SitesBLAST

K3849 (= K52) mutation to M: Does not affect intracellular vesicle localization. Affects cholesterol internalization.
T3999 (≠ S197) mutation to A: Does not affect protein expression. Affects intracellular vesicles localization. Impairs intracellular cholesterol accumulation in the vesicle.

Sites not aligning to the query:

3577 H→P: Does not affect protein expression. Decreases intracellular cholesterol accumulation in the vesicle.
4735 K→M: Does not affect intracellular vesicle localization.Affects cholesterol internalization.
4818 R→C: Does not affect protein expression. Decreases intracellular cholesterol accumulation in the vesicle.

P55339 ABC-type transporter ATP-binding protein EcsA from Bacillus subtilis (strain 168) (see paper)
29% identity, 70% coverage: 29:230/287 of query aligns to 19:224/247 of P55339

query
sites
P55339

L

L

K

K

D

N

L

V

S

S

L

F

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T

L

L

S

E

A

P

G

N

M

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G

L

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I

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G

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N

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A

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K

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M

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E

Q

G164 (≠ S169) mutation to E: In ecsA-26; exoamylase and other exoenzymes decrease, competence- and sporulation-deficient phenotype.

7o12B Abc transporter nosdfy, amppnp-bound in gdn (see paper)
34% identity, 71% coverage: 29:233/287 of query aligns to 18:220/298 of 7o12B

query
sites
7o12B

L

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N
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N

G
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G

A

A

G
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G

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K

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x
T

T
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T

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binding phosphoaminophosphonic acid-adenylate ester: N37 (= N48), G38 (= G49), G40 (= G51), K41 (= K52), T42 (≠ S53), T43 (= T54), E80 (≠ Q93)
binding magnesium ion: T42 (≠ S53), E80 (≠ Q93)

Sites not aligning to the query:

binding phosphoaminophosphonic acid-adenylate ester: 12, 17

7o17B Abc transporter nosdfy e154q, atp-bound in lipid nanodisc (see paper)
33% identity, 71% coverage: 29:233/287 of query aligns to 18:220/298 of 7o17B

query
sites
7o17B

L

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H

N
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N

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G

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A

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G

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K

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x
T

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T

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M

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L

binding adenosine-5'-triphosphate: N37 (= N48), G38 (= G49), A39 (= A50), G40 (= G51), K41 (= K52), T42 (≠ S53), T43 (= T54), E80 (≠ Q93), R123 (≠ Q135), T127 (≠ R139), S129 (= S141), K130 (≠ V142), G131 (= G143), M132 (≠ Q144)
binding magnesium ion: K41 (= K52), T42 (≠ S53)

Sites not aligning to the query:

binding adenosine-5'-triphosphate: 12, 17

Q9BZC7 ATP-binding cassette sub-family A member 2; ATP-binding cassette transporter 2; ATP-binding cassette 2; EC 7.6.2.- from Homo sapiens (Human) (see paper)
30% identity, 75% coverage: 4:218/287 of query aligns to 985:1199/2435 of Q9BZC7

query
sites
Q9BZC7

E

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L

Sites not aligning to the query:

271 modified: N5-methylglutamine; Q→R: Abolishes methylation by N6AMT1.

P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
28% identity, 74% coverage: 8:219/287 of query aligns to 1:220/343 of P30750

query
sites
P30750

I

M

L

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x
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E

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I

40:46 (vs. 48:54, 86% identical) binding ATP
E166 (= E165) mutation to Q: Exhibits little ATPase activity.

Sites not aligning to the query:

278:283 binding L-methionine
295 N→A: Reduces the binding of L-methionine to undetectable levels.
295:296 binding L-methionine

8wdbD Cryo-em structure of the atp-bound dppabcd complex
30% identity, 74% coverage: 8:219/287 of query aligns to 258:488/513 of 8wdbD

query
sites
8wdbD

I

I

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L

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N

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G

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A

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x
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G
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S
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T
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T

