SitesBLAST

54 D→A: Loss of transport activity.; D→E: Retains 50% of its transport activity.
57 D→A: Loss of transport activity.; D→E: Retains 50% of its transport activity.
317 mutation I->H,Y: Loss of transport activity.
386 R→A: Loss of transport activity.

8et8A Cryo-em structure of the organic cation transporter 1 in complex with verapamil (see paper)
24% identity, 83% coverage: 76:432/432 of query aligns to 160:520/532 of 8et8A

query
sites
8et8A

L

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E

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N

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L

binding (2S)-2-(3,4-dimethoxyphenyl)-5-{[2-(3,4-dimethoxyphenyl)ethyl](methyl)amino}-2-(propan-2-yl)pentanenitrile: K213 (≠ G137), W216 (= W140), Q240 (= Q164), W353 (≠ L260), Y360 (≠ F267), F378 (≠ T282), S381 (vs. gap), E385 (≠ C288), C449 (vs. gap), S469 (= S376)

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, 83% coverage: 76:432/432 of query aligns to 160:520/532 of 8et7A

query
sites
8et7A

L

L

G

G

S

S

A

L

L

G

F

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G

G

H

Y

F

I

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A

D

D

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G

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R

K

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binding n-[2-(benzhydryloxy)ethyl]-n,n-dimethylamine: E385 (≠ C288), F445 (vs. gap)

Sites not aligning to the query:

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

O15245 Solute carrier family 22 member 1; Organic cation transporter 1; hOCT1 from Homo sapiens (Human) (see 10 papers)
26% identity, 92% coverage: 34:432/432 of query aligns to 123:521/554 of O15245

query
sites
O15245

D

D

F

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A

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x
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G

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G

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C

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S

A

S

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C

N

D

L

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x
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W

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F

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S

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L

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L

A

A

-

A

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G

-

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V

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L

L

L160 (≠ A70) to 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
S189 (= S104) to L: no changes in MPP(+) uptake; dbSNP:rs34104736
G220 (≠ A143) to V: affects transporter activity; reduction of MPP(+) uptake when associated with V-408; dbSNP:rs36103319
Y240 (≠ P163) mutation to F: Decreased TEA uptake.
P283 (= P198) to L: in dbSNP:rs4646277; mutation to A: Decreased TEA uptake.
R287 (vs. gap) to G: in dbSNP:rs4646278
P341 (≠ T247) 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 (≠ L248) to H: no changes in MPP(+) uptake when associated with V-408; dbSNP:rs34205214
Y361 (≠ F267) mutation to F: Decreased TEA uptake.
Y376 (≠ F283) mutation to F: Decreased TEA uptake.
G401 (= G309) to S: affects transporter activity; reduction of MPP(+), serotonin and TEA uptake; no MPP(+) uptake when associated with L-160; dbSNP:rs34130495
M408 (≠ V316) 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 (= M328) 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 (= M351) to I: in dbSNP:rs35956182
V461 (= V370) to I: no changes in MPP(+) uptake when associated with V-408; dbSNP:rs34295611
G465 (= G374) 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.
R488 (≠ V398) to M: no changes in MPP(+) uptake when associated with V-408; dbSNP:rs35270274

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

Q63089 Solute carrier family 22 member 1; Organic cation transporter 1; rOCT1 from Rattus norvegicus (Rat) (see 4 papers)
24% identity, 75% coverage: 76:400/432 of query aligns to 162:491/556 of Q63089

