Gene Details:
- Gene ID: AT3G04120
- Gene Symbol: GAPC, GAPC-1, GAPC1
- Gene Name: GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE C SUBUNIT, glyceraldehyde-3-phosphate dehydrogenase C subunit 1
- Description: glyceraldehyde-3-phosphate dehydrogenase C subunit 1;(source:Araport11)
- TAIR Accession: locus:2103085
- Genome: Araport11_genome_release
- Species: Arabidopsis thaliana
Transcripts:
Plant Ontology Annotations:
- PO:0005020 — vascular bundle — haz vascular (Spanish, exact), vein (exact), 維管束 (Japanese, exact)
- PO:0025281 — pollen — polen (Spanish, exact), pollen grain (exact), 花粉 (Japanese, exact)
- PO:0025195 — pollen tube cell — célula del tubo polínico (Spanish, exact), 花粉管細胞 (Japanese, exact)
- PO:0000013 — cauline leaf — hoja caulinar (Spanish, exact), 茎生葉、茎葉 (Japanese, exact)
- PO:0000014 — rosette leaf — hoja en roseta (Spanish, exact), ロゼット葉 (Japanese, exact)
- PO:0006503 — fruit abscission zone — zona de absición del fruto (Spanish, exact), 落果実 (fruit shedding zone) (Japanese, exact)
- PO:0009046 — flower — flor (Spanish, exact), 花 (Japanese, exact), floret (related), Asteraceae floret (narrow), basal flower (narrow), double flower (narrow), hermaphrodite flower (narrow), monoclinous flower (narrow), perfect flower (narrow)
- PO:0025025 — root system — sistema de raíz (Spanish, exact), 根系 (Japanese, exact), root (broad)
- PO:0025297 — seedling radicle — radícula de la plántula (Spanish, exact), 実生幼根 (Japanese, exact)
- PO:0025471 — seedling cotyledon — NA
Gene Ontology:
- GO:0006096 — acts upstream of or within — glycolytic process
- GO:0005886 — located in — plasma membrane
- GO:0008886 — enables — glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity
- GO:0005829 — located in — cytosol
- GO:0010154 — acts upstream of or within — fruit development
- GO:0006094 — acts upstream of or within — gluconeogenesis
- GO:1901149 — enables — salicylic acid binding
- GO:0005740 — located in — mitochondrial envelope
- GO:0048316 — acts upstream of or within — seed development
- GO:0005634 — located in — nucleus
- GO:0005515 — enables — protein binding
- GO:0004365 — enables — glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
- GO:0009744 — acts upstream of or within — response to sucrose
- GO:0045893 — involved in — positive regulation of DNA-templated transcription
- GO:0006096 — involved in — glycolytic process
- GO:0042542 — acts upstream of or within — response to hydrogen peroxide
- GO:0009507 — located in — chloroplast
- GO:0009408 — acts upstream of or within — response to heat
- GO:0000325 — located in — plant-type vacuole
- GO:0005507 — enables — copper ion binding
- GO:0005739 — located in — mitochondrion
- GO:0005829 — is active in — cytosol
- GO:0051775 — acts upstream of or within — response to redox state
- GO:0009408 — involved in — response to heat
- GO:0006979 — acts upstream of or within — response to oxidative stress
- GO:0050661 — enables — NADP binding
- GO:0051287 — enables — NAD binding
- GO:0048046 — located in — apoplast
- GO:0005737 — located in — cytoplasm
Function-related keywords:
- vascular bundle , pollen , pollen tube cell , pollen , cauline leaf , rosette leaf , fruit abscission zone , flower , root system , seedling radicle , seedling cotyledon
Literature:
- Stress responses and metabolic regulation of glyceraldehyde-3-phosphate dehydrogenase genes in Arabidopsis. DOI: 10.1104/pp.101.1.209 ; PMID: 8278495
- Cloning and chromosomal mapping of nuclear genes encoding chloroplast and cytosolic glyceraldehyde-3-phosphate-dehydrogenase from Arabidopsis thaliana. DOI: 10.1016/0378-1119(92)90290-6 ; PMID: 1398114
- Intron existence predated the divergence of eukaryotes and prokaryotes. DOI: 10.1126/science.3055302 ; PMID: 3055302
- The impact of oxidative stress on Arabidopsis mitochondria. DOI: 10.1046/j.1365-313x.2002.01474.x ; PMID: 12492832
- Global expression profiling of sulfur-starved Arabidopsis by DNA macroarray reveals the role of O-acetyl-l-serine as a general regulator of gene expression in response to sulfur nutrition. DOI: 10.1046/j.1365-313x.2003.01658.x ; PMID: 12609039
- a high-density colony array study (HDCA). DOI: 10.1046/j.1365-313x.2003.01847.x ; PMID: 12969430
- Enzymes of glycolysis are functionally associated with the mitochondrion in Arabidopsis cells. DOI: 10.1105/tpc.012500 ; PMID: 12953116
- PathMAPA: a tool for displaying gene expression and performing statistical tests on metabolic pathways at multiple levels for Arabidopsis. DOI: 10.1186/1471-2105-4-56 ; PMID: 14604444
- Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins. DOI: 10.1105/tpc.016055 ; PMID: 14671022
- Target proteins of the cytosolic thioredoxins in Arabidopsis thaliana. DOI: 10.1093/pcp/pch019 ; PMID: 14749482
- 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
- The effect of alpha-amanitin on the Arabidopsis seed proteome highlights the distinct roles of stored and neosynthesized mRNAs during germination. DOI: 10.1104/pp.103.036293 ; PMID: 15047896
- Proteomic analysis of the Arabidopsis cell wall reveals unexpected proteins with new cellular locations. DOI: 10.1042/BST0320524 ; PMID: 15157177
- Effectiveness of RNA interference in transgenic plants. DOI: 10.1016/j.febslet.2004.04.043 ; PMID: 15147899
- Salt cress. A halophyte and cryophyte Arabidopsis relative model system and its applicability to molecular genetic analyses of growth and development of extremophiles. DOI: 10.1104/pp.104.041723 ; PMID: 15247369
- Co-ordinated gene expression of photosynthetic glyceraldehyde-3-phosphate dehydrogenase, phosphoribulokinase, and CP12 in Arabidopsis thaliana. DOI: 10.1093/jxb/eri020 ; PMID: 15533878
- A proteomic approach to apoplastic proteins involved in cell wall regeneration in protoplasts of Arabidopsis suspension-cultured cells. DOI: 10.1093/pcp/pci089 ; PMID: 15769804
- Evaluation of two-dimensional electrophoresis and liquid chromatography–tandem mass spectrometry for tissue-specific protein profiling of laser-microdissected plant samples. DOI: 10.1002/elps.200410399 ; PMID: 15971193
- Identification of plant glutaredoxin targets. DOI: 10.1089/ars.2005.7.919 ; PMID: 15998247
- Patterns of protein oxidation in Arabidopsis seeds and during germination. DOI: 10.1104/pp.105.062778 ; PMID: 15908592
- Gene expression in response to endoplasmic reticulum stress in Arabidopsis thaliana. DOI: 10.1111/j.1742-4658.2005.04770.x ; PMID: 15978049
- Expressed sequence tags from the Yukon ecotype of Thellungiella reveal that gene expression in response to cold, drought and salinity shows little overlap. DOI: 10.1007/s11103-005-6163-6 ; PMID: 16021339
- Stress-induced protein S-glutathionylation in Arabidopsis. DOI: 10.1104/pp.104.058917 ; PMID: 16055689
- Extracellular ATP functions as an endogenous external metabolite regulating plant cell viability. DOI: 10.1105/tpc.105.036806 ; PMID: 16199612
- Proteome mapping of mature pollen of Arabidopsis thaliana. DOI: 10.1002/pmic.200402011 ; PMID: 16247729
- 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
- Towards the proteome of Brassica napus phloem sap. DOI: 10.1002/pmic.200500155 ; PMID: 16400686
- The early responses of Arabidopsis thaliana cells to cadmium exposure explored by protein and metabolite profiling analyses. DOI: 10.1002/pmic.200500543 ; PMID: 16502469
- Proteomic investigation of the effect of salicylic acid on Arabidopsis seed germination and establishment of early defense mechanisms. DOI: 10.1104/pp.106.082057 ; PMID: 16679420
- Characterization of an Arabidopsis thaliana mutant lacking a cytosolic non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase. DOI: 10.1007/s11103-006-0060-5 ; PMID: 16927206
- Integration of metabolite with transcript and enzyme activity profiling during diurnal cycles in Arabidopsis rosettes. DOI: 10.1186/gb-2006-7-8-R76 ; PMID: 16916443
- EST database for early flower development in California poppy (Eschscholzia californica Cham., Papaveraceae) tags over 6,000 genes from a basal eudicot. DOI: 10.1007/s11103-006-9025-y ; PMID: 16915518
- Proteomic analysis of seed dormancy in Arabidopsis. DOI: 10.1104/pp.106.087452 ; PMID: 17028149
- Regulation of telomerase in Arabidopsis by BT2, an apparent target of TELOMERASE ACTIVATOR1. DOI: 10.1105/tpc.106.044321 ; PMID: 17220202
- Alternative and effective proteomic analysis in Arabidopsis. DOI: 10.1002/pmic.200700346 ; PMID: 17828791
- Recent advances in plant cell wall proteomics. DOI: 10.1002/pmic.200700938 ; PMID: 18210371
- Arabidopsis SCARs function interchangeably to meet actin-related protein 2/3 activation thresholds during morphogenesis. DOI: 10.1105/tpc.107.055350 ; PMID: 18424615
- Functional characterization of the Arabidopsis ubiquitin-specific protease gene family reveals specific role and redundancy of individual members in development. DOI: 10.1111/j.1365-313X.2008.03557.x ; PMID: 18485060
- 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
- Quantitative proteomics of a chloroplast SRP54 sorting mutant and its genetic interactions with CLPC1 in Arabidopsis. DOI: 10.1104/pp.108.124545 ; PMID: 18633119
- Characterization of Arabidopsis lines deficient in GAPC-1, a cytosolic NAD-dependent glyceraldehyde-3-phosphate dehydrogenase. DOI: 10.1104/pp.108.128769 ; PMID: 18820081
- MATERNALLY EXPRESSED PAB C-TERMINAL, a novel imprinted gene in Arabidopsis, encodes the conserved C-terminal domain of polyadenylate binding proteins. DOI: 10.1105/tpc.108.061929 ; PMID: 18796636
- Transcriptome analyses show changes in gene expression to accompany pollen germination and tube growth in Arabidopsis. DOI: 10.1104/pp.108.126375 ; PMID: 18775970
- Divalent metal ions in plant mitochondria and their role in interactions with proteins and oxidative stress-induced damage to respiratory function. DOI: 10.1104/pp.109.147942 ; PMID: 20018591
- Alteration of mitochondrial protein complexes in relation to metabolic regulation under short-term oxidative stress in Arabidopsis seedlings. DOI: 10.1016/j.phytochem.2010.11.003 ; PMID: 21146842
- In vivo protein tyrosine nitration in Arabidopsis thaliana. DOI: 10.1093/jxb/err042 ; PMID: 21378116
- Identification of lipids and lipid-binding proteins in phloem exudates from Arabidopsis thaliana. DOI: 10.1093/jxb/ers028 ; PMID: 22442409
- Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro. DOI: 10.1042/BJ20120505 ; PMID: 22607208
- Cytosolic glyceraldehyde-3-phosphate dehydrogenases interact with phospholipase Dδ to transduce hydrogen peroxide signals in the Arabidopsis response to stress. DOI: 10.1105/tpc.111.094946 ; PMID: 22589465
- Identification of novel candidate phosphatidic acid-binding proteins involved in the salt-stress response of Arabidopsis thaliana roots. DOI: 10.1042/BJ20121639 ; PMID: 23323832
- Transfer of a Redox-Signal through the Cytosol by Redox-Dependent Microcompartmentation of Glycolytic Enzymes at Mitochondria and Actin Cytoskeleton. DOI: 10.3389/fpls.2012.00284 ; PMID: 23316205
- Structural and functional characteristics of cGMP-dependent methionine oxidation in Arabidopsis thaliana proteins. DOI: 10.1186/1478-811X-11-1 ; PMID: 23289948
- Phosphatidic acid binds to cytosolic glyceraldehyde-3-phosphate dehydrogenase and promotes its cleavage in Arabidopsis. DOI: 10.1074/jbc.M112.427229 ; PMID: 23504314
- Nuclear accumulation of cytosolic glyceraldehyde-3-phosphate dehydrogenase in cadmium-stressed Arabidopsis roots. DOI: 10.1104/pp.113.215194 ; PMID: 23569110
- Endogenous Arabidopsis messenger RNAs transported to distant tissues. DOI: 10.1038/nplants.2015.25 ; PMID: 27247031
- Receptor protein kinase FERONIA controls leaf starch accumulation by interacting with glyceraldehyde-3-phosphate dehydrogenase. DOI: 10.1016/j.bbrc.2015.07.132 ; PMID: 26232644
- Hydrogen Sulfide Regulates the Cytosolic/Nuclear Partitioning of Glyceraldehyde-3-Phosphate Dehydrogenase by Enhancing its Nuclear Localization. DOI: 10.1093/pcp/pcx056 ; PMID: 28444344
- Control of auxin-induced callus formation by bZIP59-LBD complex in Arabidopsis regeneration. DOI: 10.1038/s41477-017-0095-4 ; PMID: 29358751
- Over-expression of SINAL7 increases biomass and drought tolerance, and also delays senescence in Arabidopsis. DOI: 10.1016/j.jbiotec.2018.07.013 ; PMID: 30003973
- Two Arabidopsis Receptor-like Cytoplasmic Kinases SZE1 and SZE2 Associate with the ZAR1-ZED1 Complex and Are Required for Effector-Triggered Immunity. DOI: 10.1016/j.molp.2019.03.012 ; PMID: 30947022