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M

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F

Y

G

S

Y

S

-

L

-

D

E

P

G

M

F

Y

T

S

V

V

E

F

R

R

A

A

L

I

D

E

L

E

H

P

R

L

S

R

F

V

Y

H

P

H

H

V

W

G

D

D

M

R

Q

R

L

Q

E

R

Q

Q

-

R

-

A

-

V

-

R

-

E

-

L

-

V

D

D

W

Q

L

V

A

A

R

L

F

P

E

S

L

S

D

I

V

L

T

G

Q
x
R

Q

R

V

P

Q

R

R
x
E

L

L

S
|
S

V
x
G

G
|
G

Q

Q

R

R

Q

Q

S

R

L

V

A

A

L

I

I

A

M

R

A

A

M

L

A

A

Y

L

R

R

P

P

E

E

L

V

L

L

I

V

L

C

D

D

E

Q

P

A

V

V

A

S

S

A

L

L

D

D

P

V

I

L

V

V

R

Q

R

A

K

Q

F

I

M

L

V

D

D

L

L

L

F

A

D

D

L

L

A

Q

L

A

E

D

S

L

G

G

S

L

A

T

V

Y

L

L

F

F

S

I

S

S

H

H

I

D

T

L

S

A

D

V

L

I

E

R

R

Q

V

I

A

A

S

D

H

D

V

V

A

L

L

V

I

M

K

R

Q

A

G

G

E

R

L

V

V

V

binding adenosine-5'-triphosphate: Y268 (≠ F18), S303 (≠ N48), G306 (= G51), K307 (= K52), S308 (= S53), T309 (= T54), Q353 (= Q93), R404 (≠ Q135), E408 (≠ R139), S410 (= S141), G411 (≠ V142), G412 (= G143)
binding magnesium ion: S308 (= S53), Q353 (= Q93)

Sites not aligning to the query:

binding adenosine-5'-triphosphate: 13, 39, 40, 42, 43, 44, 45, 148, 150, 152, 207
binding magnesium ion: 44, 93

8xfcD Cryo-em structure of the atp-bound mtb dppabcd with the d445a mutation of dppa
30% identity, 74% coverage: 8:219/287 of query aligns to 259:489/517 of 8xfcD

query
sites
8xfcD

I

I

L

L

E

V

F

V

S

S

K

E

V

L

N

T

K

K

V

I

F
x
Y

R

R

G

E

K

S

N

R

G

G

-

A

-

P

-

W

-

R

V

V

E

E

K

S

Q

R

A

A

L

V

K

D

D

G

L

V

S

S

L

F

R

R

L

L

S

P

A

R

G

A

M

S

V

T

V

L

G

A

L

I

L

V

G

G

Q

E

N

S

G
|
G

A

S

G
|
G

K
|
K

S
|
S

T

T

L

L

M

A

R

R

C

M

A

V

L

L

G

G

I

L

L

L

S

Q

P

P

D

T

S

S

G

G

D

T

I

V

-

V

-

F

-

D

-

G

-

T

R

Y

T

D

L

V

G

G

E

A

T

L

P

A

E

R

Q

D

L

Q

S

V

S

L

A

A

A

F

K

R

E

R

R

R

L

V

G

Q

Y

P

V

V

P

F

Q

Q

Q

N

P

P

F

Y

G

S

Y

S

-

L

-

D

E

P

G

M

F

Y

T

S

V

V

E

F

R

R

A

A

L

I

D

E

L

E

H

P

R

L

S

R

F

V

Y

H

P

H

H

V

W

G

D

D

M

R

Q

R

L

Q

E

R

Q

Q

-

R

-

A

-

V

-

R

-

E

-

L

-

V

D

D

W

Q

L

V

A

A

R

L

F

P

E

S

L

S

D

I

V

L

T

G

Q

R

V

P

Q

R

R

E

L

L

S

S

V

G

G

G

Q

Q

R

R

Q

Q

S

R

L

V

A

A

L

I

I

A

M

R

A

A

M

L

A

A

Y

L

R

R

P

P

E

E

L

V

L

L

I

V

L

C

D

D

E

Q

P

A

V

V

A

S

S

A

L

L

D

D

P

V

I

L

V

V

R

Q

R

A

K

Q

F

I

M

L

V

D

D

L

L

L

F

A

D

D

L

L

A

Q

L

A

E

D

S

L

G

G

S

L

A

T

V

Y

L

L

F

F

S

I

S

S

H

H

I

D

T

L

S

A

D

V

L

I

E

R

R

Q

V

I

A

A

S

D

H

D

V

V

A

L

L

V

I

M

K

R

Q

A

G

G

E

R

L

V

V

V

binding adenosine-5'-triphosphate: Y269 (≠ F18), G305 (= G49), G307 (= G51), K308 (= K52), S309 (= S53)