query
sites
Q63089

L

L

G

G

S

S

A

L

L

V

F

V

G

G

H

Y

F

I

G

A

D

D

R

R

I

F

G

G

R

R

K

K

S

L

T
x
C

L

L

V

L

A

V

S

T

L

T

L

L

L

V

M

T

G

S

V

V

S

S

T

G

T

V

A

L

I

T

G

A

V

V

L

A

P

P

G

D

Y

Y

D

T

S

S

I

-

G

-

V

-

W

-

A

-

P

-

I

-

L

M

C

L

L

L

L

F

R

R

F

L

G

L

Q

Q

G

G

L
x
M

G
x
V

L
x
S

G
x
K

G
|
G

E
x
S

W
|
W

G
x
V

G
x
S

A
x
G

A
x
Y

L
x
T

L
|
L

A
x
I

T
|
T

E
|
E

N
x
F

A
x
V

P

G

E

S

G

G

K

Y

R

R

A

R

W

T

F

T

G

A

M

I

F

L

P

Y

Q

Q

L

M

G

A

P

F

S

T

I

V

G

G

F

L

L

V

A

G

A

L

N

A

G

G

L

V

-

A

-

Y

-

A

-

I

-

P

-

D

-

W

-

R

F

W

L

L

T

Q

L

L

A

A

L

V

V

S

L

L

S

P

D

T

E

F

Q

L

F

F

R

L

E

L

W

Y

G

Y

W

W

R

F

I

V

P

P

-

E

-
x
S

-

P

-

R

F

W

L

L

S
|
S

A

Q

A

K

L

R

V
x
T

L

T

V

R

G

A

L

V

Y

R

V

I

R

M

L

E

K

Q

L

I

E

A

E

Q

S

K

-

N

-

G

-

K

-

V

-

P

P

P

V

A

F

D

A

L

K

K

A

M

V

L

A
x
C

R

L

H

E

E

E

R

D

V

A

K
x
S

M

E

P

K

V

R

V

S

D

P

L

S

F

F

S

A

K

D

Y

L

W

F

L

R

P

T

T

P

L

N

L

L

G

R

A

K

A

H

A

T

M

V

V

I

V

L

C

M

Y

Y

A

L

L

W

F

F

Y

S

I
x
C

S

A

T

V

V

L

F

Y

S

Q

-

G

-

L

-

I

L

M

S

H

Y

V

G

G

V

A

T

T

T

G

L

A

G

N

Y

L

S

Y

R

L

E

D

T

F

F

F

L

Y

-

S

G

S

L

L

L

V

C

E

F

F

A

P

V

A

F

F

M

I

A

I

L

L

A

V

T

T

P

-

L

-

S

-

A

-

W

-

L

-

S

I

D

D

R

R

Y

I

G

G

R

R

K

-

P

-

V

-

L

-

I

-

V

-

G

-

L

I

L

Y

A

P

I

I

A

A

S

A

G

S

F

N

T

-

M

-

E

-

P

-

L

-

L

L

T

V

S

T

G

G

S

A

T

A

A
x
C

G

L

V

L

A

M

L

I

F

F

L

I

A

P

I

H

E

E

L

L

F

H

L

W

M

L

G

N

V

V

T

T

F

L

A

A

P
x
C

M

L

G

G

A

R

L

M

-

G

-

A

-

T

-

I

-

V

-

L

-

Q

-

M

-

V

-
x
C

-

L

-

V

L

N

P

A

E

E

L

L

F

Y

P

P

T

T

H

F

V

I

R

R

Y

N

T

L

G

G

-

M

-

V

A
x
C

S

S

A

A

A

L

Y
x
C

N
x
D

L

L

G

G

I

I

V

F

G

-

A

-

S

-

A

-

A

T

P

P

F

F

F

M

A

V

Q

F

K

R

L

L

V

M

S

E

M

V

C179 (≠ T93) mutation to A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; S-322; A-358; A-418; S-437; A-470 and A-474.
M212 (≠ L134) mutation to L: No change in TEA and MPP(+) uptake.
V213 (≠ G135) mutation to G: Decreased TEA uptake. No change in MPP(+) uptake.
S214 (≠ L136) mutation to G: Decreased TEA and MPP(+) uptake.
K215 (≠ G137) mutation to Q: Loss of TEA and MPP(+) uptake activity.; mutation to R: Loss of TEA and MPP(+) uptake activity.
G216 (= G138) mutation to A: Decreased TEA and MPP(+) uptake.
S217 (≠ E139) mutation to G: No change in TEA and MPP(+) uptake.
W218 (= W140) mutation to F: Decreased guanidine, histamine, serotonin and TEA uptake. No change in MPP(+) uptake. No change in TEA and MPP(+) affinity. Decreased TEA Vmax. No change in MPP(+) Vmax.; mutation to L: Decreased guanidine, histamine, serotonin, TEA and MPP(+) uptake. Decreased TEA affinity. No change in MPP(+) affinity. Decreased TEA and MPP(+) Vmax.; mutation to Y: Decreased guanidine, histamine, serotonin and TEA uptake. No change in MPP(+) uptake. Increased TEA and MPP(+) affinity. Decreased TEA and MPP(+) Vmax.
V219 (≠ G141) mutation to L: No change in TEA and MPP(+) uptake.
S220 (≠ G142) mutation to I: Decreased TEA and MPP(+) uptake.
G221 (≠ A143) mutation to A: Decreased TEA and MPP(+) uptake.
Y222 (≠ A144) mutation to F: No change in guanidine, histamine, serotonin, TEA and MPP(+) uptake. Increased TEA affinity. No change in MPP(+) affinity. Decreased TEA Vmax. No change in MPP(+) Vmax.; mutation to L: Decreased guanidine, serotonin, TEA and MPP(+) uptake. No change in histamine uptake. Increased TEA and MPP(+) affinity. Decreased TEA and MPP(+) Vmax.
T223 (≠ L145) mutation to I: Decreased TEA uptake. No change in MPP(+) uptake.
L224 (= L146) mutation to V: Decreased TEA and MPP(+) uptake.
I225 (≠ A147) mutation to G: No change in TEA and MPP(+) uptake.
T226 (= T148) mutation to A: Decreased TEA uptake. No change in MPP(+) uptake.
E227 (= E149) mutation to D: Loss of TEA and MPP(+) uptake activity.; mutation to Q: Loss of TEA and MPP(+) uptake activity.
F228 (≠ N150) mutation to I: No change in TEA and MPP(+) uptake.
V229 (≠ A151) mutation to A: Decreased TEA and MPP(+) uptake.; mutation to L: Loss of TEA and MPP(+) uptake activity.
S286 (vs. gap) mutation to A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-292; A-296; A-328 and A-550. No effect of PKA activation on ASP uptake. No effect of PKA activation on ASP uptake; when associated with A-292; A-296; A-328 and A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-292; A-296; A-328 and A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-292; A-296; A-328 and A-550. suppresses phosphorylation by PKC; when associated with A-292; A-296; A-328 and A-550.
S292 (= S202) mutation to A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-296; A-328 and A-550. No effect of PKA activation on ASP uptake. No effect of PKA activation on ASP uptake; when associated with A-286; A-296; A-328 and A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-296; A-328 and A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-296; A-328 and A-550. suppresses phosphorylation by PKC; when associated with A-286; A-296; A-328 and A-550.
T296 (≠ V206) mutation to A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-292; A-328; A-550. Significant increase of the ASP uptake by PKA activation. No effect of PKA activation on ASP uptake; when associated with A-286; A-292; A-328; A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-292; A-328; A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-292; A-328 and A-550. suppresses phosphorylation by PKC; when associated with A-286; A-292; A-328 and A-550.
C322 (≠ A227) mutation to S: Reduces the activation by MMTS. Abolishes the activation by MMTs; when associated with M-451. Choline affinity is increased fivefold by MMTS. Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; A-358; A-418; S-437; A-470 and A-474. Choline affinity is increased four- to fivefold; when associated with M-451.
S328 (≠ K233) mutation to A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-292; A-296 and A-550. No effect of PKA activation on ASP uptake. No effect of PKA activation on ASP uptake; when associated with A-286; A-292; A-296 and A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-292; A-296; A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-292; A-296 and A-550. suppresses phosphorylation by PKC; when associated with A-286; A-292; A-296 and A-550.
C358 (≠ I263) mutation to A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-418; S-437; A-470 and A-474.
C418 (≠ A338) mutation to A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; S-437; A-470 and A-474.
C437 (≠ P357) mutation to S: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; A-418; A-470 and A-474.
C451 (vs. gap) mutation to M: Reduces the activation by MMTS. Abolishes the activation by MMTs; when associated with S-322. Abolishes the effect of MMTs on choline-induced currents. Choline affinity is not influenced by MMTS. Choline affinity is increased four- to fivefold; when associated with S-322.
C470 (≠ A375) mutation to A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; A-418; A-437 and A-474.
C474 (≠ Y379) mutation to A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; A-418; A-437 and A-470.
D475 (≠ N380) mutation to E: Decreased MPP(+) uptake, no change in MPP(+) affinity. Decreased NMN uptake, increased NMN affinity. Decreased choline uptake, increased choline affinity.; mutation to N: Decreased MPP(+) uptake.; mutation to R: Decreased MPP(+) uptake.

Sites not aligning to the query:

26 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-155; A-179; S-322; A-358; A-418; S-437; A-470 and A-474.
155 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-179; S-322; A-358; A-418; S-437; A-470 and A-474.
550 T→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-292; A-296; A-328. Significant increase of the ASP uptake by PKA activation. No effect of PKA activation on ASP uptake; when associated with A-286; A-292; A-296 and A-328. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-292; A-296; A-328. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-292; A-296 and A-328. suppresses phosphorylation by PKC; when associated with A-286; A-292; A-296 and A-328.

8sc2A Human oct1 bound to diltiazem in inward-open conformation (see paper)
27% identity, 74% coverage: 77:397/432 of query aligns to 144:426/453 of 8sc2A

query
sites
8sc2A

G

G

S

S

A

L

L

G

F

V

G

G

H

Y

F

F

G

A

D

D

R

R

I

F

G

G

R

R

K

K

S

L

T

C

L

L

V

L

A

G

S

T

L

V

L

L

L

V

M

N

G

A

V

V

S

S

T

G

T

V

A

L

I

M

G

A

V

F

L

S

P

P

G

N

Y

Y

D

M

S

S

I

-

G

-

V

-

W

-

A

-

P

-

I

-

L

M

C

L

L

L

L

F

R

R

F

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

A

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

A

R

W

T

F

V

G

A

M

I

F

M

P

Y

Q
|
Q

L

M

G

A

P
x
F

S

T

I

V

G

G

F

L

L

V

A

A

A

L

N

T

G

G

L

L

F

A

L

Y

T

A

L

L

A

P

L

-

V

-

L

-

S

-

D

-

E

-

Q

-

F

-

R

-

E

H

W

W

G

R

W

W

-

L

R

Q

I

L

P

A

F

V

L

S

L

L

S

P

A

T

A

F

L

L

V

F

L

L

V

L

G

Y

L

Y

Y

W

V

C

R

V

L

P

K

E

L

S

E

P

E

R

S

S

P

P

V

S

F

F

A

A

K

-

A

-

V

-

A

-

R

-

H

-

E

-

R

-

V

-

K

-

M

-

P

-

V

-

D

D

L

L

F

F

S

R

K

T

Y

-

W

-

L

-

P

-

T

P

L

R

L

L

G

R

A

K

A

R

A

T

M

F

V

I

V

L

C

M

Y

Y

A

L

L
x
W

F

F

Y

T

I

D

S
|
S

T

V

V

L

F

Y

S

Q

-

G

-

L

-

I

L

L

S

H

Y

M

G

G

V

A

T

T

T

-

L

-

G

-

Y

-

S

S

R

G

E

N

T

L

F

Y

L

L

G

D

L

F

L

L

C

Y

F

S

A

A

V

L

V

V

-

E

-

I

-

P

-

G

-

A

F

F

M

I

A

A

L

L

A

I

T

T

P

-

L

-

S

-

A

-

W

-

L

-

S

I

D

D

R

R

Y

V

G

G

R

R

K

I

P

Y

V

P

L

M

I

A

V

M

G

S

G

N

L

L

A

A

I

G

A

A

S

A

G

C

F

L

T

V

M

M

E

-

P

-

L

I

L

F

T

I

S

S

G

P

S

D

T

L

A

H

G

W

V

L

A

N

L

I

F

I

L

I

A

-

I

M

E

C

L

V

F

G

L

R

M

M

G

G

V

I

T

T

F

I

A

A

P
x
I

M

Q

G

M

A

I

L

C

L

L

-

V

-

N

P

A

E

E

L

L

F

Y

P

P

T

T

H

F

V

V

R

R

Y

N

T

L

G

G

-

V

-

M

-

V

A

C

S

S

A

S

A

L

Y

C

N

D

L

I

G

G

I

I

V

I

G

-

A

-

S

-

A

-

A

T

P

P

F

F

F

I

A

V

Q

F

K

R

L

L

binding Diltiazem: W199 (= W140), Q223 (= Q164), F226 (≠ P167), W293 (≠ L260), S297 (= S264), I385 (≠ P357)

Sites not aligning to the query:

binding Diltiazem: 18

O08966 Solute carrier family 22 member 1; Organic cation transporter 1; mOCT1 from Mus musculus (Mouse) (see paper)
24% identity, 75% coverage: 76:400/432 of query aligns to 162:491/556 of O08966

