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Table 3 The residues corresponding to Asp 80 of NbXIP1;1 and the residues in four of the positions in the ar/R selectivity filter

From: Single amino acid substitutions in the selectivity filter render NbXIP1;1α aquaporin water permeable

AQP

D80 (H1)a

H2P

H5P

LEP

HEP

Reference

XIP-I

I

H/Qb

G/A/Q

A/T

R

c

XIP-II, Clade A

T/S

V/I/G

I/V/T/S

V/A

R

c

XIP-III, Clade B

D

V/I/A

T/S

V/A

R

c

XIP-IV, Clade B

D

I/L/A

T

A/V

R

c

TIP1s, Gymnosperm

E

Hb

I

A

R

d

TIP1s, Mono/dicot

Q/S

H

I

A

V

d

TIP3s, Mono/dicots

E

Hb

I/M

A

R

d

PfAQP

E

W

G

F

R

e

  1. aThe acidic residue corresponding to Asp 80 in helix 1 (H1) of NbXIP1;1 is conserved in XIPs of clade B. Acidic residues at this position may form a salt bridge to arginine in HEP; bXIP-Is and some TIP1s as well as TIP3s are likely to have a TIP2-like H2P polar interaction with the arginine at HEP;c [18]; d [20]; e [45]