Sites not aligning to the query:

binding adenosine-5'-triphosphate: 14, 41, 42, 43, 44, 45, 46, 175

3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
28% identity, 74% coverage: 8:219/287 of query aligns to 2:221/344 of 3tuzC

query
sites
3tuzC

I

M

L

I

E

K

F

L

S

S

K

N

V

I

N

T

K

K

V

V

F
|
F

-

H

R
x
Q

G

G

K

T

N

R

G

T

V

I

E

-

K

-

Q

Q

A

A

L

L

K

N

D

N

L

V

S

S

L

L

R

H

L

V

S

P

A

A

G

G

M

Q

V

I

V

Y

G

G

L

V

L

I

G

G

Q

A

N

S

G
|
G

A

A

G
|
G

K
|
K

S
|
S

T
|
T

L

L

M

I

R

R

C

C

A

V

L

N

G

L

I

L

L

E

S

R

P

P

D

T

S

E

G

G

D

S

I

V

R

L

T

V

L

D

G

G

E

Q

T

E

P

L

E

T

Q

T

L

L

S

S

-

E

-

S

-

E

-

L

S

T

A

K

A

A

K

R

E

R

R

Q

L

I

G

G

Y

M

V

I

P

-

Q

-

P

-

F

-

G

-

Y

F

E

Q

G

H

F

F

T

N

V

L

E

L

R

S

A

S

L

-

D

-

L

-

H

-

R

R

S

T

F

V

Y

F

P

G

H

N

W

V

D

A

M

L

Q

P

L

L

E

E

Q

L

D

D

W

N

L

T

A

P

R

K

F

D

E

E

L

V

D

K

-

R

V

V

T

T

Q

E

Q

L

V

L

Q

S

-

L

-

V

-

G

-

L

-

G

-

D

-

K

-

H

-

D

-

S

-

Y

-

P

-

S

R

N

L

L

S

S

V

G

G

G

Q

Q

R

K

Q

Q

S

R

L

V

A

A

L

I

I

A

M

R

A

A

M

L

A

A

Y

S

R

N

P

P

E

K

L

V

L

L

I

L

L

C

D

D

E

Q

P

A

V

T

A

S

S

A

L

L

D

D

P

P

I

A

V

T

R

T

R

R

K

S

F

I

M

L

V

E

D

L

L

L

F

K

D

D

L

I

A

N

L

R

E

R

S

L

G

G

S

L

A

T

V

I

L

L

F

L

S

I

S

T

H

H

I

E

T

M

S

D

D

V

L

V

E

K

R

R

V

I

A

C

S

D

H

C

V

V

A

A

L

V

I

I

K

S

Q

N

G

G

E

E

L

L

V

I

binding adenosine-5'-diphosphate: F12 (= F18), Q14 (≠ R19), G42 (= G49), G44 (= G51), K45 (= K52), S46 (= S53), T47 (= T54)

Sites not aligning to the query:

binding selenomethionine: 274, 279, 281, 282, 283, 284, 311, 313

3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
28% identity, 74% coverage: 8:219/287 of query aligns to 2:221/344 of 3tuiC