query
sites
O08966

L

L

G

G

S

S

A

L

L

V

F

V

G

G

H

Y

F

I

G

A

D

D

R

R

I

F

G

G

R

R

K

K

S

L

T

C

L

L

V

L

A

V

S

T

L

T

L

L

L

V

M

T

G

S

V

L

S

S

T

G

T

V

A

L

I

T

G

A

V

V

L

A

P

P

G

D

Y

Y

D

T

S

S

I

-

G

-

V

-

W

-

A

-

P

-

I

-

L

M

C

L

L

L

L

F

R

R

F

L

G

L

Q

Q

G

G

L

M

G

V

L

S

G

K

G

G

E

S

W

W

G

V

G

S

A

G

A

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

A

R

W

T

F

T

G

A

M

I

F

L

P

Y

Q

Q

L

V

G

A

P

F

S

T

I

V

G

G

F

L

L

V

A

G

A

L

N

A

G

G

L

V

-

A

-

Y

-

A

-

I

-

P

-

D

-

W

-

R

F

W

L

L

T

Q

L

L

A

A

L

V

V

S

L

L

S

P

D

T

E

F

Q

L

F

F

R

L

E

L

W

Y

G

Y

W

W

R

F

I

V

P

P

-

E

-

S

-

P

-

R

F

W

L

L

S

S

A

Q

A

K

L

R

V

T

L

T

V

Q

G

A

L

V

Y

R

V

I

R

M

L

E

K

Q

L

I

E

A

E

Q

S

K

-

N

-

R

-

K

-

V

-

P

P

P

V

A

F

D

A

L

K

K

A

M

V

M

A

C

R

L

H

E

E

E

R

D

V

A

K

S

M

E

P

R

V

R

V

S

D

P

L

S

F

F

S

A

K

D

Y

L

W

F

L

R

P

T

T

P

L

S

L

L

G

R

A

K

A

H

A

T

M

L

V

I

V

L

C

M

Y

Y

A

L

L

W

F

F

Y

S

I

C

S

A

T

V

V

L

F

Y

S

Q

-

G

-

L

-

I

L

M

S

H

Y

V

G

G

V

A

T

T

T

G

L

A

G

N

Y

L

S

Y

R

L

E

D

T

F

F

F

L

Y

-

S

G

S

L

L

L

V

C

E

F

F

A

P

V

A

F

F

M

I

A

I

L

L

A

V

T

T

P

-

L

-

S

-

A

-

W

-

L

-

S

I

D

D

R

R

Y

I

G

G

R

R

K

I

P

Y

V

P

L

I

I

A

V

A

G

S

G

N

L

L

L

V

A

A

I

G

A

A

S

A

G

C

F

L

T

L

M

M

E

-

P

-

L

-

T

-

S

-

G

-

S

-

T

-

A

-

G

-

V

-

A

-

L

I

F

F

L

I

A

P

I

H

E

E

L

L

F

H

L

W

M

L

G

N

V

V

T

T

F

L

A

A

P

C

M

L

G

G

A

R

L

M

-

G

-

A

-

T

-

I

-

V

-

L

-

Q

-

M

-

V

-

C

-

L

-

V

L

N

P

A

E

E

L

L

F

Y

P

P

T

T

H

F

V

I

R

R

Y

N

T

L

G

G

-

M

-

V

A

C

S

S

A

A

A

L

Y

C

N

D

L

L

G

G

I

I

V

F

G

-

A

-

S

-

A

-

A

T

P

P

F

F

F

M

A

V

Q

F

K

R

L

L

V

M

S

E

M

V

Sites not aligning to the query:

32 L→F: Increased trospium uptake. Increased trospium affinity. No change in fenoterol uptake.
36 Y→C: Decreased fenoterol uptake. Decreased fenoterol affinity. No change in trospium uptake. No change in terbutaline affinity.

8et9A Cryo-em structure of the organic cation transporter 2 in complex with 1-methyl-4-phenylpyridinium (see paper)
24% identity, 83% coverage: 76:432/432 of query aligns to 160:505/517 of 8et9A

