Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Expresssion
Pathway
Basic Information
Gene ID
Pt5G01450
View in Genome Browser
Position
chr5:51672293-51673234 (+)
941bp
Gene Type
gene
Gene Description (Protein Product)
Endoplasmin homolog
Organism
Pinus tabuliformis
Also AS AT4G24190

Gene Structure

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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
Pt7G19640 Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress
Pt9G06420 Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress
Pt7G40960 Manganese-dependent ADP-ribose CDP-alcohol
Regulatory gene
Pt0G00460 Transcription factor
Pt0G01630 dof zinc finger protein
Pt0G07980 dof zinc finger protein

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Annotation

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

Expression Profile
DataSet Number of Samples expressed(TPM>1) Mean Min Max Standard deviation(SD) Coeffcient variation(CV)


Pathway
Go Pathway KEGG Pathway
GO Term Description GO Category
GO:0001101 response to acid chemical BP
GO:0002790 peptide secretion BP
GO:0003674 molecular_function MF
GO:0003824 catalytic activity MF
GO:0005575 cellular_component CC
GO:0005576 extracellular region CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005634 nucleus CC
GO:0005737 cytoplasm CC
GO:0005739 mitochondrion CC
GO:0005773 vacuole CC
GO:0005774 vacuolar membrane CC
GO:0005783 endoplasmic reticulum CC
GO:0005788 endoplasmic reticulum lumen CC
GO:0005886 plasma membrane CC
GO:0005911 cell-cell junction CC
GO:0006810 transport BP
GO:0006950 response to stress BP
GO:0006970 response to osmotic stress BP
GO:0008104 protein localization BP
GO:0008150 biological_process BP
GO:0009266 response to temperature stimulus BP
GO:0009306 protein secretion BP
GO:0009409 response to cold BP
GO:0009414 response to water deprivation BP
GO:0009415 response to water BP
GO:0009506 plasmodesma CC
GO:0009507 chloroplast CC
GO:0009536 plastid CC
GO:0009628 response to abiotic stimulus BP
GO:0009651 response to salt stress BP
GO:0009888 tissue development BP
GO:0009934 regulation of meristem structural organization BP
GO:0009987 cellular process BP
GO:0010035 response to inorganic substance BP
GO:0010038 response to metal ion BP
GO:0010073 meristem maintenance BP
GO:0010075 regulation of meristem growth BP
GO:0012505 endomembrane system CC
GO:0015031 protein transport BP
GO:0015833 peptide transport BP
GO:0016020 membrane CC
GO:0016462 pyrophosphatase activity MF
GO:0016787 hydrolase activity MF
GO:0016817 hydrolase activity, acting on acid anhydrides MF
GO:0016818 hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides MF
GO:0016887 ATP hydrolysis activity MF
GO:0017111 ribonucleoside triphosphate phosphatase activity MF
GO:0022603 regulation of anatomical structure morphogenesis BP
GO:0030054 cell junction CC
GO:0031090 organelle membrane CC
GO:0031974 membrane-enclosed lumen CC
GO:0032501 multicellular organismal process BP
GO:0032502 developmental process BP
GO:0032940 secretion by cell BP
GO:0033036 macromolecule localization BP
GO:0033554 cellular response to stress BP
GO:0034976 response to endoplasmic reticulum stress BP
GO:0040008 regulation of growth BP
GO:0042221 response to chemical BP
GO:0042886 amide transport BP
GO:0043226 organelle CC
GO:0043227 membrane-bounded organelle CC
GO:0043229 intracellular organelle CC
GO:0043231 intracellular membrane-bounded organelle CC
GO:0043233 organelle lumen CC
GO:0044422 obsolete organelle part CC
GO:0044424 obsolete intracellular part CC
GO:0044432 obsolete endoplasmic reticulum part CC
GO:0044437 obsolete vacuolar part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044446 obsolete intracellular organelle part CC
GO:0044464 obsolete cell part CC
GO:0045184 establishment of protein localization BP
GO:0046686 response to cadmium ion BP
GO:0046903 secretion BP
GO:0048046 apoplast CC
GO:0048507 meristem development BP
GO:0048509 regulation of meristem development BP
GO:0048638 regulation of developmental growth BP
GO:0048856 anatomical structure development BP
GO:0050789 regulation of biological process BP
GO:0050793 regulation of developmental process BP
GO:0050896 response to stimulus BP
GO:0051179 localization BP
GO:0051234 establishment of localization BP
GO:0051716 cellular response to stimulus BP
GO:0055044 symplast CC
GO:0065007 biological regulation BP
GO:0070013 intracellular organelle lumen CC
GO:0071702 organic substance transport BP
GO:0071705 nitrogen compound transport BP
GO:0071944 cell periphery CC
GO:0098588 bounding membrane of organelle CC
GO:0098805 membrane CC
GO:1901700 response to oxygen-containing compound BP
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.
map04141 Protein processing in endoplasmic reticulum The endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylated. Correctly folded proteins are packaged into transport vesicles that shuttle them to the Golgi complex. Misfolded proteins are retained within the ER lumen in complex with molecular chaperones. Proteins that are terminally misfolded bind to BiP and are directed toward degradation through the proteasome in a process called ER-associated degradation (ERAD). Accumulation of misfolded proteins in the ER causes ER stress and activates a signaling pathway called the unfolded protein response (UPR). In certain severe situations, however, the protective mechanisms activated by the UPR are not sufficient to restore normal ER function and cells die by apoptosis.