper)
24% identity, 73% coverage: 79:389/426 of query aligns to 166:482/532 of 8et7A

query
sites
8et7A

G

G

H

Y

F

I

G

A

D

D

K

R

I

F

G

G

R

R

K

K

A

L

T

C

L

L

V

L

A

A

A

T

L

T

M

L

T

I

M

S

G

A

L

V

S

S

T

G

V

V

A

L

I

M

G

A

F

V

L

A

P

P

T

D

Y

Y

A

T

S

S

I

-

G

-

V

-

A

-

P

-

L

-

L

M

A

L

L

L

C

F

R

R

L

L

G

L

Q

Q

G

G

L

L

G

V

L

S

G

K

G

G

E

S

W

W

G

M

G

S

A

G

V

Y

L

T

L

L

A

I

T

T

E

E

N

F

A

V

P

G

E

S

G

G

K

Y

R

R

T

R

W

T

Y

V

G

A

M

I

F

L

P

Y

Q

Q

L

M

G

A

A

F

P

T

A

V

G

G

F

L

I

V

L

L

A

L

T

S

G

G

I

V

-

A

-

Y

-

A

-

I

-

P

-

H

-

W

-

R

F

W

L

L

L

Q

L

L

A

A

E

V

T

S

M

L

T

P

E

T

E

F

Q

L

F

F

F

L

A

L

Y

Y

G

Y

W

W

R

C

V

V

P

P

-

E

-

S

-

P

-

R

F

W

I

L

A

L

S

S

A

Q

I

K

L

R

V

N

A

T

V

Q

G

A

L

I

F

K

I

I

R

M

L

D

R

H

I

I

A

A

E

Q

T

K

-

N

-

G

-

K

-

L

-

P

P

P

E

A

F

D

Q

L

K

K

A

M

I

L

-

S

-

L

-

K

-

E

D

D

K

S

A

T

E

E

R

K

V

L

A

S

V

P

P

S

A

F

A

A

Q

D

L

L

F

F

R

R

H

T

H

P

K

Q

M

L

N

R

L

-

F

-

L

-

G

-

T

-

I

-

G

-

T

-

M

K

A

H

T

T

F

F

V

I

L

L

F

M

Y

Y

L

L

M

-

T

-

V

-

F

-

S

-

L

-

G

-

W

W

G

F

T

T

R

S

A

S

L

V

G

L

Y

Y

S

-

R

-

E

-

E

Q

F

G

L

L

V

I

L

M

Q

H

M

M

I

G

G

A

V

T

-

G

-

N

-

L

-

Y

-

L

-

D

I

F

F

F

F

Y

G

S

L

A

T

L

I

V

P
x
E

L

F

S

P

A

A

-

A

-

F

-

I

-

L

L

V

L

T

S

I

D

D

R

R

Y

V

G

G

M

R

R

I

T

Y

I

P

M

L

V

A

I

V

V

S

T

N

V

L

L

V

I

A

G

G

L

A

Y

A

G

C

F

L

I

I

M

M

A

-

P

-

L

I

F

F

A

I

A

S

G

Q

T

D

A

L

G

H

V

W

L

L

G

N

F

I

L

T

I

V

I

A

G

C

F

V

G

G

L

R

M

M

G

G

M

I

T

T

-

I

-

V

Y
x
F

G

Q

P

M

I

V

G

C

A

L

V

V

L

N

A

A

E

E

P

L

F

Y

P

P

T

T

S

F

V

I

R

R

Y

N

T

L

G

G

A

V

S

M

L

V

A

C

F

S

N

S

L

L

A

C

G

D

I

-

L

L

G

G

A

G

S

I

L

I

A

T

P

P

Y

F

I

L

binding n-[2-(benzhydryloxy)ethyl]-n,n-dimethylamine: E385 (≠ P296), F445 (≠ Y351)

Sites not aligning to the query:

binding n-[2-(benzhydryloxy)ethyl]-n,n-dimethylamine: 35

8sc3A Human oct1 bound to fenoterol in inward-open conformation (see paper)
26% identity, 73% coverage: 79:389/426 of query aligns to 149:413/445 of 8sc3A

