Calmodulin-Binding Proteins in Plants

Protein

Method of
Identificationa

Sequence of
CaM-Binding Domain
(CaM-BD)b

Method of
Identifying
CaM-BDc

Reference(s)

Glutamate
Decarboxylased

A, B, C

HKKTDSEVQLEMITAWKKFVEEKKKK
VKKSDIDKQRDIITGWKKFVADRKKTSGIC
VKEKKMEKEILMEVIVGWRKFVKERKKMNGVC

E, S

3, 8,
147

NAD
Kinase

A, B

n.d.

n.a.

2, 75,
78, 119,
121

Apyrase
(Nuclear NTPase)

A, B

FNKCKNTIRKALKLNY

E

26, 62

Superoxide
Dismutase

B

n.d.

n.a.

53

Kinesin heavy
chain-like protein

A, B, C

ISSKEMVRLKKLVAYWKEQAGKK

E

116, 127

Elongation
factor 1a

A, B

n.d.

n.a.

40

Myosin V
homolog (MYA1)

D

IQRQFRTCMARe

S

80

Heat-shock
repressed protein

B, C

GWKIKAAMRWGFFVRKKA

E

83

Vacuolar
Ca2+-ATPase

A, B

ARQRWRSSVSIVKNRARRFRMISNL

E

89

Plasmalemma
Ca2+-ATPase

A, B

n.d.

n.a.

113, 114

ER
Ca2+-ATPase

A

n.d.

n.a.

4, 52,
61

Slow vacuolar
cation-channel

A

n.d.

n.a.

13

CaM-dependent
protein kinase II

B, C

ATPLKRLALKALSKALSEDELL

S, E

85, 143

Ca2+/CaM-activated
protein kinase

A, B

VVSRLRSFNARRKLRAAAIASVSLSS

E

105, 130

Phosphoprotein
phosphatase 2B

A

n.d.

n.a.

1, 86

Transcription factor
TGA3

A, B

LKMLVDSCLNHYANLFRMK

C

128

FK506-
binding protein

D

KIKEINKKDAKFYSNMFSKM

S

10

Root Tip
Protein

C

GKAVVGWKIKAAMRWGIFVRKKAA

B

117

Multidrug resistance
protein homolog

C

n.d.

n.a.

140

 

 

 

 

 

aIndicates the methods that have been used to demonstrate regulation of protein function by calmodulin or calmodulin binding. The general methods are: A, activity assay; B, binding assay; C, cloning via ligand binding; D, deduced from similarity to known calmodulin-binding homologs

bAmino acid sequences, given in one-letter IUPAC code, of regions demonstrated or predicted to be regions for calmodulin binding. n.d. = not determined

cIndicates the methods used to determine or predict the calmodulin-binding domain. The general methods are: B, predicted ability to form a basic, amphiphilic a-helix; E, experimentally determined using recombinant protein or peptide; C, computer prediction using the criteria of hydrophobic moment and mean hydrophobicity as described in ref. 43; S, sequence similarity with a calmodulin-binding domain from a homologous protein. n.a. = not applicable

dThe sequences for the calmodulin-binding domain of GAD are from Petunia and Arabidopsis.

eOne representative example of the six potential IQ motifs in MYA1 is shown.

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