query
sites
8et9A

L

V

G

G

S

S

A

M

L

S

F

I

G

G

H

Y

F

I

G

A

D

D

R

R

I

F

G

G

R

R

K

K

S

L

T

C

L

L

V

L

A

V

S

T

L

I

L

L

L

I

M

N

G

A

V

I

S

S

T

G

T

V

A

L

I

M

G

A

V

V

L

A

P

P

G

N

Y

Y

D

-

S

-

I

-

G

-

V

T

W

W

A

-

P

-

I

-

L

M

C

L

L

I

L

F

R

R

F

L

G

I

Q

Q

G

G

L

L

G

V

L

S

G

K

G

G

E

G

W
|
W

G

L

G

I

A

G

A

Y

L

T

L

L

A

P

T

T

E

E

N

F

A

V

P

G

E

L

G

E

K

Y

R

R

A

R

W

T

F

V

G

G

M

I

F

L

P

Y

Q
|
Q

L

M

G

A

P
x
F

S

S

I

V

G

G

F

L

L

L

A

V

A

L

N

A

G

G

L

V

-

A

-

Y

-

A

-

I

-

P

-

H

-

W

-

R

F

W

L

L

T

Q

L

L

A

A

L

V

V

T

L

L

S

P

D

N

E

F

Q

F

F

F

R

L

E

L

W

Y

G

Y

W

W

R

C

I

I

P

P

-

E

-

S

-

P

-

R

F

W

L

L

L

I

S

S

A

Q

A

N

L

-

V

-

L

-

V

-

G

-

L

-

Y

-

V

-

R

-

L

-

K

K

L

N

E

A

E

K

S

A

P

M

V

K

F

I

A

I

K

K

A

H

V

I

A

A

R

K

H

K

E

N

R

G

V

K

K

K

M

L

P

P

V

K

V

S

D

E

L

K

F

L

S

N

K

P

Y

S

W

F

L

L

P

D

T

L

L

V

-

R

-

T

-

P

-

Q

L

I

G

R

A

K

A

H

A

T

M

L

V

I

V

L

C

M

Y

Y

A

N

L

W

F

F

Y

T

I

S

S

S

T

V

V

L

F

Y

S

Q

-

G

-

L

-

I

L

M

S

H

Y

M

G

G

V

I

T

A

T

G

L

G

G

N

Y

I

S

Y

R

L

E

D

T

F

F

F

L

Y

-

S

G

A

L

L

L

V

C

E

F

F

A

P

V

A

F

F

M

I

A

I

L

I

A

L

T

T

P

-

L

-

S

-

A

-

W

-

L

-

S

I

D

D

R

R

Y

I

G

G

R

R

K

R

-

Y

-

P

-

W

-

A

P

A

V

A

L

N

I

M

V

V

G

A

G

G

L

A

A

C

I

L

A

I

S

T

G

A

F

F

T

L

M

F

E

W

P

L

L

K

L

T

T

T

S

V

G

A

S

C

T

L

A

G

G

R

V

M

A

G

L

I

F

T

L

M

A

A

I
x
F

E

E

L

M

F

V

L

C

M

F

G

V

V

N

T

T

F

-

A

-

P

-

M

-

G

-

A

-

L

-

P

-

E

E

L

L

F

Y

P

P

T

T

H

F

V

I

R

R

Y

N

T

L

G

G

-

V

-

L

-

V

A

C

S

S

A

S

A

L

Y

C

N

D

L

I

G

G

I

I

V

I

G

-

A

-

S

-

A

-

A

T

P

P

F

F

F

L

A

V

Q

Y

K

R

L

L

V

A

S

S

M

I

G

-

L

-

S

-

W

W

V

L

G

E

G

L

Y

P

V

L

S

V

V

V

A

F

A

A

V

V

I

L

S

G

L

L

I

I

A

A

-

G

-

L

V

V

L

L

C

L

L

L

K

P

E

E

T

T

R

K

N

G

T

K

T

P

L

L

binding 1-methyl-4-phenylpyridin-1-ium: W216 (= W140), Q240 (= Q164), F243 (≠ P167), F430 (≠ I346)

Q9R0W2 Solute carrier family 22 member 2; Organic cation transporter 2; rOCT2 from Rattus norvegicus (Rat) (see paper)
21% identity, 75% coverage: 76:400/432 of query aligns to 162:491/555 of Q9R0W2

