Q6Z7B0 · BIP1_ORYSJ

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).

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 annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentendoplasmic reticulum chaperone complex
Cellular Componentendoplasmic reticulum lumen
Cellular Componentmembrane
Cellular Componentnucleus
Cellular Componentplant-type vacuole membrane
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent protein folding chaperone
Molecular Functionheat shock protein binding
Molecular Functionprotein folding chaperone
Biological Processchaperone cofactor-dependent protein refolding
Biological Processendoplasmic reticulum unfolded protein response
Biological ProcessERAD pathway
Biological Processprotein folding in endoplasmic reticulum
Biological Processprotein refolding

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Heat shock 70 kDa protein BIP1
  • Alternative names
    • Luminal-binding protein 1
      (OsBiP1
      )

Gene names

    • Name
      BIP1
    • Synonyms
      BIP
    • ORF names
      OJ1442_E05.10
      , OsJ_05115
      , P0036E06.29
    • Ordered locus names
      Os02g0115900
      , LOC_Os02g02410

Organism names

  • Taxonomic identifier
  • Strains
    • cv. Ilpoombyeo
    • cv. Nipponbare
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa

Accessions

  • Primary accession
    Q6Z7B0
  • Secondary accessions
    • O24182

Proteomes

Genome annotation databases

Subcellular Location

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

PTM/Processing

Features

Showing features for signal, chain, modified residue (large scale data), glycosylation.

TypeIDPosition(s)SourceDescription
Signal1-25UniProt
ChainPRO_500817682526-665UniProtHeat shock 70 kDa protein BIP1
Modified residue (large scale data)524PTMeXchangePhosphothreonine
Glycosylation614UniProtN-linked (GlcNAc...) asparagine
Modified residue (large scale data)644PTMeXchangePhosphothreonine

Keywords

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).

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

Subunit

Interacts with P58A, P58B and ERDJ3B.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, motif.

TypeIDPosition(s)Description
Region641-665Disordered
Motif662-665Prevents secretion from ER

Sequence similarities

Belongs to the heat shock protein 70 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    665
  • Mass (Da)
    73,390
  • Last updated
    2004-07-05 v1
  • Checksum
    C6E587D999AB42F5
MDRVRGCAFLLGVLLAGSLFAFSVAKEETKKLGTVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVAFTDSERLIGEAAKNQAAVNPERTIFDVKRLIGRKFEDKEVQRDMKLVPYKIVNKDGKPYIQVKIKDGENKVFSPEEVSAMILGKMKETAEAYLGKKINDAVVTVPAYFNDAQRQATKDAGVIAGLNVARIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYFIKLIKKKYSKDISKDNRALGKLRREAERAKRALSNQHQVRVEIESLFDGTDFSEPLTRARFEELNNDLFRKTMGPVKKAMDDAGLEKSQIHEIVLVGGSTRIPKVQQLLRDYFEGKEPNKGVNPDEAVAYGAAVQGSILSGEGGDETKDILLLDVAPLTLGIETVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVSIQVFEGERSMTKDCRLLGKFDLSGIPAAPRGTPQIEVTFEVDANGILNVKAEDKGTGKSEKITITNEKGRLSQEEIDRMVREAEEFAEEDKKVKERIDARNQLETYVYNMKNTVGDKDKLADKLESEEKEKVEEALKEALEWLDENQTAEKEEYEEKLKEVEAVCNPIISAVYQRTGGAPGGGADGEGGVDDEHDEL

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0P0VDX8A0A0P0VDX8_ORYSJOs02g0115900445

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict7in Ref. 1; AAB63469
Sequence conflict102in Ref. 1; AAB63469
Sequence conflict109in Ref. 1; AAB63469
Sequence conflict127in Ref. 1; AAB63469
Sequence conflict651-658in Ref. 1; AAB63469

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp