SitesBLAST

R257 (= R287) mutation to C: Sodium-independent binding affinity for proline.
C281 (≠ F316) mutation to S: Does not affect proline uptake activity. Confers resistance to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
C344 (≠ G377) mutation to S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
C349 (≠ G382) mutation to S: Does not affect proline uptake activity. Sensitive to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
R376 (≠ K410) mutation R->E,Q: No change in activity.; mutation to K: Loss of activity.

Q92911 Sodium/iodide cotransporter; Na(+)/I(-) cotransporter; Natrium iodide transporter; Sodium-iodide symporter; Na(+)/I(-) symporter; Solute carrier family 5 member 5 from Homo sapiens (Human) (see 3 papers)
25% identity, 32% coverage: 44:221/554 of query aligns to 25:201/643 of Q92911

query
sites
Q92911

F

L

V

V

A

S

V

T

T

G

L

I

A

G

V

L

T

W

I

V

R

G

A

L

A

A

R

R

R

G

G

G

T

Q

R

R

T

S

A

A

S

E

D

D

F

F

Y

F

A

T

A

G

G

G

G

R

S

R

L

L

G

A

V

L

Q

P

N

V

G

G

L

L

A

S

I

L

A

S

G

A

D

S

Y

F

T

M

S

S

A

A

A

V

T

Q

F

V

L

L

G

G

V

V

T

P

A

S

L

E

V

A

Y

Y

G

R

S

Y

G

G

Y

L

D

K

G

F

M

L

I

W

Y

M

A

C

V

L

G

G

F

Q

L

L

V

L

G

N

F

S

P

V

M

L

I

T

L
x
A

F

L

L

L

I

F

A

M

E

P

P

V

L

F

R

Y

N

R

L

L

G

G

R

L

Y

T

T

S

F

T

A

Y

D

E

V

Y

A

L

A

E

Y

M

R

R

L

F

A

S

E

R

I

A

P

-

V

V

R

R

L

L

V

C

A

G

G

T

L

L

N

Q

T

Y

L

I

V

V

I

A

V

T

L

M

L

L

Y

Y

L

T

I

G

A

I

Q

V

M

I

V

Y

G

A

A

P

G

A

K

L

L

I

I

L

E

N

L

Q

L

V

F

T

G

G

L

L

P

D

Y

I

A

W

T

A

A

S

V

L

A

L

L

S

V

T

G

G

V

I

L

I

M

C

M

T

L

F

Y

Y

V

T

A

A

F

V

G

G

M

M

R

K

A

A

T

V

W

W

V

T

Q

D

I

V

I

F

K

Q

A

V

V

V

L

V

L

M

L

L

A

S

G

G

A102 (≠ L121) natural variant: A -> P

Sites not aligning to the query:

226 mutation H->A,D,E,K: Significant loss of iodide transport activity but no effect on its localization to the cell membrane.
237 D→A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization.
242 Required for homodimerization; Y→A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471. Loss of iodide transport activity; when associated with F-535.
243 Required for homodimerization; T→A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471.
471 Required for homodimerization; Q→A: No effect on localization to the cell membrane, iodide transport activity and homodimerization. Significant loss of homodimerization; when associated with A-242 or A243.
525 A→F: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Loss of iodide transport activity; when associated with A-242.
536 T → Q: requires 2 nucleotide substitutions
556 S → Q: requires 2 nucleotide substitutions

5nv9A Substrate-bound outward-open state of a na+-coupled sialic acid symporter reveals a novel na+-site (see paper)
22% identity, 38% coverage: 44:252/554 of query aligns to 13:222/480 of 5nv9A