query
sites
3tuiC

I

M

L

I

E

K

F

L

S

S

K

N

V

I

N

T

K

K

V

V

F
|
F

-

H

R

Q

G

G

K

T

N

R

G

T

V

I

E

-

K

-

Q

Q

A

A

L

L

K

N

D

N

L

V

S

S

L

L

R

H

L

V

S

P

A

A

G

G

M

Q

V

I

V

Y

G

G

L

V

L

I

G

G

Q

A

N

S

G
|
G

A
|
A

G
|
G

K
|
K

S
|
S

T
|
T

L

L

M

I

R

R

C

C

A

V

L

N

G

L

I

L

L

E

S

R

P

P

D

T

S

E

G

G

D

S

I

V

R

L

T

V

L

D

G

G

E

Q

T

E

P

L

E

T

Q

T

L

L

S

S

-

E

-

S

-

E

-

L

S

T

A

K

A

A

K

R

E

R

R

Q

L

I

G

G

Y

M

V

I

P

-

Q

-

P

-

F

-

G

-

Y

F

E

Q

G

H

F

F

T

N

V

L

E

L

R

S

A

S

L

-

D

-

L

-

H

-

R

R

S

T

F

V

Y

F

P

G

H

N

W

V

D

A

M

L

Q

P

L

L

E

E

Q

L

D

D

W

N

L

T

A

P

R

K

F

D

E

E

L

V

D

K

-

R

V

V

T

T

Q

E

Q

L

V

L

Q

S

-

L

-

V

-

G

-

L

-

G

-

D

-

K

-

H

-

D

-

S

-

Y

-

P

-

S

R

N

L

L

S

S

V

G

G

G

Q

Q

R

K

Q

Q

S

R

L

V

A

A

L

I

I

A

M

R

A

A

M

L

A

A

Y

S

R

N

P

P

E

K

L

V

L

L

I

L

L

C

D

D

E

Q

P

A

V

T

A

S

S

A

L

L

D

D

P

P

I

A

V

T

R

T

R

R

K

S

F

I

M

L

V

E

D

L

L

L

F

K

D

D

L

I

A

N

L

R

E

R

S

L

G

G

S

L

A

T

V

I

L

L

F

L

S

I

S

T

H

H

I

E

T

M

S

D

D

V

L

V

E

K

R

R

V

I

A

C

S

D

H

C

V

V

A

A

L

V

I

I

K

S

Q

N

G

G

E

E

L

L

V

I

binding adenosine-5'-diphosphate: F12 (= F18), G42 (= G49), A43 (= A50), G44 (= G51), K45 (= K52), S46 (= S53), T47 (= T54)

6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
28% identity, 74% coverage: 8:219/287 of query aligns to 2:221/344 of 6cvlD

query
sites
6cvlD

I

M

L

I

E

K

F

L

S

S

K

N

V

I

N

T

K

K

V

V

F
|
F

-

H

R
x
Q

G

G

K

T

N

R

G

T

V
x
I

E

-

K

-

Q

Q

A

A

L

L

K

N

D

N

L

V

S

S

L

L

R

H

L

V

S

P

A

A

G

G

M

Q

V

I

V

Y

G

G

L

V

L

I

G

G

Q

A

N
x
S

G
|
G

A
|
A

G
|
G

K
|
K

S
|
S

T
|
T

L

L

M

I

R

R

C

C

A

V

L

N

G

L

I

L

L

E

S

R

P

P

D

T

S

E

G

G

D

S

I

V

R

L

T

V

L

D

G

G

E

Q

T

E

P

L

E

T

Q

T

L

L

S

S

-

E

-

S

-

E

-

L

S

T

A

K

A

A

K

R

E

R

R

Q

L

I

G

G

Y

M

V

I

P

-

Q

-

P

-

F

-

G

-

Y

F

E

Q

G

H

F

F

T

N

V

L

E

L

R

S

A

S

L

-

D

-

L

-

H

-

R

R

S

T

F

V

Y

F

P

G

H

N

W

V

D

A

M

L

Q

P

L

L

E

E

Q

L

D

D

W

N

L

T

A

P

R

K

F

D

E

E

L

V

D

K

-

R

V

V

T

T

Q

E

Q

L

V

L

Q

S

-

L

-

V

-

G

-

L

-

G

-

D

-

K

-

H

-

D

-

S

-

Y

-

P

-

S

R
x
N

L

L

S
|
S

V

G

G

G

Q
|
Q

R

K

Q

Q

S

R

L

V

A

A

L

I

I

A

M

R

A

A

M

L

A

A

Y

S

R

N

P

P

E

K

L

V

L

L

I

L

L

C

D

D

E

Q

P

A

V

T

A

S

S

A

L

L

D

D

P

P

I

A

V

T

R

T

R

R

K

S

F

I

M

L

V

E

D

L

L

L

F

K

D

D

L

I

A

N

L

R

E

R

S

L

G

G

S

L

A

T

V

I

L

L

F

L

S

I

S

T

H
|
H

I

E

T

M

S

D

D

V

L

V

E

K

R

R

V

I

A

C

S

D

H

C

V

V

A

A

L

V

I

I

K

S

Q

N

G

G

E

E

L

L

V

I

binding phosphothiophosphoric acid-adenylate ester: F12 (= F18), Q14 (≠ R19), I19 (≠ V24), S41 (≠ N48), G42 (= G49), A43 (= A50), G44 (= G51), K45 (= K52), S46 (= S53), T47 (= T54), N141 (≠ R139), S143 (= S141), Q146 (= Q144), H200 (= H198)

