Plant Transcription Factor Database
Previous version: v3.0
Vitis vinifera
HD-ZIP Family
Species TF ID Description
GSVIVT01032491001HD-ZIP family protein
GSVIVT01020033001HD-ZIP family protein
GSVIVT01033481001HD-ZIP family protein
GSVIVT01009083001HD-ZIP family protein
GSVIVT01001366001HD-ZIP family protein
GSVIVT01018247001HD-ZIP family protein
GSVIVT01011377001HD-ZIP family protein
GSVIVT01008065001HD-ZIP family protein
GSVIVT01003431001HD-ZIP family protein
GSVIVT01005821001HD-ZIP family protein
GSVIVT01020078001HD-ZIP family protein
GSVIVT01002447001HD-ZIP family protein
GSVIVT01038619001HD-ZIP family protein
GSVIVT01009274001HD-ZIP family protein
GSVIVT01033744001HD-ZIP family protein
GSVIVT01011754001HD-ZIP family protein
GSVIVT01019012001HD-ZIP family protein
GSVIVT01014276001HD-ZIP family protein
GSVIVT01019655001HD-ZIP family protein
GSVIVT01027407001HD-ZIP family protein
GSVIVT01017073001HD-ZIP family protein
GSVIVT01030605001HD-ZIP family protein
GSVIVT01012643001HD-ZIP family protein
GSVIVT01027508001HD-ZIP family protein
GSVIVT01029396001HD-ZIP family protein
GSVIVT01017010001HD-ZIP family protein
GSVIVT01021625001HD-ZIP family protein
GSVIVT01035612001HD-ZIP family protein
GSVIVT01013073001HD-ZIP family protein
GSVIVT01010600001HD-ZIP family protein
GSVIVT01016272001HD-ZIP family protein
GSVIVT01025193001HD-ZIP family protein
GSVIVT01035238001HD-ZIP family protein
HD-ZIP Family Introduction

A homeobox (HB) encodes a protein domain, the homeodomain (HD), which is a conserved 60-amino acid motif present in transcription factors found in all the eukaryotic organisms. This 60-amino acid sequence folds into a characteristic three-helix structure that is able to interact specifically with DNA. Most HDs are able to bind DNA as monomers with high affinity, through interactions made by helix III (the so-called recognition helix) and a disordered N-terminal arm located beyond helix I. The high degree of conservation of this type of domain among diverse proteins from different kingdoms indicates that this structure is crucial to maintain the HD functionality and that the role played by this domain is vital.

Members of the HD-Zip family have a leucine zipper motif (LZ) immediately downstream of the HD. The two motifs are present in transcription factors found in species belonging to other eukaryotic kingdoms, but their association in a single protein is unique to plants. The HD is responsible for the specific binding to DNA, whereas LZ acts as a dimerization motif. HD-Zip proteins bind to DNA as dimers, and the absence of LZ absolutely abolishes their binding ability, which indicates that the relative orientation of the monomers, driven by this motif, is crucial for an efficient recognition of DNA.

Ariel FD, Manavella PA, Dezar CA, Chan RL.
The true story of the HD-Zip family.
Trends Plant Sci, 2007. 12(9): p. 419-26.
PMID: 17698401