P92990 · PGL3_ARATH
- ProteinPolygalacturonase 1 beta-like protein 3
- GenePGL3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids626 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Involved in cell size determination. May serve as a chaperone for expansins through the secretory pathway.
Miscellaneous
Unlike the tomato GP1, the BURP domain of AtPGL3 is not cleaved when the protein is secreted to the cell wall.
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | apoplast | |
Cellular Component | plant-type cell wall | |
Biological Process | cell wall modification involved in multidimensional cell growth | |
Biological Process | plant-type cell wall modification |
Names & Taxonomy
Protein names
- Recommended namePolygalacturonase 1 beta-like protein 3
- Short namesAtPGL3
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionP92990
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Slightly reduced size of the plant. Atpgl1, atpgl2 and atpgl3 triple mutants produce smaller leaves and petioles.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 42 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MLKQFLLLQSFSFFLFNVVIVGG | ||||||
Chain | PRO_0000042954 | 24-626 | Polygalacturonase 1 beta-like protein 3 | |||
Sequence: RTFGGGFSAEENPFTPKASLVRYWNKEIRGQSPRSEFLISKASPLNAVDSATFSKLAAANSLPTRFPDFCSAANLFCFPDLGASLEKHDDDVKFSVYDQKNFTNYGNARAGGADSFKNYSKDGNVVTDSFRRYSRNAAGHDDKFTVYGENSNVVEEGFNSYGTFGTGGAGDFTNYQNNVNNPTSRFTAYSDGGNGRSQTFKTYTHEANAGNGQSFTSYGKNGNGVPNEFTSYGVSSNVIGSGFSNYGESGNAANDTFTSYGSDGNVPQNNFNNYGASGNAAVDTFANYRDKANVGDDSFSSYAKDSNSEKVNFVNYGQSFNPGSETFTGYGKGAEGSKLSFKTYTPNSTFKDYAKKGVAFAKYNVSTTTANTVGDGKTVNKWIEPGKFFRESSLKEGTVIPMPDIKDKMPKRSFLPRSIITKLPFSTSKLGEIKRIFHAVENSTMGGIITDAVTECERPPSVGETKRCVGSAEDMIDFATSVLGRSVVLRTTENVAGSKEKVVIGKVNGINGGKLTKAVSCHQSLYPYLLYYCHSVPKVRVYEADLLELNSKKKINHGIAICHMDTSSWGPSHGAFLALGSKPGRIEVCHWIFENDMNWAIAD | ||||||
Glycosylation | 124 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 141 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 277 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 370 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 387 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 465 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in flowers and stems. Detected in trichomes, guard cells, root vascular tissue, root hairs, pollen sacs, sepals and styles of pistils.
Developmental stage
Barely detectable in 6 days after-germination (DAG) seedlings, but highly expressed in 14 DAG seedlings.
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 117-120 | FXXY 1 | ||||
Sequence: FSVY | ||||||
Repeat | 125-128 | FXXY 2 | ||||
Sequence: FTNY | ||||||
Repeat | 139-142 | FXXY 3 | ||||
Sequence: FKNY | ||||||
Repeat | 153-156 | FXXY 4 | ||||
Sequence: FRRY | ||||||
Repeat | 167-170 | FXXY 5 | ||||
Sequence: FTVY | ||||||
Repeat | 181-184 | FXXY 6 | ||||
Sequence: FNSY | ||||||
Repeat | 195-198 | FXXY 7 | ||||
Sequence: FTNY | ||||||
Repeat | 209-212 | FXXY 8 | ||||
Sequence: FTAY | ||||||
Repeat | 223-226 | FXXY 9 | ||||
Sequence: FKTY | ||||||
Repeat | 238-241 | FXXY 10 | ||||
Sequence: FTSY | ||||||
Repeat | 252-255 | FXXY 11 | ||||
Sequence: FTSY | ||||||
Repeat | 266-269 | FXXY 12 | ||||
Sequence: FSNY | ||||||
Repeat | 280-283 | FXXY 13 | ||||
Sequence: FTSY | ||||||
Repeat | 294-297 | FXXY 14 | ||||
Sequence: FNNY | ||||||
Repeat | 308-311 | FXXY 15 | ||||
Sequence: FANY | ||||||
Repeat | 322-325 | FXXY 16 | ||||
Sequence: FSSY | ||||||
Repeat | 336-339 | FXXY 17 | ||||
Sequence: FVNY | ||||||
Repeat | 350-353 | FXXY 18 | ||||
Sequence: FTGY | ||||||
Repeat | 364-367 | FXXY 19 | ||||
Sequence: FKTY | ||||||
Repeat | 373-376 | FXXY 20 | ||||
Sequence: FKDY | ||||||
Repeat | 383-386 | FXXY 21 | ||||
Sequence: FAKY | ||||||
Domain | 411-625 | BURP | ||||
Sequence: FFRESSLKEGTVIPMPDIKDKMPKRSFLPRSIITKLPFSTSKLGEIKRIFHAVENSTMGGIITDAVTECERPPSVGETKRCVGSAEDMIDFATSVLGRSVVLRTTENVAGSKEKVVIGKVNGINGGKLTKAVSCHQSLYPYLLYYCHSVPKVRVYEADLLELNSKKKINHGIAICHMDTSSWGPSHGAFLALGSKPGRIEVCHWIFENDMNWAIA |
Domain
The BURP domain located at the C-terminus has not been identified in non-plant proteins (PubMed:9790599).
It is critical for PGL3's role in cell growth (PubMed:26106400).
It is critical for PGL3's role in cell growth (PubMed:26106400).
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length626
- Mass (Da)68,060
- Last updated2005-11-22 v2
- ChecksumF324231B27D4B710
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 70 | in Ref. 6; AAN60310 | ||||
Sequence: A → S | ||||||
Sequence conflict | 242 | in Ref. 1; AAB39546 | ||||
Sequence: G → A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U63373 EMBL· GenBank· DDBJ | AAB39546.1 EMBL· GenBank· DDBJ | mRNA | ||
AC003671 EMBL· GenBank· DDBJ | AAC18803.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE35050.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE35051.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY056388 EMBL· GenBank· DDBJ | AAL08244.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
BT000514 EMBL· GenBank· DDBJ | AAN18083.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AK226888 EMBL· GenBank· DDBJ | BAE98965.1 EMBL· GenBank· DDBJ | mRNA | ||
AF083752 EMBL· GenBank· DDBJ | AAN60310.1 EMBL· GenBank· DDBJ | mRNA |