Basic Information
Gene ID
Position
GWHASIS00001971:34280882-34287258 (-)
6376bp
Gene Type
gene
Gene Description (Protein Product)
Multidrug Resistance
Organism
Also AS AT3G28345

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
EVM0008283 Belongs to the 14-3-3 family
EVM0008999 Belongs to the 14-3-3 family
EVM0010193 Belongs to the 14-3-3 family
Regulatory gene
EVM0000738 PHR1-LIKE 1-like
EVM0001315 transcription factor that promotes early floral meristem identity in synergy with APETALA1; FRUITFULL and LEAFY. Is required subsequently for the transition of an inflorescence meristem into a floral meristem. Seems to be partially redundant to the function of APETALA1
EVM0001600 PHR1-LIKE 1-like

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Annotation

Orthologous Group
Orthologous ID Species Number All hits in PereRegDB Hits of this species Orthologous Detail


Pathway
GO Term Description GO Category
GO:0005575 cellular_component CC
GO:0005623 obsolete cell CC
GO:0005886 plasma membrane CC
GO:0016020 membrane CC
GO:0044464 obsolete cell part CC
GO:0071944 cell periphery CC
KEGG Term Name Description
map02010 ABC transporters The ATP-binding cassette (ABC) transporters form one of the largest known protein families, and are widespread in bacteria, archaea, and eukaryotes. They couple ATP hydrolysis to active transport of a wide variety of substrates such as ions, sugars, lipids, sterols, peptides, proteins, and drugs. The structure of a prokaryotic ABC transporter usually consists of three components; typically two integral membrane proteins each having six transmembrane segments, two peripheral proteins that bind and hydrolyze ATP, and a periplasmic (or lipoprotein) substrate-binding protein. Many of the genes for the three components form operons as in fact observed in many bacterial and archaeal genomes. On the other hand, in a typical eukaryotic ABC transporter, the membrane spanning protein and the ATP-binding protein are fused, forming a multi-domain protein with the membrane-spanning domain (MSD) and the nucleotide-binding domain (NBD).