P41233 Phospholipid-transporting ATPase ABCA1; ATP-binding cassette sub-family A member 1; ATP-binding cassette transporter 1; ABC-1; ATP-binding cassette 1; EC 7.6.2.1 from Mus musculus (Mouse) (see paper)
30% identity, 71% coverage: 16:220/287 of query aligns to 906:1111/2261 of P41233

query
sites
P41233

K

K

V

V

F

Y

R

R

G

-

K

-

N

D

G

G

V

M

E

-

K

K

Q

V

A

A

L

V

K

D

D

G

L

L

S

A

L

L

R

N

L

F

S

Y

A

E

G

G

M

Q

V

I

V

T

G

S

L

F

L

L

G

G

Q

H

N

N

G

G

A

A

G

G

K

K

S

T

T

T

L

T

M

M

R

S

C

I

A

L

L

T

G

G

I

L

L

F

S

P

P

P

D

T

S

S

G

G

D

T

I

A

R

Y

T

I

L

L

G

G

E

K

T

D

P

I

E

R

Q

S

L

E

S

M

S

S

A

S

A

I

K

R

E

Q

R

N

L

L

G

G

Y

V

V

C

P

P

Q

Q

Q

H

P

N

F

V

G

L

Y

F

E

D

G

M

F

L

T

T

V

V

E

E

R

E

A

-

L

-

D

-

L

-

H

H

R

I

S

W

F

F

Y

Y

P

A

-

R

-

L

-

K

-

G

-

L

-

S

-

E

-

K

H

H

W

V

D

K

M

A

Q

E

L

M

E

E

Q

Q

D

-

W

-

L

-

A

-

R

-

F

M

E

A

L

L

D

D

V

V

-

G

-

L

-

P

-

S

-

K

-

L

T

K

Q

S

Q

K

V

T

Q

S

R

Q

L

L

S

S

V

G

G

G

Q

M

R

Q

Q

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Sites not aligning to the query:

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

O95477 Phospholipid-transporting ATPase ABCA1; ATP-binding cassette sub-family A member 1; ATP-binding cassette transporter 1; ABC-1; ATP-binding cassette 1; Cholesterol efflux regulatory protein; EC 7.6.2.1 from Homo sapiens (Human) (see 35 papers)
30% identity, 71% coverage: 16:220/287 of query aligns to 906:1111/2261 of O95477

query
sites
O95477

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D917 (≠ K30) to Y: in a colorectal cancer sample; somatic mutation
T929 (≠ V42) to I: in TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; loss protein subcellular localization to the plasma membrane; dbSNP:rs1832457117
N935 (= N48) to S: in TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; dbSNP:rs28937313
K939 (= K52) mutation to M: Inhibits ATPase activity; when associated with M-1952. Decreases translocase activity; when associated with M-1952. Does not affect protein subcellular localization in plasma membrane and endosome; when associated with M-1952.
S1042 (≠ A149) modified: Phosphoserine; by PKA
P1065 (= P172) natural variant: P -> S
M1091 (≠ T200) to T: in FHA1; loss of localization to plasma membrane; decreased cholesterol efflux; decreased phospholipid efflux
C1110 (≠ V219) modified: S-palmitoyl cysteine; mutation to S: Decreased palmitoylation; when associated with S-3, S-23 and S-1111.
C1111 (≠ L220) modified: S-palmitoyl cysteine; mutation to S: Decreased palmitoylation; when associated with S-3, S-23 and S-1110.

Sites not aligning to the query:

3 modified: S-palmitoyl cysteine; C→S: Mild decrease of palmitoylation. Loss of localization to plasma membrane. Decreased cholesterol efflux. Decreased phospholipid efflux. Decreased palmitoylation; when associated with S-23, S-1110 and S-1111.
23 modified: S-palmitoyl cysteine; C→S: Mild decrease of palmitoylation. Loss of localization to plasma membrane. Decreased palmitoylation; when associated with S-3, S-1110 and S-1111.
74 I→C: 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with C-371.; I→K: 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with E-371.
75 modified: Disulfide link with 309
85 P → L: in FHA1; Alabama; dbSNP:rs145183203
98 modified: carbohydrate, N-linked (GlcNAc...) asparagine
100 S→C: Highly decreased protein abundance. Highly decreased ATPase activity. Highly decreased phospholipid translocase activity.
210 E → D: in a colorectal cancer sample; somatic mutation
219 R → K: in dbSNP:rs2230806
230 R → C: in dbSNP:rs9282541
244 modified: carbohydrate, N-linked (GlcNAc...) asparagine
248 P → A: in dbSNP:rs142625938
255 A → T: in TGD; deficient cellular cholesterol efflux; dbSNP:rs758100110
304 V→C: No effect on phospholipid and cholesterol efflux or localization to cell membrane; when associated with C-308.
308 V→C: No effect on phospholipid and cholesterol efflux or localization to cell membrane; when associated with C-304.
309 modified: Disulfide link with 75
364 S → C: in dbSNP:rs775035559
371 I→C: No effect on phospholipid and cholesterol efflux or localization to cell membrane. 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with C-74 or C-375.; I→E: 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-74.
375 L→C: 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with C-371.
399 V → A: in dbSNP:rs9282543
401 K → Q: in dbSNP:rs138487227
496 R → W: in dbSNP:rs147675550
568 K→A: 60-65% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane.
573 Y→F: No effect on phospholipid and cholesterol efflux and on localization to cell membrane.
581 D→K: 80-85% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-584 and K-585.
583 F→K: 90-95% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with E-590.
584 E→K: 80-85% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-581 and K-585.
585 D→K: 80-85% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-581 and K-584.
590 W → S: in TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; dbSNP:rs137854496; W→E: 90-95% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-583.
593 F→L: Moderately decreased protein abundance. Highly decreased ATPase activity. Highly decreased phospholipid translocase activity.
638 R → Q: in dbSNP:rs374190304
771 V → M: in dbSNP:rs2066718
774 T → P: in dbSNP:rs35819696; natural variant: T -> S
776 K → N: in dbSNP:rs138880920
815 E → G: in dbSNP:rs145582736
825 V → I: in dbSNP:rs2066715
883 I → M: in dbSNP:rs2066714
1172 E → D: in dbSNP:rs33918808
1181 S → F: in dbSNP:rs76881554
1216 G → V: in dbSNP:rs562403512
1341 R → T: in dbSNP:rs147743782
1376 S → G: in dbSNP:rs145689805
1379 L → F: in TGD; the mutant protein is retained in the endoplasmic reticulum while the wild-type protein is located at the plasma membrane; dbSNP:rs1831213945
1407 A → T: in a colorectal cancer sample; somatic mutation; dbSNP:rs189206655
1463 modified: Disulfide link with 1477
1477 modified: Disulfide link with 1463; C → R: in TGD; loss of interaction with APOE; unable to generate APOE-containing high density lipoproteins; moderately decreased protein abundance; moderately decreased ATPase activity; moderately decreased phospholipid translocase activity; dbSNP:rs137854494
1512 T→M: Moderately decreased protein abundance. Does not affect ATPase activity. Moderately decreased phospholipid translocase activity.
1555 I → T: in dbSNP:rs1997618
1587 K → R: in dbSNP:rs2230808
1611 N → D: in FHA1; deficient cellular cholesterol efflux
1615 R → Q: in dbSNP:rs1251839800
1648 L → P: in dbSNP:rs1883024
1670 A → T: in dbSNP:rs1203589782
1680 R → Q: in dbSNP:rs150125857
1704 V → D: in TGD; the mutant protein is retained in the endoplasmic reticulum while the wild-type protein is located at the plasma membrane
1731 S → C: in dbSNP:rs760507032
1897 R → W: in FHA1; uncertain significance; dbSNP:rs760768125
1925 R → Q: in Scott syndrome; shows impaired trafficking of the mutant protein to the plasma membrane; dbSNP:rs142688906
1952 K→M: Inhibits ATPase activity; when associated with M-939. Decreases translocase activity; when associated with M-939. Does not affect protein subcellular localization in plasma membrane and endosome; when associated with M-939.
2054 modified: Phosphoserine; by PKA
2081 R → W: in TGD; highly decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; loss protein subcellular localization to the plasma membrane; dbSNP:rs137854501
2109 A → T: in a colorectal cancer sample; somatic mutation
2150 P → L: in FHA1; moderately decreased protein abundance; does not affect ATPase activity; moderately decreased phospholipid translocase activity; dbSNP:rs369098049
2163 natural variant: F -> S
2168 L → P: in dbSNP:rs2853577
2243 D → E: in dbSNP:rs34879708
2244 V → I: in dbSNP:rs144588452