- Nuclear moonlighting of cytosolic glyceraldehyde-3-phosphate dehydrogenase regulates Arabidopsis response to heat stress. DOI: 10.1038/s41467-020-17311-4 ; PMID: 32651385
- The Meloidogyne incognita Nuclear Effector MiEFF1 Interacts With Arabidopsis Cytosolic Glyceraldehyde-3-Phosphate Dehydrogenases to Promote Parasitism. DOI: 10.3389/fpls.2021.641480 ; PMID: 33897729
- Potassium transporter TRH1/KUP4 contributes to distinct auxin-mediated root system architecture responses. DOI: 10.1093/plphys/kiab472 ; PMID: 34633458
- The impact of oxidative stress on Arabidopsis mitochondria. DOI: 10.1046/j.1365-313x.2002.01474.x ; PMID: 12492832
- Enzymes of glycolysis are functionally associated with the mitochondrion in Arabidopsis cells. DOI: 10.1105/tpc.012500 ; PMID: 12953116
- Analysis of the Arabidopsis nuclear proteome and its response to cold stress. DOI: 10.1046/j.1365-313x.2003.01907.x ; PMID: 14617066
- Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins. DOI: 10.1105/tpc.016055 ; PMID: 14671022
- Evaluation of two-dimensional electrophoresis and liquid chromatography–tandem mass spectrometry for tissue-specific protein profiling of laser-microdissected plant samples. DOI: 10.1002/elps.200410399 ; PMID: 15971193
- Proteome mapping of mature pollen of Arabidopsis thaliana. DOI: 10.1002/pmic.200402011 ; PMID: 16247729
- The early responses of Arabidopsis thaliana cells to cadmium exposure explored by protein and metabolite profiling analyses. DOI: 10.1002/pmic.200500543 ; PMID: 16502469
- A proteomics dissection of Arabidopsis thaliana vacuoles isolated from cell culture. DOI: 10.1074/mcp.M600250-MCP200 ; PMID: 17151019
- Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis. DOI: 10.1074/mcp.M600429-MCP200 ; PMID: 17317660
- Membrane proteomic analysis of Arabidopsis thaliana using alternative solubilization techniques. DOI: 10.1021/pr060525b ; PMID: 17432890
- A high content in lipid-modified peripheral proteins and integral receptor kinases features in the arabidopsis plasma membrane proteome. DOI: 10.1074/mcp.M700099-MCP200 ; PMID: 17644812
- Comparative proteomic analysis of NaCl stress-responsive proteins in Arabidopsis roots. DOI: 10.1093/jxb/erm207 ; PMID: 17916636
- Identification by 2-D DIGE of apoplastic proteins regulated by oligogalacturonides in Arabidopsis thaliana. DOI: 10.1002/pmic.200700523 ; PMID: 18324730
- Sorting signals, N-terminal modifications and abundance of the chloroplast proteome. DOI: 10.1371/journal.pone.0001994 ; PMID: 18431481
- Arabidopsis SCARs function interchangeably to meet actin-related protein 2/3 activation thresholds during morphogenesis. DOI: 10.1105/tpc.107.055350 ; PMID: 18424615
- Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics; an oxidative stress case study. DOI: 10.1016/j.phytochem.2008.04.007 ; PMID: 18538804
- Structural and functional characteristics of cGMP-dependent methionine oxidation in Arabidopsis thaliana proteins. DOI: 10.1186/1478-811X-11-1 ; PMID: 23289948