query
sites
8sc3A

G

G

H

Y

F

F

G

A

D

D

K

R

I

F

G

G

R

R

K

K

A

L

T

C

L

L

V

L

A

G

A

T

L

V

M

L

T

V

M

N

G

A

L

V

S

S

T

G

V

V

A

L

I

M

G

A

F

F

L

S

P

P

T

N

Y

Y

A

M

S

S

I

-

G

-

V

-

A

-

P

-

L

-

L

M

A

L

L

L

C

F

R

R

L

L

G

L

Q

Q

G

G

L

L

G

V

L

S

G

K

G

G

E

N

W
|
W

G
x
M

G

A

A

G

V

Y

L

T

L

L

A

I

T

T

E

E

N

F

A

V

P

G

E

S

G

G

K

S

R

R

T

R

W

T

Y

V

G

A

M

I

F

M

P

Y

Q
|
Q

L

M

G

A

A
x
F

P

T

A

V

G

G

F

L

I

V

L

A

A

L

T

T

G

G

I

L

F

A

L

Y

L

A

L

L

A

P

E

H

T

-

M

-

T

-

E

-

Q

-

F

-

A

-

Y

-

G

-

W

W

R

R

V

-

P

-

F

-

I

-

A

-

S

-

A

W

I

L

L

Q

V

L

A

A

V

V

G

S

L

L

F

P

I

T

R

F

L

L

R

F

I

L

A

L

E

Y

T

Y

P

P

E

S

F

F

Q

-

K

-

A

-

I

-

D

-

K

-

A

-

E

-

R

-

V

-

A

-

V

-

P

-

A

-

A

A

Q

D

L

L

F

F

R

R

H

T

H

P

K

R

M

L

N

R

L

-

F

-

L

-

G

-

T

-

I

-

G

-

T

-

M

K

A

R

T

T

F

F

V

I

L

L

F

M

Y

Y

L

L

M

-

T

-

V

-

F

-

S

-

L

-

G

-

W
|
W

G

F

T

T

R

D

A

S

L

V

G

L

Y
|
Y

S

-

R

-

E

-

E

Q

F

G

L

L

V

I

L

L

Q

H

M

M

-

G

-

A

-

T

I

S

G

G

V

N

I

L

F

Y

F

L

G

D

-

F

-

L

-

Y

-

S

-

A

-

L

L

V

T

E

I

I

P

P

-

G

-

A

-

F

L

I

S

A

A

L

L

I

L

T

S

I

D

D

R

R

Y

V

G

G

M

R

R

I

T

Y

I

P

M

M

V

A

I

M

V

S

T

N

V

L

L

L

I

A

G

G

L

A

Y

A

G

C

F

L

I

V

M

M

A

-

P

-

L

I

F

F

A

I

A

S

G

P

T

D

A

L

G

H

V

W

L

L

G

N

F

I

L

I

I

I

I

M

G

C

F

V

G

G

L

R

M

M

G

G

M

I

T

T

Y

I

G

A

-
x
I

-

Q

P

M

I

I

G
x
C

A

L

V

V

L

N

A

A

E

E

P

L

F

Y

P

P

T

T

S

F

V

V

R

R

Y

N

T

L

G

G

A

V

S

M

L

V

A

C

F

S

N

S

L

L

A

C

G

D

I

I

L

-

G

G

A

G

S

I

L

I

A

T

P

P

Y

F

I

I

binding Fenoterol: W199 (= W137), M200 (≠ G138), Q223 (= Q161), F226 (≠ A164), W284 (= W268), Y291 (= Y275), I376 (vs. gap), C380 (≠ G355)

O15244 Solute carrier family 22 member 2; Organic cation transporter 2; hOCT2 from Homo sapiens (Human) (see 8 papers)
25% identity, 79% coverage: 54:389/426 of query aligns to 145:484/555 of O15244

query
sites
O15244

N

N

S

S

A

W

L

M

L

L

Q

D

S

L

F

F

-

Q

A

S

T

S

F

V

A

N

I

V

A

G

F

F

A

-

R

-

P

-

V

I

G

G

A

S

A
x
M

I

S

F

I

G

G

H
x
Y

F

I

G

A

D

D

K

R

I

F

G

G

R

R

K

K

A

L

T

C

L

L

V

L

A

T

L

V

M

L

T

I

M

N

G

A

L

A

S

A

T

G

V

V

A

L

I

M

G

A

F

I

L

S

P

P

T

T

Y

Y

A
x
T

S

-

I

-

G

-

V

-

A

-

P

-

L

-

L

W

L

M

A

L

L

I

C

F

R

R

L

L

G

I

Q

Q

G

G

L

L

G

V

L

S

G

K

G

A

E

G

W

W

G

L

G

I

A

G

V

Y

L

I

L

L

A

I

T

T

E

E

N

F

A

V

P

G

E

R

G

R

K

Y

R

R

T

R

W

T

Y

V

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Y

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A

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P

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A

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G

G

F

L

I

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L

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A

L

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A

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-

A

-
x
Y

-

A

-

L

-

P

-

H

F

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R

L

W

L

L

A

Q

E

F

T

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x
S

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F

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-

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-

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A

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Y

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x
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P

F
x
E

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x
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x
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x
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-

