O22609 · DEGP1_ARATH
- ProteinProtease Do-like 1, chloroplastic
- GeneDEGP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids439 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Serine protease that is required at high temperature. May be involved in the degradation of damaged proteins. In vivo, can degrade beta-casein.
Activity regulation
Inhibited by phenylmethylsulfonyl fluoride and O-phenanthroline.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 173 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 203 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 282 | Charge relay system | ||||
Sequence: S |
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 | chloroplast | |
Cellular Component | chloroplast thylakoid | |
Cellular Component | chloroplast thylakoid membrane | |
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Cellular Component | thylakoid | |
Cellular Component | thylakoid lumen | |
Molecular Function | identical protein binding | |
Molecular Function | serine-type endopeptidase activity | |
Molecular Function | serine-type peptidase activity | |
Biological Process | photosystem II repair | |
Biological Process | protein catabolic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProtease Do-like 1, chloroplastic
- EC number
- 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 accessionO22609
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Plastid, chloroplast thylakoid membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 282 | Loss of activity. | ||||
Sequence: S → G |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 25 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | ?-105 | Thylakoid | ||||
Sequence: MATTTSCSLLLSSTLFLHSPPSSHLSFFNLSSSRSSPISLYPIRSKRYFRILSKLSLNDNNRDDDDDTLHFTPFSAVKPFFLLCTSVALSFSLFAASPAVESASA | ||||||
Transit peptide | 1-? | Chloroplast | ||||
Chain | PRO_0000026940 | 106-439 | Protease Do-like 1, chloroplastic | |||
Sequence: FVVSTPKKLQTDELATVRLFQENTPSVVYITNLAVRQDAFTLDVLEVPQGSGSGFVWDKQGHIVTNYHVIRGASDLRVTLADQTTFDAKVVGFDQDKDVAVLRIDAPKNKLRPIPVGVSADLLVGQKVFAIGNPFGLDHTLTTGVISGLRREISSAATGRPIQDVIQTDAAINPGNSGGPLLDSSGTLIGINTAIYSPSGASSGVGFSIPVDTVGGIVDQLVRFGKVTRPILGIKFAPDQSVEQLGVSGVLVLDAPPSGPAGKAGLQSTKRDGYGRLVLGDIITSVNGTKVSNGSDLYRILDQCKVGDEVTVEVLRGDHKEKISVTLEPKPDES |
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with PTAC16 and other potential targets for degradation under high light conditions.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O22609 | DEGP1 O22609 | 2 | EBI-2895934, EBI-2895934 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 154-323 | Serine protease | ||||
Sequence: QGSGSGFVWDKQGHIVTNYHVIRGASDLRVTLADQTTFDAKVVGFDQDKDVAVLRIDAPKNKLRPIPVGVSADLLVGQKVFAIGNPFGLDHTLTTGVISGLRREISSAATGRPIQDVIQTDAAINPGNSGGPLLDSSGTLIGINTAIYSPSGASSGVGFSIPVDTVGGIV | ||||||
Domain | 326-423 | PDZ | ||||
Sequence: LVRFGKVTRPILGIKFAPDQSVEQLGVSGVLVLDAPPSGPAGKAGLQSTKRDGYGRLVLGDIITSVNGTKVSNGSDLYRILDQCKVGDEVTVEVLRGD |
Sequence similarities
Belongs to the peptidase S1C family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length439
- Mass (Da)46,674
- Last updated2004-08-16 v2
- Checksum05EB437DCE71A251
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 12-25 | in Ref. 1 | ||||
Sequence: SSTLFLHSPPSSHL → HSPPSSQLSNST | ||||||
Sequence conflict | 38 | in Ref. 1; AAC39436 | ||||
Sequence: I → V | ||||||
Sequence conflict | 56 | in Ref. 1; AAC39436 | ||||
Sequence: S → P | ||||||
Sequence conflict | 62 | in Ref. 1; AAC39436 | ||||
Sequence: R → G | ||||||
Sequence conflict | 66 | in Ref. 1; AAC39436 | ||||
Sequence: D → G | ||||||
Sequence conflict | 70-71 | in Ref. 1; AAC39436 | ||||
Sequence: HF → LL | ||||||
Sequence conflict | 357 | in Ref. 1; AAC39436 | ||||
Sequence: V → L | ||||||
Sequence conflict | 383 | in Ref. 1; AAC39436 | ||||
Sequence: V → I | ||||||
Sequence conflict | 418 | in Ref. 1; AAC39436 | ||||
Sequence: E → Q |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF028842 EMBL· GenBank· DDBJ | AAC39436.1 EMBL· GenBank· DDBJ | mRNA | ||
AP000371 EMBL· GenBank· DDBJ | BAB02539.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP001302 EMBL· GenBank· DDBJ | BAB02539.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE77381.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | ANM63717.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY039585 EMBL· GenBank· DDBJ | AAK62640.1 EMBL· GenBank· DDBJ | mRNA | ||
AY113073 EMBL· GenBank· DDBJ | AAM47381.1 EMBL· GenBank· DDBJ | mRNA |