Q6Z7B0 · BIP1_ORYSJ
- ProteinHeat shock 70 kDa protein BIP1
- GeneBIP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids665 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Key chaperone involved in folding of secretory proteins in the endoplasmic reticulum (ER) lumen (Probable). Involved in ER quality control for seed storage proteins during seed maturation (PubMed:19567376, PubMed:21223397).
Functions as a sensor of the ER stress response, and provides suitable conditions for the production of secretory proteins by alleviating ER stress (PubMed:19567376, PubMed:21223397).
Functions as a sensor of the ER stress response, and provides suitable conditions for the production of secretory proteins by alleviating ER stress (PubMed:19567376, PubMed:21223397).
Miscellaneous
The kernels of the over-expressing transformant exhibit floury and shrunken features due to defects in seed storage proteins and starch synthesis.
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 | cytoplasm | |
Cellular Component | endoplasmic reticulum chaperone complex | |
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | membrane | |
Cellular Component | nucleus | |
Cellular Component | plant-type vacuole membrane | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent protein folding chaperone | |
Molecular Function | heat shock protein binding | |
Molecular Function | protein folding chaperone | |
Biological Process | chaperone cofactor-dependent protein refolding | |
Biological Process | endoplasmic reticulum unfolded protein response | |
Biological Process | ERAD pathway | |
Biological Process | protein folding in endoplasmic reticulum | |
Biological Process | protein refolding |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameHeat shock 70 kDa protein BIP1
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionQ6Z7B0
- Secondary accessions
Proteomes
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes close to the endoplasmic reticulum (ER) membrane complex of developing endosperm cells. Localizes to the periphery of the prolamine protein bodies which originate directly from the ER.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, modified residue (large scale data), glycosylation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-25 | UniProt | |||||
Sequence: MDRVRGCAFLLGVLLAGSLFAFSVA | |||||||
Chain | PRO_5008176825 | 26-665 | UniProt | Heat shock 70 kDa protein BIP1 | |||
Sequence: KEETKKLGTVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVAFTDSERLIGEAAKNQAAVNPERTIFDVKRLIGRKFEDKEVQRDMKLVPYKIVNKDGKPYIQVKIKDGENKVFSPEEVSAMILGKMKETAEAYLGKKINDAVVTVPAYFNDAQRQATKDAGVIAGLNVARIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYFIKLIKKKYSKDISKDNRALGKLRREAERAKRALSNQHQVRVEIESLFDGTDFSEPLTRARFEELNNDLFRKTMGPVKKAMDDAGLEKSQIHEIVLVGGSTRIPKVQQLLRDYFEGKEPNKGVNPDEAVAYGAAVQGSILSGEGGDETKDILLLDVAPLTLGIETVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVSIQVFEGERSMTKDCRLLGKFDLSGIPAAPRGTPQIEVTFEVDANGILNVKAEDKGTGKSEKITITNEKGRLSQEEIDRMVREAEEFAEEDKKVKERIDARNQLETYVYNMKNTVGDKDKLADKLESEEKEKVEEALKEALEWLDENQTAEKEEYEEKLKEVEAVCNPIISAVYQRTGGAPGGGADGEGGVDDEHDEL | |||||||
Modified residue (large scale data) | 524 | PTMeXchange | Phosphothreonine | ||||
Sequence: T | |||||||
Glycosylation | 614 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 644 | PTMeXchange | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
By dithiothreitol-induced endoplasmic reticulum (ER) stress response (PubMed:21223397, PubMed:24153418).
Induced by tunicamycin-induced ER stress response (PubMed:24153418).
Induced by tunicamycin-induced ER stress response (PubMed:24153418).
Developmental stage
During seed development, expressed from 5 to 20 days after flowering (DAF), with a peak at 10 DAF. Not expressed in mature seeds.
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 641-665 | Disordered | ||||
Sequence: YQRTGGAPGGGADGEGGVDDEHDEL | ||||||
Motif | 662-665 | Prevents secretion from ER | ||||
Sequence: HDEL |
Sequence similarities
Belongs to the heat shock protein 70 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length665
- Mass (Da)73,390
- Last updated2004-07-05 v1
- ChecksumC6E587D999AB42F5
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0P0VDX8 | A0A0P0VDX8_ORYSJ | Os02g0115900 | 445 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 7 | in Ref. 1; AAB63469 | ||||
Sequence: C → S | ||||||
Sequence conflict | 102 | in Ref. 1; AAB63469 | ||||
Sequence: L → D | ||||||
Sequence conflict | 109 | in Ref. 1; AAB63469 | ||||
Sequence: D → E | ||||||
Sequence conflict | 127 | in Ref. 1; AAB63469 | ||||
Sequence: D → I | ||||||
Sequence conflict | 651-658 | in Ref. 1; AAB63469 | ||||
Sequence: GADGEGGV → RRRGRL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF006825 EMBL· GenBank· DDBJ | AAB63469.1 EMBL· GenBank· DDBJ | mRNA | ||
EU267978 EMBL· GenBank· DDBJ | ACA50500.1 EMBL· GenBank· DDBJ | mRNA | ||
AP004121 EMBL· GenBank· DDBJ | BAD07713.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP004867 EMBL· GenBank· DDBJ | BAD07938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP008208 EMBL· GenBank· DDBJ | BAF07589.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP014958 EMBL· GenBank· DDBJ | BAS76651.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CM000139 EMBL· GenBank· DDBJ | EAZ21491.1 EMBL· GenBank· DDBJ | Genomic DNA |