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-

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-

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-

A

-

V

-

G

W

L

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F

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N

A

A

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A

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A

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A

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L

R

R

H

L

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E

-

E

-

T

-

G

-

K

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N

-

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Y

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-

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L

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A

A

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E

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x
Y

P

P

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T

S

F

V

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R

Y

N

T

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G

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L

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M165 (≠ A76) to I: lower Vmax for MPP(+) transport; no change in transport efficiency (Vmax/Km) and clearance of cyclo(his-pro) and salsolinol; dbSNP:rs8177507
Y169 (≠ H80) mutation to F: No change in TEA uptake.
T201 (≠ A112) to M: in dbSNP:rs145450955
Y241 (≠ P160) mutation to F: Slight decrease in TEA uptake. No change in tyrosine phosphorylation. Strong decrease in TEA uptake; when associated with F-362. Strong decrease in TEA and metformin uptake and YES1-mediated tyrosine phosphorylation; when associated with F-362 and F-377.
Y257 (vs. gap) mutation to F: No change in TEA uptake.
S270 (≠ T183) to A: decreased Ki value for TBA inhibition of MPP(+); no change in transport efficiency (Vmax/Km) and clearance of cyclo(his-pro) and salsolinol; dbSNP:rs316019
Y279 (= Y190) mutation to F: No change in TEA uptake.
Y280 (≠ G191) mutation to F: No change in TEA uptake.
P284 (= P195) mutation to A: Decreased TEA and metformin uptake. Decreased tyrosine phosphorylation.
PESPR 284:288 (≠ PFIAS 195:199) Proline-rich sequence
S286 (≠ I197) mutation to A: No change in TEA and metformin uptake. No change in tyrosine phosphorylation.
P287 (≠ A198) mutation to A: Decreased TEA and metformin uptake. Decreased tyrosine phosphorylation.
Y362 (= Y275) mutation to F: Decreased TEA uptake and YES1-mediated tyrosine phosphorylation. Strong decrease in TEA uptake; when associated with F-241. Strong decrease in TEA uptake; when associated with F-377. Strong decrease in TEA and metformin uptake and YES1-mediated tyrosine phosphorylation; when associated with F-241 and F-377.
Y377 (≠ G287) mutation to F: Slight decrease in TEA uptake. No change in tyrosine phosphorylation. Strong decrease in TEA uptake; when associated with F-362. Strong decrease in TEA and metformin uptake and YES1-mediated tyrosine phosphorylation; when associated with F-241 and F-362.
R400 (= R304) to C: lower Vmax and reduced Ki value for TBA inhibition of MPP(+); lower transport efficiency (Vmax/Km) and clearance of cyclo(his-pro); no change in transport efficiency (Vmax/Km) and clearance of salsolinol; dbSNP:rs8177516
K432 (≠ G338) to Q: lower Km value for MPP(+) and reduced Ki value for TBA inhibition of MPP; no change in transport efficiency (Vmax/Km) and clearance of cyclo(his-pro) and salsolinol; dbSNP:rs8177517
Y458 (≠ F362) mutation to F: No change in TEA uptake.

Sites not aligning to the query:

54 P → S: in dbSNP:rs8177504
73 Y→F: No change in TEA uptake.
92 Y→F: No change in TEA uptake.
128 Y→F: No change in TEA uptake.
544 Y→F: No change in TEA uptake.

8ju0A Hoct1 in complex with spironolactone in inward facing occluded conformation (see paper)
26% identity, 73% coverage: 79:389/426 of query aligns to 145:401/431 of 8ju0A

query
sites
8ju0A

G

G

H

Y

F

F

G

A

D

D

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K

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K

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W

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F

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Y

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I

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F

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-

F

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A

-

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F

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A

A

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F

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x
Q

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A

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A

A

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E

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Y

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P

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F

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R

Y

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T

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S

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P

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F

I

I

binding spironolactone: K192 (≠ G134), W195 (= W137), Q216 (= Q161), F219 (≠ A164), Y279 (= Y275), Q365 (vs. gap)

Sites not aligning to the query:

binding spironolactone: 10

P36035 Carboxylic acid transporter protein homolog from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
29% identity, 40% coverage: 66:234/426 of query aligns to 183:336/616 of P36035

query
sites
P36035

I

L

A

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F

L

F

F

A

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R

R

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S

V

A

G

G

A

A

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D

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Y

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G

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A

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A

A

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E

N

D

A

A

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P

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K

A

R

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-

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S

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F

F

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F

Q

S

L

A

G

Y

A

A

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-

A

M

G

G

F

F

I

I

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F

A

A

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G

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F

Y

L

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A

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G

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W

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F

F

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A

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A

I

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F

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P

A

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V

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L

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F

F

I

W

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R

L

L

R

L

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W

A

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E

E

T

T

P

K

E

Y

F

F

Q

T

K

K

A

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I

L

D

-

K

K

A

A

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A

A

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
9 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
338 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Query Sequence

>WP_004687208.1 NCBI__GCF_000022745.1:WP_004687208.1
MTVAEAVAPQANSVRRVLTASMIGTTIEFFDFYIYATAAVIVFPHLFFPASDGNSALLQS
FATFAIAFFARPVGAAIFGHFGDKIGRKATLVAALMTMGLSTVAIGFLPTYASIGVAAPL
LLALCRLGQGLGLGGEWGGAVLLATENAPEGKRTWYGMFPQLGAPAGFILATGIFLLLAE
TMTEEQFFAYGWRVPFIASAILVAVGLFIRLRIAETPEFQKAIDKAERVAVPAAQLFRHH
KMNLFLGTIGTMATFVLFYLMTVFSLGWGTRALGYSREEFLVLQMIGVIFFGLTIPLSAL
LSDRYGMRTIMVIVTVLIGLYGFIMAPLFAAGTAGVLGFLIIGFGLMGMTYGPIGAVLAE
PFPTSVRYTGASLAFNLAGILGASLAPYIATWLATDYGFAYVGYYMVAAAIISLIGFVFI
TLKDKK

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