Information report for AT5G06140
Gene Details
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Functional Descriptions
- PO:0009005 — root — raíz (Spanish, exact), radices (exact, plural), radix (exact), 根 (Japanese, exact), aerial root (narrow), climbing root (narrow)
- GO:0008333 — acts upstream of or within — endosome to lysosome transport
- GO:0048364 — acts upstream of or within — root development
- GO:0006623 — acts upstream of or within — protein targeting to vacuole
- GO:0006896 — acts upstream of or within — Golgi to vacuole transport
- GO:0030904 — part of — retromer complex
- GO:0005515 — enables — protein binding
- GO:0005768 — is active in — endosome
- GO:0009958 — acts upstream of or within — positive gravitropism
- GO:0043231 — located in — intracellular membrane-bounded organelle
- GO:0035091 — enables — phosphatidylinositol binding
- GO:0009507 — located in — chloroplast
- GO:0005771 — located in — multivesicular body
- GO:0016020 — located in — membrane
- GO:0005886 — located in — plasma membrane
- GO:0005768 — located in — endosome
Literature and News
- The maize genome contains a helitron insertion. DOI: 10.1105/tpc.008375 ; PMID: 12566579
- 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
- Learning the lipid language of plant signalling. DOI: 10.1016/j.tplants.2004.06.008 ; PMID: 15358268
- Genome-wide identification of genes expressed in Arabidopsis pistils specifically along the path of pollen tube growth. DOI: 10.1104/pp.105.060558 ; PMID: 15894741
- Comparative analyses of the gene expression profiles of Arabidopsis intact plant and cultured cells. DOI: 10.1007/s10529-005-8456-x ; PMID: 16132859
- Large-scale analysis of mRNA translation states during sucrose starvation in arabidopsis cells identifies cell proliferation and chromatin structure as targets of translational control. DOI: 10.1104/pp.106.079418 ; PMID: 16632591
- Plant retromer, localized to the prevacuolar compartment and microvesicles in Arabidopsis, may interact with vacuolar sorting receptors. DOI: 10.1105/tpc.105.035907 ; PMID: 16582012
- AtVPS29, a putative component of a retromer complex, is required for the efficient sorting of seed storage proteins. DOI: 10.1093/pcp/pcj103 ; PMID: 16926167
- AtSNX1 defines an endosome for auxin-carrier trafficking in Arabidopsis. DOI: 10.1038/nature05046 ; PMID: 16936718
- 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
- Differential degradation of PIN2 auxin efflux carrier by retromer-dependent vacuolar targeting. DOI: 10.1073/pnas.0808073105 ; PMID: 19004783
- Systems analysis of seed filling in Arabidopsis: using general linear modeling to assess concordance of transcript and protein expression. DOI: 10.1104/pp.109.152413 ; PMID: 20118269
- BLOS1, a putative BLOC-1 subunit, interacts with SNX1 and modulates root growth in Arabidopsis. DOI: 10.1242/jcs.069732 ; PMID: 20971704
- CLASP interacts with sorting nexin 1 to link microtubules and auxin transport via PIN2 recycling in Arabidopsis thaliana. DOI: 10.1016/j.devcel.2013.02.007 ; PMID: 23477787
- Phosphatidylinositol 3-Phosphate 5-Kinase, FAB1/PIKfyve Kinase Mediates Endosome Maturation to Establish Endosome-Cortical Microtubule Interaction in Arabidopsis. DOI: 10.1104/pp.15.01368 ; PMID: 26353760