7tbwA The structure of atp-bound abca1 (see paper)
29% identity, 71% coverage: 16:220/287 of query aligns to 761:966/1928 of 7tbwA

query
sites
7tbwA

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binding adenosine-5'-triphosphate: Y763 (≠ F18), D765 (≠ N22), K768 (= K26), N790 (= N48), G791 (= G49), G793 (= G51), K794 (= K52), T795 (≠ S53), Q835 (= Q93), Q887 (≠ R139), S889 (= S141), H944 (= H198)
binding magnesium ion: Q835 (= Q93), D912 (= D164), Q913 (≠ E165)

Sites not aligning to the query:

binding adenosine-5'-triphosphate: 1630, 1633, 1657, 1658, 1660, 1661, 1662, 1663, 1702, 1753, 1755, 1756, 1757, 1779, 1783, 1811
binding cholesterol: 218, 219, 360, 367
binding magnesium ion: 1662, 1702

Q8R420 Phospholipid-transporting ATPase ABCA3; ATP-binding cassette sub-family A member 3; Xenobiotic-transporting ATPase ABCA3; EC 7.6.2.1; EC 7.6.2.2 from Mus musculus (Mouse) (see paper)
28% identity, 73% coverage: 9:218/287 of query aligns to 530:741/1704 of Q8R420

query
sites
Q8R420

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Sites not aligning to the query:

292 E→V: Knockin new born mice are healthy and survive into adulthood without overt signs of respiratory distress. Knockin mice show a severe lung phenotype that begins with alveolar inflammatory cell infiltration at the early stage of the mouse life followed by aberrant lung remodeling with characteristics of diffuse parenchymal lung disease (DPLD)- and emphysema-like alveolar disruption in older mice.

7roqA Alternative structure of human abca1
30% identity, 69% coverage: 21:219/287 of query aligns to 776:980/1831 of 7roqA

query
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7roqA

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D

E

E

P

P

V

T

A

A

S

G

L

V

D

D

P

P

I

Y

V

S

R

R

K

G

F

I

M

W

V

E

D

L

L

L

F

-

D

-

L

L

A

K

L

Y

E

R

S

Q

G

G

S

R

A

T

V

I

L

I

F

L

S

S

S

T

H

H

I

H

T

M

S

D

D

E

L

A

E

D

R

V

V

L

A

G

S

D

H

R

V

I

A

A

L

I

I

I

K

S

Q

H

G

G

E

K

L

L

V

C

Sites not aligning to the query:

binding cholesterol: 688, 1106, 1426, 1526, 1527

Q5M243 Energy-coupling factor transporter ATP-binding protein EcfA1; ECF transporter A component EcfA1; EC 7.-.-.- from Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311) (see paper)
32% identity, 71% coverage: 15:218/287 of query aligns to 6:215/276 of Q5M243

