Gene Details:
- Gene ID: AT3G04790
- Gene Symbol: EMB3119
- Gene Name: EMBRYO DEFECTIVE 3119
- Description: Ribose 5-phosphate isomerase, type A protein;(source:Araport11)
- TAIR Accession: locus:2084898
- Genome: Araport11_genome_release
- Species: Arabidopsis thaliana
Transcripts:
Plant Ontology Annotations:
- PO:0009001 — fruit — frucht (exact, German), fruto (exact, Spanish), 果実 (exact, Japanese), coenocarp (narrow), syncarp (narrow), aggregate fruit (broad), compound fruit (broad), dehiscent fruit (broad), diaspore (broad), indehiscent fruit (broad), multiple fruit (broad), propagule (broad)
- PO:0009005 — root — raíz (Spanish, exact), radices (exact, plural), radix (exact), 根 (Japanese, exact), aerial root (narrow), climbing root (narrow)
- PO:0009025 — vascular leaf — foliage leaf (exact), hoja vascular (Spanish, exact), leaf, vascular (exact), vascular leaves (exact, plural), 維管束のある葉, または維管束植物の葉 (Japanese, exact), crozier (related), macrophyll (related), megaphyll (related), ascidia (narrow), ascidium (narrow), fiddlehead (narrow), frond (narrow), needle-like leaf (narrow), pitcher (narrow), pitcher blade (narrow), pitcher-blade (narrow), scale-like leaf (narrow), sterile frond (narrow), trophophyll (narrow)
- PO:0009049 — inflorescence — inflorescencia (Spanish, exact), 花序 (Japanese, exact), Triticeae spike (narrow)
Gene Ontology:
- GO:0009535 — located in — chloroplast thylakoid membrane
- GO:0009507 — located in — chloroplast
- GO:0009052 — involved in — pentose-phosphate shunt, non-oxidative branch
- GO:0004751 — enables — ribose-5-phosphate isomerase activity
- GO:0009941 — located in — chloroplast envelope
- GO:0009570 — located in — chloroplast stroma
- GO:0019253 — acts upstream of or within — reductive pentose-phosphate cycle
- GO:0005829 — located in — cytosol
Function-related keywords:
- fruit , root , vascular leaf , inflorescence
Literature:
- The Arabidopsis ppi1 mutant is specifically defective in the expression, chloroplast import, and accumulation of photosynthetic proteins. DOI: 10.1105/tpc.012955 ; PMID: 12897258
- Inactivation of the chloroplast ATP synthase gamma subunit results in high non-photochemical fluorescence quenching and altered nuclear gene expression in Arabidopsis thaliana. DOI: 10.1074/jbc.M308435200 ; PMID: 14576160
- Linking protein fractionation with multidimensional monolithic reversed-phase peptide chromatography/mass spectrometry enhances protein identification from complex mixtures even in the presence of abundant proteins. DOI: 10.1002/rcm.1376 ; PMID: 15052571
- Functional specialization amongst the Arabidopsis Toc159 family of chloroplast protein import receptors. DOI: 10.1105/tpc.104.023309 ; PMID: 15273297
- New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast, and versatile fractionation strategy. DOI: 10.1074/jbc.M406763200 ; PMID: 15322131
- New targets of Arabidopsis thioredoxins revealed by proteomic analysis. DOI: 10.1002/pmic.200400805 ; PMID: 15352244
- A coumaroyl-ester-3-hydroxylase insertion mutant reveals the existence of nonredundant meta-hydroxylation pathways and essential roles for phenolic precursors in cell expansion and plant growth. DOI: 10.1104/pp.105.069690 ; PMID: 16377748
- Transcriptional profiling implicates novel interactions between abiotic stress and hormonal responses in Thellungiella, a close relative of Arabidopsis. DOI: 10.1104/pp.105.070508 ; PMID: 16500996
- Post-translational modifications, but not transcriptional regulation, of major chloroplast RNA-binding proteins are related to Arabidopsis seedling development. DOI: 10.1002/pmic.200500657 ; PMID: 16548064
- High light response of the thylakoid proteome in arabidopsis wild type and the ascorbate-deficient mutant vtc2-2. A comparative proteomics study. DOI: 10.1104/pp.106.080150 ; PMID: 16648217
- Structural and functional insights into the chloroplast ATP-dependent Clp protease in Arabidopsis. DOI: 10.1105/tpc.106.044594 ; PMID: 16980539
- A mutation in an Arabidopsis ribose 5-phosphate isomerase reduces cellulose synthesis and is rescued by exogenous uridine. DOI: 10.1111/j.1365-313X.2006.02902.x ; PMID: 17059404
- Modifications to the Arabidopsis defense proteome occur prior to significant transcriptional change in response to inoculation with Pseudomonas syringae. DOI: 10.1104/pp.106.086231 ; PMID: 17028151
- Oviposition by pierid butterflies triggers defense responses in Arabidopsis. DOI: 10.1104/pp.106.090837 ; PMID: 17142483
- Comparative proteomic approaches for the isolation of proteins interacting with thioredoxin. DOI: 10.1002/pmic.200600443 ; PMID: 17163439
- Phosphoproteomic identification of targets of the Arabidopsis sucrose nonfermenting-like kinase SnRK2.8 reveals a connection to metabolic processes. DOI: 10.1073/pnas.0610208104 ; PMID: 17404219
- Global analysis of Arabidopsis gene expression uncovers a complex array of changes impacting pathogen response and cell cycle during geminivirus infection. DOI: 10.1104/pp.108.121038 ; PMID: 18650403
- Identification of nuclear genes encoding chloroplast-localized proteins required for embryo development in Arabidopsis. DOI: 10.1104/pp.110.168120 ; PMID: 21139083
- Proteome and metabolome profiling of cytokinin action in Arabidopsis identifying and up-regulation. DOI: 10.1093/jxb/ert227 ; PMID: 24064926
- Endogenous Arabidopsis messenger RNAs transported to distant tissues. DOI: 10.1038/nplants.2015.25 ; PMID: 27247031
- Genome-wide identification of EMBRYO-DEFECTIVE (EMB) genes required for growth and development in Arabidopsis. DOI: 10.1111/nph.16071 ; PMID: 31334862
- Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis. DOI: 10.1021/pr034025j ; PMID: 12938931
- The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions. DOI: 10.1016/j.cub.2004.02.039 ; PMID: 15028209
- New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast, and versatile fractionation strategy. DOI: 10.1074/jbc.M406763200 ; PMID: 15322131
- High light response of the thylakoid proteome in arabidopsis wild type and the ascorbate-deficient mutant vtc2-2. A comparative proteomics study. DOI: 10.1104/pp.106.080150 ; PMID: 16648217