query
sites
5nv9A

F

Y

V

L

A

A

V

A

T

M

L

L

A

L

V

V

T

G

I

V

R

Y

A

F

A

S

R

K

R

R

G

-

T

Q

R

K

T

T

A

A

S

D

D

D

F

Y

Y

F

A

R

A

G

G

G

S

R

L

V

G

P

G

G

V

W

Q

A

N

A

G

G

L

V

A

S

I

V

A

F

G
x
A

D
x
T

Y
x
T

T
x
L

S
|
S

A

S

A
x
I

T
|
T

F

F

L

M

G

S

V

I

T

P

A

A

L

K

V

A

Y

Y

G

T

S

S

G

D

Y

W

D

T

G

F

M

I

I

I

Y
x
G

A
x
Q

V

Y

G

L

F

A

L

I

V

A

G

I

F

L

P

P

M

L

I

V

L

F

F

Y

L

F

I

Y

A

I

E

P

P

F

L

F

R

R

N

K

L

L

G

K

R

I

Y

T

T

S

F

A

A

Y

D

E

V

Y

A

L

A

E

Y

A

R

R

L

F

A

-

E

D

I

V

P

R

V

S

R

R

L

L

V

F

A

A

G

S

L

L

N

S

T

-

L

-

V

-

I

-

V

F

L

M

L

L

Y

F

L

H

I

I

A

G

Q
x
R

M

V

V

A

G

I

A

I

G

T

K

Y

L

L

I

T

E

V

L

L

-

A

-

L

-

R

-

P

L

F

F

M

G

G

L

I

P

D

Y

P

A

V

T

V

A

L

V

I

A

V

L

L

V

I

G

S

V

L

L

L

M

C

M

I

L

I

Y

Y

V

T

A

W

F

M

G

G

M

I

R

E

A

G

T
x
V

T

I

W

W

V

T

Q
x
D

I

V

I

I

K

Q

A

G

V

L

L

L

L

S

A

G

G

G

T

A

A

V

L

L

M

I

A

F

A

I

L

M

I

I

L

C

A

F

R

K

F

V

G

D

F

G

S

G

L

I

E

S

A

E

L

I

F

F

-

T

A

A

R

Q

A

A

I

D

A

K

L

F

H

F

P

P

K

T

S

T

R

Q

binding sodium ion: A52 (≠ G84), T53 (≠ D85), L55 (≠ T87), S56 (= S88), V174 (≠ T207), D178 (≠ Q211)
binding N-acetyl-beta-neuraminic acid: T54 (≠ Y86), S56 (= S88), I58 (≠ A90), T59 (= T91), G77 (≠ Y109), Q78 (≠ A110), R131 (≠ Q168)

Sites not aligning to the query:

B4EZY7 Sodium/sialic acid symporter SiaT; Na(+)-coupled sialic acid symporter; Sialic acid transporter from Proteus mirabilis (strain HI4320) (see paper)
22% identity, 38% coverage: 44:252/554 of query aligns to 17:226/496 of B4EZY7

query
sites
B4EZY7

F

Y

V

L

A

A

V

A

T

M

L

L

A

L

V

V

T

G

I

V

R

Y

A

F

A

S

R

K

R

R

G

-

T

Q

R

K

T

T

A

A

S

D

D

D

F

Y

Y

F

A

R

A

G

G

G

S

R

L

V

G

P

G

G

V

W

Q

A

N

A

G

G

L

V

A

S

I

V

A

F

G
x
A

D

T

Y
x
T

T
x
L

S
|
S

A

S

A

I

T
|
T

F

F

L

M

G

S

V

I

T

P

A

A

L

K

V

A

Y

Y

G

T

S

S

G

D

Y

W

D

T

G

F

M

I

I

I

Y

G

A
x
Q

V

Y

G

L

F

A

L

I

V

A

G

I

F

L

P

P

M

L

I

V

L

F

F

Y

L

F

I

Y

A

I

E

P

P

F

L

F

R

R

N

K

L

L

G

K

R

I

Y

T

T

S

F

A

A

Y

D

E

V

Y

A

L

A

E

Y

A

R

R

L

F

A

-

E

D

I

V

P

R

V

S

R

R

L

L

V

F

A

A

G

S

L

L

N

S

T

-

L

-

V

-

I

-

V

F

L

M

L

L

Y

F

L

H

I

I

A

G

Q
x
R

M

V

V

A

G

I

A

I

G

T

K

Y

L

L

I

T

E

V

L

L

-

A

-

L

-

R

-

P

L

F

F

M

G

G

L

I

P

D

Y

P

A

V

T

V

A

L

V

I

A

V

L

L

V

I

G

S

V

L

L

L

M

C

M

I

L

I

Y

Y

V

T

A

W

F

M

G

G

M

I

R

E

A

G

T

V

T

I

W

W

V

T

Q
x
D

I

V

I

I

K

Q

A

G

V

L

L

L

L

S

A

G

G

G

T

A

A

V

L

L

M

I

A

F

A

I

L

M

I

I

L

C

A

F

R

K

F

V

G

D

F

G

S

G

L

I

E

S

A

E

L

I

F

F

-

T

A

A

R

Q

A

A

I

D

A

K

L

F

H

F

P

P

K

T

S

T

R

Q

A56 (≠ G84) binding Na(+)
T58 (≠ Y86) mutation to A: 2-fold increase in Neu5Ac transport.
L59 (≠ T87) binding Na(+)
S60 (= S88) mutation to A: Abolishes Neu5Ac transport.
T63 (= T91) mutation to A: Abolishes Neu5Ac transport.
Q82 (≠ A110) mutation to D: Abolishes Neu5Ac transport.
R135 (≠ Q168) mutation to E: Abolishes Neu5Ac transport.
D182 (≠ Q211) binding Na(+); mutation to A: Abolishes Neu5Ac transport.

