Basic Information
Gene ID
Ciclev10000326m.g.v1.0
Position
scaffold_5:1089867-1094215 (+)
4348bp
Gene Type
gene
Gene Description (Protein Product)
actin binding
Organism
Also AS AT3G48090CICLE_v10000326mg

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
Ciclev10007551m.g.v1.0 Belongs to the adaptor complexes medium subunit family
Ciclev10026756m.g.v1.0 Binds to actin and affects the structure of the cytoskeleton. At high concentrations; profilin prevents the polymerization of actin; whereas it enhances it at low concentrations
Ciclev10009877m.g.v1.0 Binds to actin and affects the structure of the cytoskeleton. At high concentrations; profilin prevents the polymerization of actin; whereas it enhances it at low concentrations
Regulatory gene
Ciclev10000225m.g.v1.0 B3 domain-containing
Ciclev10000756m.g.v1.0 Transcription factor
Ciclev10000850m.g.v1.0 Protein SENSITIVE TO PROTON RHIZOTOXICITY

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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:0000003 reproduction BP
GO:0000226 microtubule cytoskeleton organization BP
GO:0000278 mitotic cell cycle BP
GO:0000281 mitotic cytokinesis BP
GO:0000746 obsolete conjugation BP
GO:0000747 conjugation with cellular fusion BP
GO:0000755 cytogamy BP
GO:0000910 cytokinesis BP
GO:0000912 assembly of actomyosin apparatus involved in cytokinesis BP
GO:0000915 actomyosin contractile ring assembly BP
GO:0003674 molecular_function MF
GO:0003779 actin binding MF
GO:0005488 binding MF
GO:0005515 protein binding MF
GO:0005575 cellular_component CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005737 cytoplasm CC
GO:0005826 actomyosin contractile ring CC
GO:0005856 cytoskeleton CC
GO:0005937 mating projection CC
GO:0005938 cell cortex CC
GO:0006996 organelle organization BP
GO:0007010 cytoskeleton organization BP
GO:0007015 actin filament organization BP
GO:0007017 microtubule-based process BP
GO:0007049 cell cycle BP
GO:0007163 establishment or maintenance of cell polarity BP
GO:0008064 regulation of actin polymerization or depolymerization BP
GO:0008092 cytoskeletal protein binding MF
GO:0008104 protein localization BP
GO:0008150 biological_process BP
GO:0008360 regulation of cell shape BP
GO:0009987 cellular process BP
GO:0010638 positive regulation of organelle organization BP
GO:0015629 actin cytoskeleton CC
GO:0016043 cellular component organization BP
GO:0019953 sexual reproduction BP
GO:0022402 cell cycle process BP
GO:0022413 reproductive process in single-celled organism BP
GO:0022414 reproductive process BP
GO:0022603 regulation of anatomical structure morphogenesis BP
GO:0022604 regulation of cell morphogenesis BP
GO:0022607 cellular component assembly BP
GO:0030029 actin filament-based process BP
GO:0030036 actin cytoskeleton organization BP
GO:0030427 site of polarized growth CC
GO:0030832 regulation of actin filament length BP
GO:0030833 regulation of actin filament polymerization BP
GO:0030838 positive regulation of actin filament polymerization BP
GO:0030863 cortical cytoskeleton CC
GO:0030864 cortical actin cytoskeleton CC
GO:0030865 cortical cytoskeleton organization BP
GO:0030866 cortical actin cytoskeleton organization BP
GO:0031032 actomyosin structure organization BP
GO:0031334 positive regulation of protein-containing complex assembly BP
GO:0032153 cell division site CC
GO:0032155 obsolete cell division site part CC
GO:0032271 regulation of protein polymerization BP
GO:0032273 positive regulation of protein polymerization BP
GO:0032505 reproduction of a single-celled organism BP
GO:0032506 cytokinetic process BP
GO:0032535 regulation of cellular component size BP
GO:0032956 regulation of actin cytoskeleton organization BP
GO:0032970 regulation of actin filament-based process BP
GO:0033036 macromolecule localization BP
GO:0033043 regulation of organelle organization BP
GO:0033365 protein localization to organelle BP
GO:0034613 protein localization BP
GO:0042995 cell projection CC
GO:0043226 organelle CC
GO:0043228 non-membrane-bounded organelle CC
GO:0043229 intracellular organelle CC
GO:0043232 intracellular non-membrane-bounded organelle CC
GO:0043254 regulation of protein-containing complex assembly BP
GO:0043332 mating projection tip CC
GO:0044085 cellular component biogenesis BP