- A mutation in an Arabidopsis ribose 5-phosphate isomerase reduces cellulose synthesis and is rescued by exogenous uridine. DOI: 10.1111/j.1365-313X.2006.02902.x ; PMID: 17059404
- Modifications to the Arabidopsis defense proteome occur prior to significant transcriptional change in response to inoculation with Pseudomonas syringae. DOI: 10.1104/pp.106.086231 ; PMID: 17028151
- Sorting signals, N-terminal modifications and abundance of the chloroplast proteome. DOI: 10.1371/journal.pone.0001994 ; PMID: 18431481
- Quantitative proteomics of a chloroplast SRP54 sorting mutant and its genetic interactions with CLPC1 in Arabidopsis. DOI: 10.1104/pp.108.124545 ; PMID: 18633119
- The oligomeric stromal proteome of Arabidopsis thaliana chloroplasts. DOI: 10.1074/mcp.M500180-MCP200 ; PMID: 16207701
- Analysis of protein complexes in Arabidopsis leaves using size exclusion chromatography and label-free protein correlation profiling. DOI: 10.1016/j.jprot.2017.06.004 ; PMID: 28627464
Sequences:
cDNA Sequence
- >AT3G04790.1
AAGTCAAAAACCAAACCTTTCGATTTCATTTTATTTCTTCTCCAACCATTCTCAATCCTCTCTCTCCAATGGCTTCCTTATCCTTCGTTTCCTCTTCTCACCTTACGCTACGCACTCCTTCTATTGCCCTACGCAGCACTGGCTCTTCTCCTCGAACCTCCGTTTCATTCTCCGTCAAGGCTCAATCCGTCGCGCTTTCACAGGACGATTTGAAGAAGCTCGCGGCGGAGAAAGCTGTGGAGGCAATTAAACCTGGGATGGTTCTAGGGCTCGGAACCGGATCCACCGCAGCTTTCGCTGTTGATCAGATCGGGAAACTACTCTCTTCCGGTGAACTCTACGATATTGTCGGTATCCCAACGTCGAAACGAACGGAGGAACAAGCACGGTCGTTAGGGATTCCTCTTGTTGGGTTAGATACACATCCGAGAATCGATCTCGCTATTGACGGAGCAGACGAGGTAGATCCGAATCTTGATTTAGTCAAAGGTCGTGGAGGTGCTCTTCTCCGTGAGAAAATGGTGGAAGCTGTGGCTGACAAGTTTATTGTTGTGGCTGATGATACCAAACTCGTTACAGGACTCGGTGGAAGTGGATTAGCTATGCCGGTGGAAGTTGTTCAATTCTGCTGGAACTTTAATTTGATTAGATTGCAAGACCTCTTCAAGGAATTTGGATGTGAATCAAAGCTTAGAGTTGATGGTGATGGCAAGCCTTATGTGACTGATAACAGTAATTACATTATTGATTTGTATTTTAAGACTCCTTTGAAGGATGGATTCGCTGCGGCTAAAGAGATTGGGAAGTTTCAAGGAGTGGTGGAGCATGGTCTGTTTCTCGGAATGGCTACTTCTGTCATTATCGCTGGAAAGAATGGCGTTGAAGTTATGACCAAGTGAGGTTAAAAGTTCAATCTTTCTCTTCTTCTTTGATTGACAAATTTTTCTCCTTTGTAAAATTATCAATTGAGTTTTTATGTGAGATCATTTCAA
CDS Sequence
- >AT3G04790.1
ATGGCTTCCTTATCCTTCGTTTCCTCTTCTCACCTTACGCTACGCACTCCTTCTATTGCCCTACGCAGCACTGGCTCTTCTCCTCGAACCTCCGTTTCATTCTCCGTCAAGGCTCAATCCGTCGCGCTTTCACAGGACGATTTGAAGAAGCTCGCGGCGGAGAAAGCTGTGGAGGCAATTAAACCTGGGATGGTTCTAGGGCTCGGAACCGGATCCACCGCAGCTTTCGCTGTTGATCAGATCGGGAAACTACTCTCTTCCGGTGAACTCTACGATATTGTCGGTATCCCAACGTCGAAACGAACGGAGGAACAAGCACGGTCGTTAGGGATTCCTCTTGTTGGGTTAGATACACATCCGAGAATCGATCTCGCTATTGACGGAGCAGACGAGGTAGATCCGAATCTTGATTTAGTCAAAGGTCGTGGAGGTGCTCTTCTCCGTGAGAAAATGGTGGAAGCTGTGGCTGACAAGTTTATTGTTGTGGCTGATGATACCAAACTCGTTACAGGACTCGGTGGAAGTGGATTAGCTATGCCGGTGGAAGTTGTTCAATTCTGCTGGAACTTTAATTTGATTAGATTGCAAGACCTCTTCAAGGAATTTGGATGTGAATCAAAGCTTAGAGTTGATGGTGATGGCAAGCCTTATGTGACTGATAACAGTAATTACATTATTGATTTGTATTTTAAGACTCCTTTGAAGGATGGATTCGCTGCGGCTAAAGAGATTGGGAAGTTTCAAGGAGTGGTGGAGCATGGTCTGTTTCTCGGAATGGCTACTTCTGTCATTATCGCTGGAAAGAATGGCGTTGAAGTTATGACCAAGTGA
Protein Sequence
- >AT3G04790.1
MASLSFVSSSHLTLRTPSIALRSTGSSPRTSVSFSVKAQSVALSQDDLKKLAAEKAVEAIKPGMVLGLGTGSTAAFAVDQIGKLLSSGELYDIVGIPTSKRTEEQARSLGIPLVGLDTHPRIDLAIDGADEVDPNLDLVKGRGGALLREKMVEAVADKFIVVADDTKLVTGLGGSGLAMPVEVVQFCWNFNLIRLQDLFKEFGCESKLRVDGDGKPYVTDNSNYIIDLYFKTPLKDGFAAAKEIGKFQGVVEHGLFLGMATSVIIAGKNGVEVMTK