Sites not aligning to the query:

339 binding Na(+)
342 binding Na(+); binding Na(+); S→A: Abolishes Neu5Ac transport.
343 binding Na(+); S→A: Abolishes Neu5Ac transport.
345 binding Na(+); S→A: Reduces Neu5Ac transport.
346 binding Na(+); S→A: Slightly increases Neu5Ac transport.

Q9Y289 Sodium-dependent multivitamin transporter; Na(+)-dependent multivitamin transporter; hSMVT; Solute carrier family 5 member 6 from Homo sapiens (Human) (see 10 papers)
22% identity, 85% coverage: 59:528/554 of query aligns to 52:515/635 of Q9Y289

query
sites
Q9Y289

G

G

T

R

R

H

T

T

A

V

S

G

D

E

F

L

Y

L

A

M

A

A

G

D

G

R

S

K

L

M

G

G

G
x
C

V

L

Q

P

N

V

G

A

L

L

A

S

I

L

A

L

G

A

D
x
T

Y

F

T

Q

S

S

A

A

A

V

T

A

F

I

L

L

G

G

V

V

T

P

A

S

L

E

V

I

Y

Y

-
x
R

-
x
F

G
|
G

S
x
T

G
x
Q

Y
|
Y

D
x
W

-
x
F

-
x
L

G
|
G

M
x
C

I
x
C

Y
|
Y

A
x
F

V
x
L

G
|
G

F
x
L

L
|
L

V
x
I

G

-

F

-

P
|
P

M
x
A

I
x
H

L
x
I

F
|
F

L
x
I

I

-

A

-

E

-

P
|
P

L
x
V

R
x
F

N

-

L

-

G

-

R

-

Y
|
Y

T
x
R

F
x
L

A
x
H

D
x
L

V
x
T

A
x
S

A
|
A

Y
|
Y

R
x
E

L
x
Y

A
x
L

E
|
E

I
x
L

-
x
R

-
x
F

-
x
N

-
x
K

P
x
T

V
|
V

R
|
R

L
x
V

V
x
C

A
x
G

G
x
T

L
x
V

N
x
T

T
x
F

L
x
I

V
x
F

I
x
Q

V
x
M

L
x
V

L
x
I

Y
|
Y

L
x
M

I
x
G

A
x
V

Q
x
V

M
x
L

V
x
Y

G
x
A

A
x
P

G
x
S

K
x
L

L
x
A

I
x
L

E
x
N

L
x
A

L
x
V

F
x
T

G
|
G

L
x
F

P
x
D

Y
x
L

A
x
W

T
x
L

A
x
S

V
|
V

A
x
L

L
x
A

V
x
L

G
|
G

V
x
I

L
x
V

M
x
C

M
x
T

L
x
V

Y
|
Y

V
x
T

A
|
A

F
x
L

G
|
G

M
x
L

R
x
K

A
|
A

T
x
V

T
x
I

W
|
W

V
x
T

Q
x
D

I
x
V

I
x
F

K
x
Q

A
x
T

V
x
L

L
x
V

L
x
M

L
x
F

A
x
L

G
|
G

T
x
Q

A
x
L

L
x
A

M
x
V

A
x
I

L
x
V

I
x
G

L
x
S

A
|
A

R
x
K

F
x
V

G
|
G

F

-

S
x
G

L
|
L

E
x
G

A
x
R

L
x
V

F
x
W

A
|
A

R
x
V

A
|
A

I
x
S

A
x
Q

L
x
H

H
x
G

P
x
R

K
x
I

S
|
S

R
x
G

A
x
F

I
x
E

M
x
L

A
x
D

P
|
P

G
x
D

G
x
P

L
x
F

V
|
V

R
|
R

D
x
H

P
x
T

V
x
F

S
x
W

A
x
T

L
|
L

S
x
A

L
x
F

-
x
G

G
|
G

L
x
V

A
x
F

L
x
M

I
x
M

F
x
L

G
x
S

T
x
L

A
x
Y

G
|
G

L
x
V

P
x
N

H
x
Q

-
x
A

I
x
Q

L
x
V

M
x
Q

R
|
R

F
x
Y

F
x
L

T
x
S

V
x
S

A
x
R

D
x
T

A
x
E

R
x
K

E
x
A

A
|
A

R
x
V

L
|
L

S
|
S

V
x
C

L
x
Y

V
x
A

A
x
V

T
x
F

G
x
P

F
|
F

I
x
Q

T
x
Q

V
|
V

F
x
S

Y
x
L

T
x
C

L
x
V

L
x
G

F
x
C

V
x
L

L
x
I

G
|
G

F
x
L

G
x
V

A
x
M

I
x
F

A
|
A

L
x
Y

V
x
Y

L
x
Q

G
x
E

E
x
Y

P
|
P

A
x
M

F
x
S

T
x
I

D
x
Q

A
x
Q

A
|
A

G
x
Q

R

-

L

-

I

-

G
x
A

P
|
P

N
x
D

M
x
Q

V
x
F

A
x
V

L
|
L

H
x
Y

L
x
F

A
x
V

-
x
M

D
|
D

R
x
L

L
|
L

G
x
K

G
|
G

A
x
L

P
|
P

-
x
G

L
|
L

L
x