query
sites
Q9R0W2

L

I

G

G

S

A

A

M

L

M

F

I

G

G

H

Y

F

L

G

A

D

D

R

R

I

F

G

G

R

R

K

K

S

F

T

C

L

L

V

L

A

V

S

T

L

I

L

L

L

I

M

N

G

A

V

I

S

S

T

G

T

A

A

L

I

M

G

A

V

I

L

S

P

P

G

N

Y

Y

D

-

S

-

I

-

G

-

V

A

W

W

A

-

P

-

I

-

L

M

C

L

L

V

L

F

R

R

F

F

G

L

Q

Q

G

G

L

L

G

V

L

S

G

K

G

A

E

G

W

W

G

L

G

I

A

G

A

Y

L

I

L

L

A

I

T

T

E

E

N

F

A

V

P

G

E

L

G

G

K

Y

R

R

A

R

W

M

F

V

G

G

M

I

F

C

P

Y

Q

Q

L

I

G

A

P

F

S

T

I

V

G

G

-

L

-

I

-

L

-

A

-

G

-

V

-

A

F

Y

L

V

A

I

A

P

N

N

G

W

L

R

F

W

L

L

T

Q

L

F

A

A

L

V

V

T

L

L

S

P

D

N

E

F

Q

C

F

F

R

L

E

L

W

Y

G

F

W

W

R

C

I

I

P

P

-

E

-

S

-

P

-

R

F

W

L

L

L

I

S

S

-

Q

-

N

-

K

-

I

-

V

A

K

A

A

L

M

V

K

L

I

V

I

G

K

L

H

Y

I

V

A

R

K

L

K

K

N

L

G

E

K

E

S

S

V

P

P

V

V

F

S

A

L

K

Q

A

N

V

L

A

T

R

P

H

D

E

E

R

D

V

A

K

G

M

K

P

K

V

L

V

N

D

P

L

S

F

F

S

L

K

D

Y

L

W

V

L

R

P

T

T

P

L

Q

L

I

G

R

A

K

A

H

A

T

M

L

V

I

V

L

C

M

Y

Y

A

N

L

W

F

F

Y

T

I

S

S

S

T

V

V

L

F

Y

S

Q

-

G

-

L

-

I

L

M

S

H

Y

M

G

G

V

L

T

A

T

G

L

D

G

N

Y

I

S

Y

R

L

E

D

T

F

F

F

L

Y

G

S

-

A

L

L

L

V

C

E

F

F

A

P

V

A

F

F

M

I

A

I

L

I

A

L

T

T

P

-

L

-

S

-

A

-

W

-

L

-

S

I

D

D

R

R

Y

V

G

G

R

R

K

R

P

Y

V

P

L

W

I

A

V

V

G

S

G

N

L

M

L

V

A

A

I

-

A

-

S

-

G

-

F

-

T

-

M

-

E

-

P

-

L

-

T

-

S

-

G

G

S

A

T

A

A

C

G

L

V

A

A

S

L

V

F

F

L

I

A

P

I

D

E

D

L

L

F

Q

L

W

M

L

G

K

V

I

T

T

F

I

A

A

P

C

M

L

G

G

A

R

L

M

-

G

-

I

-

T

-

M

-

A

-

Y

-

E

-

M

-

V

-
x
C

-

L

-

V

L

N

P

A

E

E

L

L

F

Y

P

P

T

T

H

Y

V

I

R

R

Y

N

T

L

G

G

-

V

-

L

-

V

A

C

S

S

A

S

A

M

Y

C

N

D

L

I

G

G

I

I

V

I

G

-

A

-

S

-

A

-

A

T

P

P

F

F

F

L

A

V

Q

Y

K

R

L

L

V

T

S

D

M

I

C451 (vs. gap) Involved in recognition of organic cations and participates in structural changes that occur during translocation of organic cations; mutation to M: Transport activity strongly reduced.

8sc6A Human oct1 bound to thiamine in inward-open conformation (see paper)
28% identity, 74% coverage: 77:397/432 of query aligns to 144:419/447 of 8sc6A

query
sites
8sc6A

G

G

S

S

A

L

L

G

F

V

G

G

H

Y

F

F

G

A

D

D

R

R

I

F

G

G

R

R

K

K

S

L

T

C

L

L

V

L

A

G

S

T

L

V

L

L

L

V

M

N

G

A

V

V

S

S

T

G

T

V

A

L

I

M

G

A

V

F

L

S

P

P

G

N

Y

Y

D

M

S

S

I

-

G

-

V

-

W

-

A

-

P

-

I

-

L

M

C

L

L

L

L

F

R

R

F

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

A

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

A

R

W

T

F

V

G

A

M

I

F

M

P

Y

Q
|
Q

L

M

G

A

P
x
F

S

T

I

V

G

G

F

L

L

V

A

A

A

L

N

T

G

G

L

L

F

A

L

Y

T

A

L

L

A

P

L

-

V

-

L

-

S

-

D

-

E

-

Q

-

F

-

R

-

E

H

W

W

G

R

W

W

R

-

I

L

P

Q

F

L

L

A

L

V

S

S

A

L

A

P

L

T

V

F

L

L

V

F

G

L

L

L

Y

Y

V

Y

R

-

L

-

K

-

L

-

E

-

E

W

S

S

P

P

V

S

F

F

A

A

K

-

A

-

V

-

A

-

R

-

H

-

E

-

R

-

V

-

K

-

M

-

P

-

V

-

D

D

L

L

F

F

S

R

K

T

Y

-

W

-

L

-

P

-

T

P

L

R

L

L

G

R

A

K

A

R

A

T

M

F

V

I

V

L

C

M

Y

Y

A

L

L

W

F

F

Y

T

I

D

S

S

T

V

V

L

F
x
Y

S
x
Q

-

G

-

L

-

I

L

L

S

H

Y

M

G

G

V

A

T

T

T

-

L

-

G

-

Y

-

S

S

R

G

E

N

T

L

F

Y

L

L

G

D

L

F

L

L

C

Y

F

S

A

A

V

L

V

V

-
x
E

-

I

-

P

-

G

-

A

F

F

M

I

A

A

L

L

A

I

T

T

P

-

L

-

S

-

A

-

W

-

L

-

S

I

D

D

R

R

Y

V

G

G

R

R

K

I

P

Y

V

P

L

M

I

A

V

M

G

S

G

N

L

L

A

A

I

G

A

A

S

A

G

C

F

L

T

V

M

M

E

-

P

-

L

I

L

F

T

I

S

S

G

P

S

D

T

L

A

H

G

W

V

L

A

N

L

I

F

I

L

I

A

-

I

M

E

C

L

V

F

G

L

R

M

M

G

G

V

I

T

T

F

I

A

A

P
x
I

M
x
Q

G

M

A

I

L

C

L

L

-

V

-

N

P

A

E

E

L

L

F

Y

P

P

T

T

H

F

V

V

R

R

Y

N

T

L

G

G

-

V

-

M

-

V

A

C

S

S

A

S

A

L

Y

C

N

D

L

I

G

G

I

I

V

I

G

-

A

-

S

-

A

-

A

T

P

P

F

F

F

I

A

V

Q

F

K

R

L

L

binding 3-(4-amino-2-methyl-pyrimidin-5-ylmethyl)-5-(2-hydroxy-ethyl)-4-methyl-thiazol-3-ium: Q223 (= Q164), F226 (≠ P167), Y293 (≠ F267), Q294 (≠ S268), E318 (vs. gap), I378 (≠ P357), Q379 (≠ M358)

8sc3A Human oct1 bound to fenoterol in inward-open conformation (see paper)
33% identity, 23% coverage: 77:177/432 of query aligns to 144:236/445 of 8sc3A

query
sites
8sc3A

G

G

S

S

A

L

L

G

F

V

G

G

H

Y

F

F

G

A

D

D

R

R

I

F

G

G

R

R

K

K

S

L

T

C

L

L

V

L

A

G

S

T

L

V

L

L

L

V

M

N

G

A

V

V

S

S

T

G

T

V

A

L

I

M

G

A

V

F

L

S

P

P

G

N

Y

Y

D

M

S

S

I

-

G

-

V

-

W

-

A

-

P

-

I

-

L

M

C

L

L

L

L

F

R

R

F

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

A

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

A

R

W

T

F

V

G

A

M

I

F

M

P

Y

Q
|
Q

L

M

G

A

P
x
F

S

T

I

V

G

G

F

L

L

V

A

A

A

L

N

T

G

G

L

L

binding Fenoterol: W199 (= W140), M200 (≠ G141), Q223 (= Q164), F226 (≠ P167)

Sites not aligning to the query:

binding Fenoterol: 284, 291, 376, 380

P36035 Carboxylic acid transporter protein homolog from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
25% identity, 37% coverage: 68:226/432 of query aligns to 182:326/616 of P36035

query
sites
P36035

G

G

I

L

A

V

F

L

L

F

A

V

R

R

P

S

L

A

G

G

S

A

A

V

L

I

F

F

G

G

H

L

F

W

G

T

D

D

R

K

I

S

G

S

R

R

K

K

S

W

T

P

L

Y

V

I

A

T

S

C

L

L

L

F

L

L

M

F

G

V

V

I

S

A

T

Q

T

L

A

C

I

T

G

P

V

W

L

C

P

D

G

T

Y

Y

D

E

S

K

-

F

I

L

G

G

V

V

W

-

A

-

P

-

I

-

L

-

C

-

L

-

R

R

F

W

G

I

Q

T

G

G

L

I

G

A

L

M

G

G

E

I

W

Y

G

G

G

C

A

A

A

S

L

A

L

T

A

A

T

I

E

E

N

D

A

A

P

P

E

V

G

K

K

A

R

R

A

S

W

F

F

L

G

S

M

G

F

L

P

F

Q

F

L

S

G

A

P

Y

S

A

I

M

G

G

F

F

L

I

A

F

A

A

N

I

G

I

L

F

F

Y

L

R

T

A

L

F

A

G

L

Y

V

-

L

-

S

-

D

-

E

-

Q

-

F

F

R

R

E

D

W

D

G

G

W

W

R

K

I

I

P

L

F

F

L

W

L

F

S

S

A

I

A

F

L

L

V

P

L

I

V

L

G

L

L

I

Y

F

V

W

R

R

L

L

K

L

L

W

E

P

E

E

S

T

P

K

V

Y

F

F

A

T

K

K

A

V

V

L

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

>PP_1458 FitnessBrowser__Putida:PP_1458
MTSSTYAQAPAAPVNSPARVATASFIGTAIEFYDFYVYATAAALVIGPVFFPSGSGTAQM
LAAFLTFGIAFLARPLGSALFGHFGDRIGRKSTLVASLLLMGVSTTAIGVLPGYDSIGVW
APIILCLLRFGQGLGLGGEWGGAALLATENAPEGKRAWFGMFPQLGPSIGFLAANGLFLT
LALVLSDEQFREWGWRIPFLLSAALVLVGLYVRLKLEESPVFAKAVARHERVKMPVVDLF
SKYWLPTLLGAAAMVVCYALFYISTVFSLSYGVTTLGYSRETFLGLLCFAVVFMALATPL
SAWLSDRYGRKPVLIVGGLLAIASGFTMEPLLTSGSTAGVALFLAIELFLMGVTFAPMGA
LLPELFPTHVRYTGASAAYNLGGIVGASAAPFFAQKLVSMGGLSWVGGYVSVAAVISLIA
VLCLKETRNTTL

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