GO:0044087 regulation of cellular component biogenesis BP
GO:0044089 positive regulation of cellular component biogenesis BP
GO:0044380 protein localization to cytoskeleton BP
GO:0044422 obsolete organelle part CC
GO:0044424 obsolete intracellular part CC
GO:0044430 obsolete cytoskeletal part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044446 obsolete intracellular organelle part CC
GO:0044448 obsolete cell cortex part CC
GO:0044463 obsolete cell projection part CC
GO:0044464 obsolete cell part CC
GO:0044703 multi-organism reproductive process BP
GO:0044764 obsolete multi-organism cellular process BP
GO:0044837 actomyosin contractile ring organization BP
GO:0045010 actin nucleation BP
GO:0048518 positive regulation of biological process BP
GO:0048522 positive regulation of cellular process BP
GO:0050789 regulation of biological process BP
GO:0050793 regulation of developmental process BP
GO:0050794 regulation of cellular process BP
GO:0051017 actin filament bundle assembly BP
GO:0051128 regulation of cellular component organization BP
GO:0051130 positive regulation of cellular component organization BP
GO:0051179 localization BP
GO:0051285 cell cortex of cell tip CC
GO:0051286 cell tip CC
GO:0051301 cell division BP
GO:0051493 regulation of cytoskeleton organization BP
GO:0051495 positive regulation of cytoskeleton organization BP
GO:0051641 cellular localization BP
GO:0051704 obsolete multi-organism process BP
GO:0061572 actin filament bundle organization BP
GO:0061640 cytoskeleton-dependent cytokinesis BP
GO:0065007 biological regulation BP
GO:0065008 regulation of biological quality BP
GO:0070727 cellular macromolecule localization BP
GO:0070938 contractile ring CC
GO:0071840 cellular component organization or biogenesis BP
GO:0071944 cell periphery CC
GO:0071963 establishment or maintenance of cell polarity regulating cell shape BP
GO:0072697 protein localization to cell cortex BP
GO:0072741 protein localization to cell division site BP
GO:0090066 regulation of anatomical structure size BP
GO:0097435 supramolecular fiber organization BP
GO:0099568 cytoplasmic region CC
GO:0099738 cell cortex region CC
GO:0110053 regulation of actin filament organization BP
GO:0120025 plasma membrane bounded cell projection CC
GO:0120038 obsolete plasma membrane bounded cell projection part CC
GO:1902407 assembly of actomyosin apparatus involved in mitotic cytokinesis BP
GO:1902410 mitotic cytokinetic process BP
GO:1902903 regulation of supramolecular fiber organization BP
GO:1902905 positive regulation of supramolecular fiber organization BP
GO:1903047 mitotic cell cycle process BP
GO:1903119 protein localization to actin cytoskeleton BP
GO:1903475 mitotic actomyosin contractile ring assembly BP
GO:1904498 protein localization to mitotic actomyosin contractile ring BP
GO:1904600 actin fusion focus assembly BP
GO:1990179 protein localization to actomyosin contractile ring BP
GO:1990778 protein localization to cell periphery BP
GO:1990819 actin fusion focus CC
KEGG Term Name Description
map04626 Plant-pathogen interaction Plants lack animal-like adaptive immunity mechanisms, and therefore have evolved a specific system with multiple layers against invading pathogens. The primary response includes the perception of pathogens by cell-surface pattern-recognition receptors (PRRs) and is referred to as PAMP-triggered immunity (PTI). Activation of FLS2 and EFR triggers MAPK signaling pathway that activates defense genes for antimictobial compounds. The increase in the cytosolic Ca2+ concentration is also a regulator for production of reactive oxygen species and localized programmed cell death/hypersensitive response. The secondary response is called effector-triggered immunity (ETI). Pathogens can acquire the ability to suppress PTI by directly injecting effector proteins into the plant cell through secretion systems. In addition, pathogens can manipulate plant hormone signaling pathways to evade host immune responses using coronatine toxin. Some plants possess specific intracellular surveillance proteins (R proteins) to monitor the presence of pathogen virulence proteins. This ETI occurs with localized programmed cell death to arrest pathogen growth, resulting in cultivar-specific disease resistance.