P

G
|
G

F
x
L

I
x
F

S
x
I

A
|
A

V
x
C

A
x
L

F
|
F

A
x
S

T
x
G

I
x
S

L
|
L

A
x
S

V
x
T

V
x
I

S
|
S

G
x
S

L
x
A

A
x
F

I
x
N

A
x
S

G
x
L

A
|
A

S
x
T

A
x
V

A
x
T

S
x
M

H
x
E

D
|
D

L
|
L

Y
x
I

A
x
R

R
x
P

V
x
W

L
x
F

R
x
P

R

-

G

-

R
x
E

A
x
F

S
|
S

E
|
E

A
|
A

E
x
R

E
x
A

V
x
I

R
x
M

V
x
L

S
|
S

K
x
R

G
|
G

A
x
L

A
|
A

V
x
F

A
x
G

I
x
Y

S
x
G

L
|
L

A

-

M
x
L

A
x
C

L
|
L

G
|
G

L
x
M

A
|
A

F
x
Y

E
x
I

N
x
S

Q
x
S

N
x
Q

I
x
M

A
x
G

F
x
P

L
x
V

V
x
L

G
x
Q

L
x
A

V
x
A

F
x
I

A
x
S

I
|
I

A
x
F

A
x
G

S
x
M

A
x
V

N
x
G

F
x
G

P
|
P

V
x
L

I
x
L

-
x
G

-
x
L

-
x
F

V
x
C

L
|
L

S
x
G

V
x
M

S
x
F

W
x
F

P
|
P

G
x
C

L
x
A

T
x
N

T
x
P

R
x
P

G
|
G

A
|
A

V
|
V

A
x
V

G
|
G

S
x
L

L
|
L

A
|
A

G
|
G

L
|
L

L
x
V

C
x
M

A
|
A

L
x
F

G

-

L

-

M

-

I
x
W

L
x
I

G
|
G

P
x
I

G
|
G

V
x
S

W
x
I

T
x
V

A
x
T

V
x
S

L
x
M

G
|
G

L
x
S

G
x
S

A
x
M

A
x
P

P
|
P

F
x
S

P
|
P

Y

-

D
x
S

N
|
N

P
x
G

A
x
S

L
x
S

F
|
F

S
|
S

V
x
L

P
|
P

L
x
T

A
x
N

F
x
L

V
x
T

T
x
V

A
|
A

V
x
T

A
x
V

V
x
T

S
x
T

R
x
L

L
x
M

D
x
P

R
x
L

S
x
T

A
x
T

A
x
F

A
x
S

R
x
K

C68 (≠ G75) mutation to A: No effect on biotin transport.
T78 (≠ D85) mutation to A: Reduced membrane localization. Decrease in biotin transport.
C104 (≠ M107) mutation to A: No effect on biotin transport.
R123 (≠ T135) to L: in SMVTD; reduced membrane localization; impaired biotin transport
S128 (≠ A140) mutation to A: No effect on biotin transport.
N138 (vs. gap) mutation to A: Reduced protein levels. Decrease in biotin transport.
C144 (≠ V152) mutation to A: No effect on biotin transport.
Y162 (≠ V170) to C: in COMNB; no effect on membrane localization
C187 (≠ M195) mutation to A: No effect on biotin transport.
S242 (= S251) mutation to A: No effect on biotin transport.
S283 (≠ T290) mutation to A: No effect on protein levels or membrane localization.
T286 (≠ D293) mutation to A: Resistant to phorbol 12-myristate 13-acetate (PMA)-induced inhibition of biotin transport. No effect on protein levels or membrane localization.
C294 (≠ V301) mutation to A: Reduced membrane localization. Decrease in biotin transport (decreased Vmax, no change in Km).; mutation C->S,M: Decrease in biotin transport.
C309 (≠ F316) mutation to A: No effect on biotin transport.
C358 (≠ V366) mutation to A: No effect on biotin transport.
T366 (≠ V374) mutation to A: No effect on biotin transport.
R400 (≠ K410) to T: in SMVTD; impaired biotin transport; dbSNP:rs370950187
C410 (≠ A422) mutation to A: No effect on biotin transport.
S429 (≠ A441) to G: in COMNB; no effect on membrane localization