query
sites
Q5M243

N

N

K

L

V

K

F

F

R

K

G

Y

K

N

N

Q

G

D

V

Q

E

T

K

S

Q

Y

A

T

L

L

K

N

D

D

L

V

S

S

L

F

R

H

L

V

S

K

A

H

G

G

M

E

V

W

V

L

G

S

L

I

L

V

G

G

Q

H

N

N

G

G

A

S

G

G

K

K

S

S

T

T

L

T

M

A

R

R

C

L

A

I

L

G

G

G

I

L

L

L

S

V

P

A

D

D

S

S

G

G

D

Q

I

I

R

I

T

V

L

D

G

G

-

Q

E

E

T

L

P

T

E

E

Q

E

L

T

S

V

S

W

A

D

A

I

K

R

E

D

R

K

L

I

G

G

Y

M

V

V

P

F

Q

Q

Q

N

P

P

F

D

G

N

-
x
Q

Y

F

E

V

G

G

F

A

T

T

V

V

E

E

R

D

-

D

-

V

A

A

L

F

D

G

L

L

H

E

R

N

S

K

F

G

Y

L

P

P

H

Y

W

K

D

E

M

M

-

V

-

S

-

R

-

V

Q

Q

L

E

E

A

Q

L

D

S

W

F

L

V

A

G

R

M

F

M

E

D

L

F

D

K

V

-

T

D

Q

R

Q

E

V

P

Q

A

R

R

L

L

S

S

V

G

G

G

Q

Q

R

K

Q

Q

S

R

L

V

A

A

L

I

I

A

M

G

A

I

M

I

A

A

Y

M

R

R

P

P

E

S

L

I

L

L

I

I

L

L

D

D

E
|
E

P

A

V

T

A

S

S

M

L

L

D

D

P

P

I

E

V

G

R

R

R

Q

K

E

F

L

M

I

V

Q

D

Y

L

I

F

E

D

D

L

I

A

R

L

Q

E

Q

S

Y

G

G

S

M

A

T

V

V

L

L

F

-

S

-

H

S

I

I

T

T

S

H

D

D

L

L

E

D

R

E

V

V

A

A

-

M

-

S

S

N

H

R

V

V

A

L

L

V

I

L

K

K

Q

Q

G

G

E

K

L

V

Q90 (vs. gap) mutation to A: No effect on ATPase, 10-fold decrease in riboflavin uptake; when associated with A-97 in EcfA2.
E163 (= E165) mutation to Q: 10-fold decrease in ATPase and riboflavin uptake; when associated with Q-171 in EcfA2.

7tbyA The structure of human abca1 in nanodisc (see paper)
30% identity, 69% coverage: 21:219/287 of query aligns to 688:892/1788 of 7tbyA

query
sites
7tbyA

K

K

N

L

G

G

V

V

E

S

K

I

Q

Q

A

N

L

L

K

V

D

K

-

V

-

Y

L

L

S

A

L

L

R

N

L

F

S

Y

A

E

G

G

M

Q

V

I

V

T

G

S

L

F

L

L

G

G

Q

H

N

N

G

G

A

A

G

G

K

K

S

T

T

T

L

T

M

M

R

S

C

I

A

L

L

T

G

G

I

L

L

F

S

P

P

P

D

T

S

S

G

G

D

T

I

A

R

Y

T

I

L

L

G

G

E

K

T

D

P

I

E

R

Q

S

L

E

S

M

S

S

A

T

A

I

K

R

E

Q

R

N

L

L

G

G

Y

V

V

C

P

P

Q

Q

Q

H

P

N

F

V

G

L

Y

F

E

D

G

M

F

L

T

T

V

V

E

E

R

E

A

-

L

-

D

-

L

-

H

H

R

I

S

W

F

F

Y

Y

P

A

-

R

-

L

-

K

-

G

-

L

-

S

-

E

-

K

H

H

W

V

D

K

M

A

Q

E

L

M

E

E

Q

Q

D

-

W

-

L

-

A

-

R

-

F

M

E

A

L

L

D

D

V

V

-

G

-

L

-

P

-

S

-

K

-

L

T

K

Q

S

Q

K

V

T

Q

S

R

Q

L

L

S

S

V

G

G

G

Q

M

R

Q

Q

R

S

K

L

L

A

S

L

V

I

A

M

L

A

A

M

F

A

V

Y

G

R

G

P

S

E

K

L

V

I

I

L

L

D

D

E

E

P

P

V

T

A

A

S

G

L

V

D

D

P

P

I

Y

V

S

R

R

K

G

F

I

M

W

V

E

D

L

L

L

F

-

D

-

L

L

A

K

L

Y

E

R

S

Q

G

G

S

R

A

T

V

I

L

I

F

L

S

S

S

T

H

H

I

H

T

M

S

D

D

E

L

A

E

D

R

V

V

L

A

G

S

D

H

R

V

I

A

A

L

I

I

I

K

S

Q

H

G

G

E

K

L

L

V

C

Sites not aligning to the query:

binding cholesterol: 161, 162

Query Sequence

>199270 FitnessBrowser__MR1:199270
MDQEFPPILEFSKVNKVFRGKNGVEKQALKDLSLRLSAGMVVGLLGQNGAGKSTLMRCAL
GILSPDSGDIRTLGETPEQLSSAAKERLGYVPQQPFGYEGFTVERALDLHRSFYPHWDMQ
LEQDWLARFELDVTQQVQRLSVGQRQSLALIMAMAYRPELLILDEPVASLDPIVRRKFMV
DLFDLALESGSAVLFSSHITSDLERVASHVALIKQGELVLFKEIDALREEVRLLKLAAGA
ELPEQVRILSRDGDSVLVDKGEVDLNLPGVQRSEALNLEQLFVELHK

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