- Differential Gene Expression and Protein Phosphorylation as Factors Regulating the State of the Arabidopsis SNX1 Protein Complexes in Response to Environmental Stimuli. DOI: 10.3389/fpls.2016.01456 ; PMID: 27725825
- The retromer, sorting nexins and the plant endomembrane protein trafficking. DOI: 10.1242/jcs.203695 ; PMID: 29061884
- The Inhibitor Endosidin 4 Targets SEC7 Domain-Type ARF GTPase Exchange Factors and Interferes with Subcellular Trafficking in Eukaryotes. DOI: 10.1105/tpc.18.00127 ; PMID: 30018156
- Interaction between VPS35 and RABG3f is necessary as a checkpoint to control fusion of late compartments with the vacuole. DOI: 10.1073/pnas.1905321116 ; PMID: 31570580
- Sorting Nexin1 negatively modulates phosphate uptake by facilitating Phosphate Transporter1;1 degradation in Arabidopsis. DOI: 10.1111/tpj.15778 ; PMID: 35436372
- Plant retromer, localized to the prevacuolar compartment and microvesicles in Arabidopsis, may interact with vacuolar sorting receptors. DOI: 10.1105/tpc.105.035907 ; PMID: 16582012
Gene Resources
- UniProt: A0A178UD05
- EMBL: CACRSJ010000110, CACSHJ010000096, LUHQ01000005
- AlphaFoldDB: A0A178UD05
- EnsemblPlants: AT5G06140.1
- Gramene: AT5G06140.1
- KEGG: ath:AT5G06140
- Orthologous matrix: LWETFLM
- ExpressionAtlas: AT5G06140
- InterPro: IPR001683, IPR015404, IPR027267
- PANTHER: PTHR10555, PTHR10555:SF170
- SUPFAM: SSF103657, SSF64268
- PROSITE: PS50195
- Gene3D: 1.20.1270.60, 3.30.1520.10
- OrthoDB: A0A178UD05
- SWISS-MODEL: A0A178UD05
- Conserved Domain Database: cd06859, cd07596
Sequences
cDNA Sequence
- >AT5G06140.1
AACCTTTCTCTTTTCAAAGGTTACTTACTTGTGCACCGAAAGTTGAACACAAAACTCGTGAATATTACAAATCTGCCACTAGAGGTGAATTTTTGACTAAATCGTTTTTTTTTTTTTTCGATCTCACGGGGTTGATTCTCGTTGTTGTCTCATGGAGAGCACGGAGCAGCCGAGGAACATCTCCGGATCGATGCAGAGCCCTAGATCTCCGTCTTCGCATCCGTATCTGTCAGTCTCCGTCACAGATCCTGTCAAATTAGGCAATGGCGTACAAGCTTATATCTCTTACAGAGTTATCACCAAGACTAACTTGCCGGAGTACCAAGGACCCGAGAAGATTGTTATTAGACGATACAGTGATTTCGTCTGGTTACGGGATCGGCTTTTTGAAAAGTACAAGGGCATTTTCATTCCTCCTCTTCCAGAGAAGAGTGCTGTAGAAAAATTCCGCTTTAGTGCCGAATTTATTGAAATGAGGCGAGCAGCATTGGATATATTTGTTAATCGAATAGCATTACACCCTGAGCTTCAGCAGAGTGAGGATCTTAGGACCTTTTTGCAAGCAGATGAAGAGACAATGGACAGATTCAGGTTTCAGGAAACTAGTATATTCAAGAAGCCTGCAGATCTAATGCAAATGTTTAGGGATGTCCAGTCAAAAGTTAGTGATGCTGTCCTTGGAAAAGAAAAACCTGTTGAAGAAACTACTGCTGACTACGAGAAGCTTAAACATTACATTTTCGAGCTTGAGAACCACTTGACTGAGGCTCAGAAGCATGCGTATCGCCTAGTCAAGAGGCATAGAGAGTTGGGTCAATCACTGTTGGATTTTGGCAAGGCTGTAAAACTTCTTGGGGCTTGTGAGGGTGAACCTACAGGAAAAGCATTTTCCGATCTTGGAACTAAATCTGAACTGTTATCGATTAAGCTCCAGAAAGAGGCTCAACAAGTCCTGATGAACTTCGAGGAACCCTTGAAGGACTATGTTCGTTATGTACAATCGATTAAGGCAACAATAGCAGAACGAGGCACTGCTTTCAAACAACATTGTGAATTGTCAGAAACAACAAAGTTAAAAGAAATAAATCTTGACAAACTCATGCTCACACGTTCAGACAAAGTAGGAGAAGCTGAGATCGAATACAGAGAGATAAAAGCAGAAAGTGAGGAAGCCACGAGAAGATTTGAGAGGATAGTAAAGAGAATGGAAGATGAGATAGTAAGGTTTCAAGAGCAGAAGACGGAAGAGATGGGAGTGGCATTCCATCAGTTTGCGAAAGGACAAGCTCGCTTAGCAAACAGTGTCGCGGATGCTTGGAGATCCCTTCTTCCCAAACTTGAAGCTTCTTATTCTGTCTAAATCCAAAACTAAACTTACCTGTGTCTGTGTGTGTTCCTTCATGAGAGGGTTTGTGTCTAGAGGCAGTTTGTTTTTGTGAGAAATTCTGGTGTTTTTTTGTCAACTTCAAGTTTAGTTAACTTGGCTTGTTTCCACTTGTAAAGAAGATACATATGCGTCATTATTACTCTCCTAAACGTTCATATAACAATTTTATTTTAGATTACAACTTTCCCAA
CDS Sequence
Protein Sequence