C443 (≠ V452) mutation to A: No effect on biotin transport.
C450 (≠ G459) mutation to A: No effect on biotin transport.
S481 (≠ L493) to F: in dbSNP:rs1395
N489 (= N502) mutation to A: Slight decrease in protein levels. Decrease in biotin transport.
N498 (≠ A511) mutation to A: No effect on biotin transport.

Sites not aligning to the query:

94:635 natural variant: Missing (in SMVTD and COMNB; reduced membrane localization; impaired biotin transport; dbSNP:rs994218778)
534 N→A: No effect on biotin transport.
567:635 mutation Missing: Loss of biotin transport. Loss of membrane localization.
570:635 mutation Missing: Loss of biotin transport. Loss of membrane localization.
575:635 mutation Missing: Partial loss (75%) of biotine transport. Apical membrane localization and intracellular structure localization in polarized cells.
577 C→A: No effect on biotin transport.
583 C→A: No effect on biotin transport.
584:635 mutation Missing: Partial loss (75%) of biotine transport. Apical membrane localization and intracellular structure localization in polarized cells.
600:635 mutation Missing: Partial loss (75%) of biotine transport. Apical membrane localization and intracellular structure localization in polarized cells.
612:635 mutation Missing: Partial loss (75%) of biotine transport. Apical membrane localization and intracellular structure localization in polarized cells.
616:635 mutation Missing: Loss of apical membrane localization in polarized cells. Basolateral localization in polarized cells.
620:635 mutation Missing: Partial loss (25%) of biotine transport. No change in apical membrane localization in polarized cells.
624:635 mutation Missing: Partial loss (25%) of biotine transport. No change in apical membrane localization in polarized cells.
627 T→A: No effect on biotin transport.
628 mutation C->A,S: Decrease in biotin transport.
632:635 mutation Missing: Partial loss (25%) of biotine transport. No change in apical membrane localization in polarized cells.

Query Sequence

>WP_012333673.1 NCBI__GCF_000019365.1:WP_012333673.1
MRPRLLPALVPLALAAGPAAADALSGPSSRQALNPVAIGLFLAFVAVTLAVTIRAARRGT
RTASDFYAAGGSLGGVQNGLAIAGDYTSAATFLGVTALVYGSGYDGMIYAVGFLVGFPMI
LFLIAEPLRNLGRYTFADVAAYRLAEIPVRLVAGLNTLVIVLLYLIAQMVGAGKLIELLF
GLPYATAVALVGVLMMLYVAFGGMRATTWVQIIKAVLLLAGTALMAALILARFGFSLEAL
FARAIALHPKSRAIMAPGGLVRDPVSALSLGLALIFGTAGLPHILMRFFTVADAREARLS
VLVATGFITVFYTLLFVLGFGAIALVLGEPAFTDAAGRLIGGPNMVALHLADRLGGAPLL
GFISAVAFATILAVVSGLAIAGASAASHDLYARVLRRGRASEAEEVRVSKGAAVAISLAA
MALGLAFENQNIAFLVGLVFAIAASANFPVIVLSVSWPGLTTRGAVAGSLAGLLCALGLM
ILGPGVWTAVLGLGAAPFPYDNPALFSVPLAFVTAVAVSRLDRSAAARAVRAAYRAQHVT
AQTGFDRPRPVAAH

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