Q43607 · PRU1_PRUDU
- ProteinPrunin 1 Pru du 6
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids551 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Seed storage protein.
Temperature Dependence
Thermostable up to 77 degrees Celsius. Complete thermal denaturation at 90 degrees Celsius. Thermal stability decreases in the presence of a reducing agent, dithiothreitol (DTT). The acidic and basic chains have lower thermal stabilities than the native multimeric protein.
Features
Showing features for binding site.
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 | extraorganismal space | |
Molecular Function | metal ion binding | |
Molecular Function | nutrient reservoir activity | |
Biological Process | cotyledon development | |
Biological Process | protein hexamerization | |
Biological Process | seed development |
Keywords
- Molecular function
- Ligand
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePrunin 1 Pru du 6
- Short namesPru 1 Pru du 6
- Alternative names
- Cleaved into 2 chains
- Allergen namePru du 6
Organism names
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Rosales > Rosaceae > Amygdaloideae > Amygdaleae > Prunus
Accessions
- Primary accessionQ43607
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Allergenic properties
Causes an allergic reaction in human. Binds to IgE of patients allergic to almonds (Probable).
Keywords
- Disease
Protein family/group databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MAKAFVFSLCLLLVFNGCLA | ||||||
Chain | PRO_5007750930 | 21-367 | Prunin 1 Pru du 6 acidic chain | |||
Sequence: ARQSQLSPQNQCQLNQLQAREPDNRIQAEAGQIETWNFNQGDFQCAGVAASRITIQRNGLHLPSYSNAPQLIYIVQGRGVLGAVFSGCPETFEESQQSSQQGRQQEQEQERQQQQQGEQGRQQGQQEQQQERQGRQQGRQQQEEGRQQEQQQGQQGRPQQQQQFRQLDRHQKTRRIREGDVVAIPAGVAYWSYNDGDQELVAVNLFHVSSDHNQLDQNPRKFYLAGNPENEFNQQGQSQPRQQGEQGRPGQHQQPFGRPRQQEQQGNGNNVFSGFNTQLLAQALNVNEETARNLQGQNDNRNQIIQVRGNLDFVQPPRGRQEREHEERQQEQLQQERQQQGEQLMAN | ||||||
Disulfide bond | 32↔65 | |||||
Sequence: CQLNQLQAREPDNRIQAEAGQIETWNFNQGDFQC | ||||||
Disulfide bond | 108↔374 | Interchain (between acidic and basic chains) | ||||
Sequence: CPETFEESQQSSQQGRQQEQEQERQQQQQGEQGRQQGQQEQQQERQGRQQGRQQQEEGRQQEQQQGQQGRPQQQQQFRQLDRHQKTRRIREGDVVAIPAGVAYWSYNDGDQELVAVNLFHVSSDHNQLDQNPRKFYLAGNPENEFNQQGQSQPRQQGEQGRPGQHQQPFGRPRQQEQQGNGNNVFSGFNTQLLAQALNVNEETARNLQGQNDNRNQIIQVRGNLDFVQPPRGRQEREHEERQQEQLQQERQQQGEQLMANGLEETFC | ||||||
Chain | PRO_0000448060 | 368-551 | Prunin 1 Pru du 6 basic chain | |||
Sequence: GLEETFCSLRLKENIGNPERADIFSPRAGRISTLNSHNLPILRFLRLSAERGFFYRNGIYSPHWNVNAHSVVYVIRGNARVQVVNENGDAILDQEVQQGQLFIVPQNHGVIQQAGNQGFEYFAFKTEENAFINTLAGRTSFLRALPDEVLANAYQISREQARQLKYNRQETIALSSSQQRRAVV |
Post-translational modification
Proteolytically processed from a single precursor to produce an acidic and a basic chain that are linked by a disulfide bond.
Keywords
- PTM
Expression
Tissue specificity
Expressed in seed (at protein level) (PubMed:18097098, PubMed:18553996, PubMed:19374443).
Expressed in seed (PubMed:7865791).
Expressed in seed (PubMed:7865791).
Developmental stage
Expressed during seed development. Expressed in cotyledons 110 and 120 days after flowering (DAF). Not expressed in pericarp, root of 30-day germinating plantlet or young leaf.
Interaction
Subunit
Hexamer of two trimers; each subunit is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond.
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 37-312 | Cupin type-1 1 | ||||
Sequence: LQAREPDNRIQAEAGQIETWNFNQGDFQCAGVAASRITIQRNGLHLPSYSNAPQLIYIVQGRGVLGAVFSGCPETFEESQQSSQQGRQQEQEQERQQQQQGEQGRQQGQQEQQQERQGRQQGRQQQEEGRQQEQQQGQQGRPQQQQQFRQLDRHQKTRRIREGDVVAIPAGVAYWSYNDGDQELVAVNLFHVSSDHNQLDQNPRKFYLAGNPENEFNQQGQSQPRQQGEQGRPGQHQQPFGRPRQQEQQGNGNNVFSGFNTQLLAQALNVNEETAR | ||||||
Compositional bias | 111-186 | Polar residues | ||||
Sequence: TFEESQQSSQQGRQQEQEQERQQQQQGEQGRQQGQQEQQQERQGRQQGRQQQEEGRQQEQQQGQQGRPQQQQQFRQ | ||||||
Region | 111-194 | Disordered | ||||
Sequence: TFEESQQSSQQGRQQEQEQERQQQQQGEQGRQQGQQEQQQERQGRQQGRQQQEEGRQQEQQQGQQGRPQQQQQFRQLDRHQKTR | ||||||
Region | 238-293 | Disordered | ||||
Sequence: NPRKFYLAGNPENEFNQQGQSQPRQQGEQGRPGQHQQPFGRPRQQEQQGNGNNVFS | ||||||
Compositional bias | 248-293 | Polar residues | ||||
Sequence: PENEFNQQGQSQPRQQGEQGRPGQHQQPFGRPRQQEQQGNGNNVFS | ||||||
Region | 329-360 | Disordered | ||||
Sequence: GNLDFVQPPRGRQEREHEERQQEQLQQERQQQ | ||||||
Compositional bias | 337-353 | Basic and acidic residues | ||||
Sequence: PRGRQEREHEERQQEQL | ||||||
Motif | 367-372 | NGXEET; peptidase recognition motif | ||||
Sequence: NGLEET | ||||||
Domain | 380-529 | Cupin type-1 2 | ||||
Sequence: ENIGNPERADIFSPRAGRISTLNSHNLPILRFLRLSAERGFFYRNGIYSPHWNVNAHSVVYVIRGNARVQVVNENGDAILDQEVQQGQLFIVPQNHGVIQQAGNQGFEYFAFKTEENAFINTLAGRTSFLRALPDEVLANAYQISREQAR |
Sequence similarities
Belongs to the 11S seed storage protein (globulins) family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length551
- Mass (Da)63,017
- Last updated1996-11-01 v1
- Checksum70D93418A222BA8F
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 111-186 | Polar residues | ||||
Sequence: TFEESQQSSQQGRQQEQEQERQQQQQGEQGRQQGQQEQQQERQGRQQGRQQQEEGRQQEQQQGQQGRPQQQQQFRQ | ||||||
Compositional bias | 248-293 | Polar residues | ||||
Sequence: PENEFNQQGQSQPRQQGEQGRPGQHQQPFGRPRQQEQQGNGNNVFS | ||||||
Compositional bias | 337-353 | Basic and acidic residues | ||||
Sequence: PRGRQEREHEERQQEQL |
Keywords
- Technical term