Q53LQ0 · PDI11_ORYSJ
- ProteinProtein disulfide isomerase-like 1-1
- GenePDIL1-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids512 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Probable protein disulfide isomerase that plays an essential role in the segregation of proglutelin and prolamin polypeptides within the ER lumen of endosperm. Required to retain proglutelin in the cisternal ER lumen until ER export and, thereby, indirectly prevents heterotypic interactions with prolamin polypeptides.
Catalytic activity
Features
Showing features for active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 69 | Nucleophile | ||||
Sequence: C | ||||||
Site | 70 | Contributes to redox potential value | ||||
Sequence: G | ||||||
Site | 71 | Contributes to redox potential value | ||||
Sequence: H | ||||||
Active site | 72 | Nucleophile | ||||
Sequence: C | ||||||
Site | 137 | Lowers pKa of C-terminal Cys of first active site | ||||
Sequence: R | ||||||
Active site | 414 | Nucleophile | ||||
Sequence: C | ||||||
Site | 415 | Contributes to redox potential value | ||||
Sequence: G | ||||||
Site | 416 | Contributes to redox potential value | ||||
Sequence: H | ||||||
Active site | 417 | Nucleophile | ||||
Sequence: C | ||||||
Site | 477 | Lowers pKa of C-terminal Cys of second active site | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum lumen | |
Molecular Function | protein disulfide isomerase activity | |
Biological Process | endosperm development | |
Biological Process | protein folding | |
Biological Process | protein folding in endoplasmic reticulum | |
Biological Process | response to endoplasmic reticulum stress |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein disulfide isomerase-like 1-1
- EC number
- Short namesOsPDIL1-1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionQ53LQ0
- Secondary accessions
Proteomes
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Distributed asymmetrically within the cortical endoplasmic reticulum (ER) and largely restricted to the cisternal ER.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Accumulation of large quantities of glutelin precursor (proglutelin) in the endosperm.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-25 | UniProt | |||||
Sequence: MAISKAWISLLLALAVVLSAPAARA | |||||||
Chain | PRO_0000400028 | 26-512 | UniProt | Protein disulfide isomerase-like 1-1 | |||
Sequence: EEAAAAEEGGDAAAEAVLTLDADGFDEAVAKHPFMVVEFYAPWCGHCKKLAPEYEKAAQELSKHDPPIVLAKVDANDEKNKPLATKYEIQGFPTLKIFRNQGKNIQEYKGPREAEGIVEYLKKQVGPASKEIKSPEDATNLIDDKKIYIVGIFSELSGTEYTNFIEVAEKLRSDYDFGHTLHANHLPRGDAAVERPLVRLFKPFDELVVDSKDFDVTALEKFIDASSTPKVVTFDKNPDNHPYLLKFFQSSAAKAMLFLNFSTGPFESFKSVYYGAAEEFKDKEIKFLIGDIEASQGAFQYFGLREDQVPLIIIQDGESKKFLKAHVEPDQIVSWLKEYFDGKLSPFRKSEPIPEVNDEPVKVVVADNVHDFVFKSGKNVLVEFYAPWCGHCKKLAPILDEAATTLKSDKDVVIAKMDATANDVPSEFDVQGYPTLYFVTPSGKMVPYESGRTADEIVDFIKKNKETAGQAKEKAESAPAEPLKDEL | |||||||
Disulfide bond | 69↔72 | UniProt | Redox-active | ||||
Sequence: CGHC | |||||||
Glycosylation | 285 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 414↔417 | UniProt | Redox-active | ||||
Sequence: CGHC | |||||||
Modified residue (large scale data) | 502 | PTMeXchange | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
By dithiothreitol-induced endoplasmic reticulum (ER) stress response.
Developmental stage
Expressed in developing seeds from 3 to 9 days after anthesis.
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 32-151 | Thioredoxin 1 | ||||
Sequence: EEGGDAAAEAVLTLDADGFDEAVAKHPFMVVEFYAPWCGHCKKLAPEYEKAAQELSKHDPPIVLAKVDANDEKNKPLATKYEIQGFPTLKIFRNQGKNIQEYKGPREAEGIVEYLKKQVG | ||||||
Domain | 372-491 | Thioredoxin 2 | ||||
Sequence: FRKSEPIPEVNDEPVKVVVADNVHDFVFKSGKNVLVEFYAPWCGHCKKLAPILDEAATTLKSDKDVVIAKMDATANDVPSEFDVQGYPTLYFVTPSGKMVPYESGRTADEIVDFIKKNKE | ||||||
Region | 492-512 | Disordered | ||||
Sequence: TAGQAKEKAESAPAEPLKDEL | ||||||
Motif | 509-512 | Prevents secretion from ER | ||||
Sequence: KDEL |
Sequence similarities
Belongs to the protein disulfide isomerase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length512
- Mass (Da)56,855
- Last updated2005-05-24 v1
- Checksum60CA68E115728496
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0P0XZP3 | A0A0P0XZP3_ORYSJ | Os11g0199200 | 415 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 435 | in Ref. 2; AAX85991 | ||||
Sequence: K → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB373950 EMBL· GenBank· DDBJ | BAG50157.1 EMBL· GenBank· DDBJ | mRNA | ||
AY987391 EMBL· GenBank· DDBJ | AAX85991.1 EMBL· GenBank· DDBJ | mRNA | ||
AC139170 EMBL· GenBank· DDBJ | AAX96742.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DP000010 EMBL· GenBank· DDBJ | ABA91939.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DP000010 EMBL· GenBank· DDBJ | ABA91940.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP008217 EMBL· GenBank· DDBJ | BAF27799.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP014967 EMBL· GenBank· DDBJ | BAT13066.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CM000148 EMBL· GenBank· DDBJ | EAZ17736.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK068268 EMBL· GenBank· DDBJ | BAG90833.1 EMBL· GenBank· DDBJ | mRNA |