P22010 · BIP_KLULA

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

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.

TypeIDPosition(s)Description
Binding site59-62ATP (UniProtKB | ChEBI)
Binding site118ATP (UniProtKB | ChEBI)
Binding site248-250ATP (UniProtKB | ChEBI)
Binding site314-321ATP (UniProtKB | ChEBI)
Binding site385-388ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum chaperone complex
Cellular Componentendoplasmic reticulum lumen
Cellular Componentmembrane
Cellular Componentnucleus
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent protein folding chaperone
Biological Processendoplasmic reticulum unfolded protein response

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Endoplasmic reticulum chaperone BiP
  • EC number
  • Alternative names
    • Immunoglobulin heavy chain-binding protein homolog
      (BiP
      )

Gene names

    • Name
      GRP78
    • Synonyms
      BIP
    • Ordered locus names
      KLLA0D09559g

Organism names

Accessions

  • Primary accession
    P22010
  • Secondary accessions
    • Q6CRF1

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-43
ChainPRO_000001358244-679Endoplasmic reticulum chaperone BiP

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, motif.

TypeIDPosition(s)Description
Region147-301Nucleotide-binding (NBD)
Region421-521Substrate-binding (SBD)
Region652-679Disordered
Compositional bias664-679Acidic residues
Motif676-679Prevents 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
    679
  • Mass (Da)
    74,448
  • Last updated
    1991-08-01 v1
  • Checksum
    530BC47F3224E0F2
MFSARKSSVGWLVSSLAVFYVLLAVIMPIALTGSQSSRVVARAAEDHEDYGTVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVSFTDDERLIGDAAKNQAASNPKNTIFDIKRLIGLQYNDPTVQRDIKHLPYTVVNKGNKPYVEVTVKGEKKEFTPEEVSGMILGKMKQIAEDYLGKKVTHAVVTVPAYFNDAQRQATKDAGAIAGLNILRIVNEPTAAAIAYGLDKTEDEHQIIVYDLGGGTFDVSLLSIENGVFEVQATAGDTHLGGEDFDYKLVRHFAQLFQKKHDLDVTKNDKAMAKLKREAEKAKRSLSSQTSTRIEIDSFFNGIDFSETLTRAKFEELNLALFKKTLKPVEKVLKDSGLQKEDIDDIVLVGGSTRIPKVQQLLEKFFNGKKASKGINPDEAVAYGAAVQAGVLSGEEGVEDIVLLDVNALTLGIETTGGVMTPLIKRNTAIPTKKSQIFSTAVDNQKAVRIQVYEGERAMVKDNNLLGNFELSDIRAAPRGVPQIEVTFALDANGILTVSATDKDTGKSESITIANDKGRLSQDDIDRMVEEAEKYAAEDAKFKAKSEARNTFENFVHYVKNSVNGELAEIMDEDDKETVLDNVNESLEWLEDNSDVAEAEDFEEKMASFKESVEPILAKASASQGSTSGEGFEDEDDDDYFDDEL

Sequence caution

The sequence CAH00584.1 differs from that shown. Reason: Frameshift

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias664-679Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X54709
EMBL· GenBank· DDBJ
CAA38516.1
EMBL· GenBank· DDBJ
Genomic DNA
CR382124
EMBL· GenBank· DDBJ
CAH00584.1
EMBL· GenBank· DDBJ
Genomic DNA Frameshift

Genome annotation databases

Similar Proteins

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