P22010 · BIP_KLULA
- ProteinEndoplasmic reticulum chaperone BiP
- GeneGRP78
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids679 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis.
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Activity regulation
The chaperone activity is regulated by ATP-induced allosteric coupling of the nucleotide-binding (NBD) and substrate-binding (SBD) domains. In the ADP-bound and nucleotide-free (apo) states, the two domains have little interaction. In contrast, in the ATP-bound state the two domains are tightly coupled, which results in drastically accelerated kinetics in both binding and release of polypeptide substrates. J domain-containing co-chaperones stimulate the ATPase activity and are required for efficient substrate recognition.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 59-62 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GTTY | ||||||
Binding site | 118 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 248-250 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GGT | ||||||
Binding site | 314-321 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EKAKRSLS | ||||||
Binding site | 385-388 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GSTR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum chaperone complex | |
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | membrane | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent protein folding chaperone | |
Biological Process | endoplasmic reticulum unfolded protein response |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEndoplasmic reticulum chaperone BiP
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Kluyveromyces
Accessions
- Primary accessionP22010
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-43 | |||||
Sequence: MFSARKSSVGWLVSSLAVFYVLLAVIMPIALTGSQSSRVVARA | ||||||
Chain | PRO_0000013582 | 44-679 | Endoplasmic reticulum chaperone BiP | |||
Sequence: AEDHEDYGTVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVSFTDDERLIGDAAKNQAASNPKNTIFDIKRLIGLQYNDPTVQRDIKHLPYTVVNKGNKPYVEVTVKGEKKEFTPEEVSGMILGKMKQIAEDYLGKKVTHAVVTVPAYFNDAQRQATKDAGAIAGLNILRIVNEPTAAAIAYGLDKTEDEHQIIVYDLGGGTFDVSLLSIENGVFEVQATAGDTHLGGEDFDYKLVRHFAQLFQKKHDLDVTKNDKAMAKLKREAEKAKRSLSSQTSTRIEIDSFFNGIDFSETLTRAKFEELNLALFKKTLKPVEKVLKDSGLQKEDIDDIVLVGGSTRIPKVQQLLEKFFNGKKASKGINPDEAVAYGAAVQAGVLSGEEGVEDIVLLDVNALTLGIETTGGVMTPLIKRNTAIPTKKSQIFSTAVDNQKAVRIQVYEGERAMVKDNNLLGNFELSDIRAAPRGVPQIEVTFALDANGILTVSATDKDTGKSESITIANDKGRLSQDDIDRMVEEAEKYAAEDAKFKAKSEARNTFENFVHYVKNSVNGELAEIMDEDDKETVLDNVNESLEWLEDNSDVAEAEDFEEKMASFKESVEPILAKASASQGSTSGEGFEDEDDDDYFDDEL |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 147-301 | Nucleotide-binding (NBD) | ||||
Sequence: KPYVEVTVKGEKKEFTPEEVSGMILGKMKQIAEDYLGKKVTHAVVTVPAYFNDAQRQATKDAGAIAGLNILRIVNEPTAAAIAYGLDKTEDEHQIIVYDLGGGTFDVSLLSIENGVFEVQATAGDTHLGGEDFDYKLVRHFAQLFQKKHDLDVTK | ||||||
Region | 421-521 | Substrate-binding (SBD) | ||||
Sequence: VQAGVLSGEEGVEDIVLLDVNALTLGIETTGGVMTPLIKRNTAIPTKKSQIFSTAVDNQKAVRIQVYEGERAMVKDNNLLGNFELSDIRAAPRGVPQIEVT | ||||||
Region | 652-679 | Disordered | ||||
Sequence: AKASASQGSTSGEGFEDEDDDDYFDDEL | ||||||
Compositional bias | 664-679 | Acidic residues | ||||
Sequence: EGFEDEDDDDYFDDEL | ||||||
Motif | 676-679 | Prevents secretion from ER | ||||
Sequence: DDEL |
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.
- Length679
- Mass (Da)74,448
- Last updated1991-08-01 v1
- Checksum530BC47F3224E0F2
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 664-679 | Acidic residues | ||||
Sequence: EGFEDEDDDDYFDDEL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X54709 EMBL· GenBank· DDBJ | CAA38516.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CR382124 EMBL· GenBank· DDBJ | CAH00584.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift |