Q8S8I4 · EPF1_ARATH
- ProteinProtein EPIDERMAL PATTERNING FACTOR 1
- GeneEPF1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids104 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Controls stomatal patterning. Regulates asymmetric cell division during guard cell differentiation. Mediates stomatal development inhibition. Not cleaved by the protease CRSP (AC Q9LNU1) (PubMed:25043023).
MEPF1: mobile signal controlling stomatal development in a non-cell-autonomous manner (PubMed:22241782).
Uses ERL1 as major receptor (PubMed:22241782).
May act by competing with somatogen (AC Q9SV72) for the same receptor, TMM (AC Q9SSD1) (PubMed:22027592).
MEPF1: mobile signal controlling stomatal development in a non-cell-autonomous manner (PubMed:22241782).
Uses ERL1 as major receptor (PubMed:22241782).
May act by competing with somatogen (AC Q9SV72) for the same receptor, TMM (AC Q9SSD1) (PubMed:22027592).
GO annotations
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Biological Process | negative regulation of stomatal complex development | |
Biological Process | stomatal complex development | |
Biological Process | stomatal complex patterning |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameProtein EPIDERMAL PATTERNING FACTOR 1
- Cleaved into 1 chains
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ8S8I4
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Increased stomatal density and violation of the one-cell-spacing rule (clustering of stomata).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 5 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MKSLLLLAFFLSFFFGSLLA | ||||||
Chain | PRO_0000392497 | 21-104 | Protein EPIDERMAL PATTERNING FACTOR 1 | |||
Sequence: RHLPTSSHPSHHHVGMTGALKRQRRRPDTVQVAGSRLPDCSHACGSCSPCRLVMVSFVCASVEEAETCPMAYKCMCNNKSYPVP | ||||||
Chain | PRO_0000430505 | 53-104 | MEPF1 | |||
Sequence: AGSRLPDCSHACGSCSPCRLVMVSFVCASVEEAETCPMAYKCMCNNKSYPVP | ||||||
Disulfide bond | 60↔94 | |||||
Sequence: CSHACGSCSPCRLVMVSFVCASVEEAETCPMAYKC | ||||||
Disulfide bond | 64↔70 | |||||
Sequence: CGSCSPC | ||||||
Disulfide bond | 67↔96 | |||||
Sequence: CSPCRLVMVSFVCASVEEAETCPMAYKCMC | ||||||
Disulfide bond | 79↔88 | |||||
Sequence: CASVEEAETC | ||||||
Glycosylation | 98 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in shoots, but not in roots. Mostly localized in developing leaves, specifically in meristemoids, guard mother cells (GMCs), and young guard cells.
Induction
Not induced by high CO2.
Gene expression databases
Structure
Family & Domains
Sequence similarities
Belongs to the plant cysteine rich small secretory peptide family. Epidermal patterning factor subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length104
- Mass (Da)11,444
- Last updated2002-06-01 v1
- Checksum1B7FC910706F78C1
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC006234 EMBL· GenBank· DDBJ | AAM15214.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC07090.1 EMBL· GenBank· DDBJ | Genomic DNA |