- Identification of multiple salicylic acid-binding proteins using two high throughput screens. DOI: 10.3389/fpls.2014.00777 ; PMID: 25628632
- 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
- >AT3G04120.1
GACCCCTCCTCCACGTTCTTCTCTCTTTTAAATAACCTCTTCACGGAACCCTTCTCACTCACCTATCTCACTCTAAAATCTCTCTCTGCCAATCTCATCTTCAACCTCTCTCTAACTCTCGTTTTCGATTCTACAATGGCTGACAAGAAGATTAGGATCGGAATCAACGGATTCGGAAGAATTGGTCGTTTGGTTGCTAGAGTTGTTCTCCAGAGGGACGATGTTGAGCTCGTCGCTGTCAACGACCCCTTCATCACTACTGAGTACATGACCTACATGTTCAAGTACGACAGTGTTCACGGTCAATGGAAACACAATGAACTCAAGATCAAGGATGAGAAGACCCTTCTCTTCGGTGAGAAGCCAGTCACTGTTTTCGGCATCAGGAACCCTGAGGATATCCCATGGGCCGAGGCTGGAGCTGACTACGTTGTTGAGTCTACTGGTGTCTTCACTGACAAAGACAAGGCTGCAGCTCACTTGAAGGGTGGTGCCAAGAAGGTTGTTATCTCTGCCCCCAGCAAAGACGCTCCAATGTTTGTTGTTGGTGTCAACGAGCACGAATACAAGTCCGACCTTGACATTGTCTCCAACGCTAGCTGCACCACTAACTGCCTTGCTCCCCTTGCCAAGGTTATCAATGACAGATTTGGAATTGTTGAGGGTCTTATGACTACAGTCCACTCAATCACTGCTACTCAGAAGACTGTTGATGGGCCTTCAATGAAGGACTGGAGAGGTGGAAGAGCTGCTTCATTCAACATTATTCCCAGCAGCACTGGAGCTGCCAAGGCTGTCGGAAAGGTGCTTCCAGCTCTTAACGGAAAGTTGACTGGAATGTCTTTCCGTGTCCCAACCGTTGATGTCTCAGTTGTTGACCTTACTGTCAGACTCGAGAAAGCTGCTACCTACGATGAAATCAAAAAGGCTATCAAGGAGGAATCCGAAGGCAAACTCAAGGGAATCCTTGGATACACCGAGGATGATGTTGTCTCAACTGACTTCGTTGGCGACAACAGGTCGAGCATTTTTGACGCCAAGGCTGGAATTGCATTGAGCGACAAGTTTGTGAAATTGGTGTCATGGTACGACAACGAATGGGGTTACAGTTCCCGTGTGGTCGACTTGATCGTCCACATGTCAAAGGCCTAAGCTAAGAAGCAGATCTCGAATGATAGGGAGTGGAAAGTCATCTGTTCATCCCCTTTTATGGTCTGAATTTGTCGTTTTCGAATAAAATTTCTTTGAACTTGGAACTTTTTTTTTTTTTGGTTTTCTTAATTCTCATTCATGTGAGGTGATGGGAGTTTGTAGACCGATGTTTTACTGGAAGCCCTTTGTTTTTGGCTTTTGATATATTGAGTTAACGTTATGGTTTTCAATTTTGTTCCACTTCTCTTTTTAACTATATACTAAATCAAATCTGAACGAAAAATGAAACTAAATGAGCTCCCGTTGATGATGACGTAGCAAATCTAAGGAACTAGAGGTGTACACTTATTAATCTAGCTTCTTCTAGTTTTCGAATAAAAGTTTCTAAGTGGAACCTATATTTTATGTTTGCGATTCTCATTTATGCGAGTTTGTAGACTGATGTTTGAATGAAAAGTATTTCATGTTGCCTTTTGTTATTGATTCTTCTCAAAACATAAGAAATTCATTAACAGATGTGCGGTTTATAAAGACAACGAAATATGTGTTCATCTGTAAA
CDS Sequence
- >AT3G04120.1
ATGGCTGACAAGAAGATTAGGATCGGAATCAACGGATTCGGAAGAATTGGTCGTTTGGTTGCTAGAGTTGTTCTCCAGAGGGACGATGTTGAGCTCGTCGCTGTCAACGACCCCTTCATCACTACTGAGTACATGACCTACATGTTCAAGTACGACAGTGTTCACGGTCAATGGAAACACAATGAACTCAAGATCAAGGATGAGAAGACCCTTCTCTTCGGTGAGAAGCCAGTCACTGTTTTCGGCATCAGGAACCCTGAGGATATCCCATGGGCCGAGGCTGGAGCTGACTACGTTGTTGAGTCTACTGGTGTCTTCACTGACAAAGACAAGGCTGCAGCTCACTTGAAGGGTGGTGCCAAGAAGGTTGTTATCTCTGCCCCCAGCAAAGACGCTCCAATGTTTGTTGTTGGTGTCAACGAGCACGAATACAAGTCCGACCTTGACATTGTCTCCAACGCTAGCTGCACCACTAACTGCCTTGCTCCCCTTGCCAAGGTTATCAATGACAGATTTGGAATTGTTGAGGGTCTTATGACTACAGTCCACTCAATCACTGCTACTCAGAAGACTGTTGATGGGCCTTCAATGAAGGACTGGAGAGGTGGAAGAGCTGCTTCATTCAACATTATTCCCAGCAGCACTGGAGCTGCCAAGGCTGTCGGAAAGGTGCTTCCAGCTCTTAACGGAAAGTTGACTGGAATGTCTTTCCGTGTCCCAACCGTTGATGTCTCAGTTGTTGACCTTACTGTCAGACTCGAGAAAGCTGCTACCTACGATGAAATCAAAAAGGCTATCAAGGAGGAATCCGAAGGCAAACTCAAGGGAATCCTTGGATACACCGAGGATGATGTTGTCTCAACTGACTTCGTTGGCGACAACAGGTCGAGCATTTTTGACGCCAAGGCTGGAATTGCATTGAGCGACAAGTTTGTGAAATTGGTGTCATGGTACGACAACGAATGGGGTTACAGTTCCCGTGTGGTCGACTTGATCGTCCACATGTCAAAGGCCTAA
Protein Sequence
- >AT3G04120.1
MADKKIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHNELKIKDEKTLLFGEKPVTVFGIRNPEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGYSSRVVDLIVHMSKA