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Protein

Endoplasmic reticulum chaperone BiP

Gene

HSPA5

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 (By similarity).By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.By similarity

Activity regulationi

The chaperone activity is regulated by ATP-induced allosteric coupling of the nucleotide-binding (NBD) and substrate-binding (SBD) domains (By similarity). In the ADP-bound and nucleotide-free (apo) states, the two domains have little interaction (By similarity). 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 (By similarity). J domain-containing co-chaperones (DNAJB9/ERdj4 or DNAJC10/ERdj5) stimulate the ATPase activity and are required for efficient substrate recognition by HSPA5/BiP. Homooligomerization inactivates participating HSPA5/BiP protomers and probably act as reservoirs to store HSPA5/BiP molecules when they are not needed by the cell (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei94ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi34 – 37ATPBy similarity4
Nucleotide bindingi225 – 227ATPBy similarity3
Nucleotide bindingi291 – 298ATPBy similarity8
Nucleotide bindingi362 – 365ATPBy similarity4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone, Hydrolase
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Endoplasmic reticulum chaperone BiPBy similarity (EC:3.6.4.10By similarity)
Alternative name(s):
78 kDa glucose-regulated proteinBy similarity
Short name:
GRP-78By similarity
Binding-immunoglobulin proteinBy similarity
Short name:
BiPBy similarity
Heat shock protein 70 family protein 5By similarity
Short name:
HSP70 family protein 5By similarity
Heat shock protein family A member 5By similarity
Immunoglobulin heavy chain-binding proteinBy similarity
Gene namesi
Name:HSPA5By similarity
Synonyms:GRP78By similarity
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 17

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16Sequence analysisAdd BLAST16
ChainiPRO_000001357017 – 652Endoplasmic reticulum chaperone BiPAdd BLAST636

Proteomic databases

PaxDbiQ90593
PRIDEiQ90593

Expressioni

Gene expression databases

BgeeiENSGALG00000001000 Expressed in 11 organ(s), highest expression level in liver

Interactioni

Subunit structurei

Monomer and homooligomer; homooligomerization via the interdomain linker inactivates the chaperone activity and acts as a storage of HSPA5/BiP molecules (By similarity). Interacts with DNAJC10 (By similarity). Interacts with DNAJB9/ERdj4; leading to recruit HSPA5/BiP to ERN1/IRE1. Interacts with ERN1/IRE1; interaction takes place following interaction with DNAJB9/ERdj4 and leads to inactivate ERN1/IRE1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
KCNMA1Q8AYS83EBI-1635886,EBI-1635766

GO - Molecular functioni

Protein-protein interaction databases

BioGridi676734, 3 interactors
IntActiQ90593, 1 interactor
STRINGi9031.ENSGALP00000001474

Structurei

3D structure databases

ProteinModelPortaliQ90593
SMRiQ90593
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni123 – 278Nucleotide-binding (NBD)By similarityAdd BLAST156
Regioni407 – 417Interdomain linkerBy similarityAdd BLAST11
Regioni418 – 498Substrate-binding (SBD)By similarityAdd BLAST81

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi649 – 652Prevents secretion from ERPROSITE-ProRule annotation4

Domaini

The interdomain linker regulates the chaperone activity by mediating the formation of homooligomers. Homooligomers are formed by engagement of the interdomain linker of one HSPA5/BiP molecule as a typical substrate of an adjacent HSPA5/BiP molecule. HSPA5/BiP oligomerization inactivates participating HSPA5/BiP protomers. HSPA5/BiP oligomers probably act as reservoirs to store HSPA5/BiP molecules when they are not needed by the cell. When the levels of unfolded proteins rise, cells can rapidly break up these oligomers to make active monomers.By similarity

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0101 Eukaryota
COG0443 LUCA
GeneTreeiENSGT00930000150862
HOGENOMiHOG000228135
HOVERGENiHBG051845
InParanoidiQ90593
KOiK09490
OMAiCVGVMQK
OrthoDBiEOG091G0352
PhylomeDBiQ90593
TreeFamiTF105044

Family and domain databases

Gene3Di1.20.1270.10, 1 hit
2.60.34.10, 1 hit
InterProiView protein in InterPro
IPR018181 Heat_shock_70_CS
IPR029048 HSP70_C_sf
IPR029047 HSP70_peptide-bd_sf
IPR013126 Hsp_70_fam
PANTHERiPTHR19375 PTHR19375, 1 hit
PfamiView protein in Pfam
PF00012 HSP70, 1 hit
PRINTSiPR00301 HEATSHOCK70
SUPFAMiSSF100920 SSF100920, 1 hit
SSF100934 SSF100934, 1 hit
PROSITEiView protein in PROSITE
PS00014 ER_TARGET, 1 hit
PS00297 HSP70_1, 1 hit
PS00329 HSP70_2, 1 hit
PS01036 HSP70_3, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q90593-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRHLLLALLL LGGARADDEE KKEDVGTVVG IDLGTTYSCV GVFKNGRVEI
60 70 80 90 100
IANDQGNRIT PSYVAFTPEG ERLIGDAAKN QLTSNPENTV FDAKRLIGRT
110 120 130 140 150
WNDPSVQQDI KYLPFKVVEK KAKPHIQVDV GGGQTKTFAP EEISAMVLTK
160 170 180 190 200
MKETAEAYLG KKVTHAVVTV PAYFNDAQRQ ATKDAGTIAG LNVMRIINEP
210 220 230 240 250
TAAAIAYGLD KREGEKNILV FDLGGGTFDV SLLTIDNGVF EVVATNGDTH
260 270 280 290 300
LGGEDFDQRV MEHFIKLYKK KTGKDVRKDN RAVQKLRREV EKAKRALSSQ
310 320 330 340 350
HQARIEIESF FEGEDFSETL TRAKFEELNM DLFRSTMKPV QKVLEDSDLK
360 370 380 390 400
KSDIDEIVLV GGSTRIPKIQ QLVKEFFNGK EPSRGINPDE AVAYGAAVQA
410 420 430 440 450
GVLSGDQDTG DLVLLDVCPL TLGIETVGGV MTKLIPRNTV VPTKKSQIFS
460 470 480 490 500
TASDNQPTVT IKVYEGERPL TKDNHLLGTF DLTGIPPAPR GVPQIEVTFE
510 520 530 540 550
IDVNGILRVT AEDKGTGNKN KITITNDQNR LTPEEIERMV NDAEKFAEED
560 570 580 590 600
KKLKERIDAR NELESYAYSL KNQIGDKEKL GGKLSSEDKE TIEKAVEEKI
610 620 630 640 650
EWLESHQDAD IEDFKSKKKE LEEVVQPIVS KLYGSAGPPP TGEEEAAEKD

EL
Length:652
Mass (Da):72,019
Last modified:November 1, 1996 - v1
Checksum:i4E4BB58A3EEFAF6F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27260 mRNA Translation: AAA48785.1
PIRiI50242
RefSeqiNP_990822.1, NM_205491.1
UniGeneiGga.4219

Genome annotation databases

EnsembliENSGALT00000001476; ENSGALP00000001474; ENSGALG00000001000
GeneIDi396487
KEGGigga:396487

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27260 mRNA Translation: AAA48785.1
PIRiI50242
RefSeqiNP_990822.1, NM_205491.1
UniGeneiGga.4219

3D structure databases

ProteinModelPortaliQ90593
SMRiQ90593
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676734, 3 interactors
IntActiQ90593, 1 interactor
STRINGi9031.ENSGALP00000001474

Proteomic databases

PaxDbiQ90593
PRIDEiQ90593

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000001476; ENSGALP00000001474; ENSGALG00000001000
GeneIDi396487
KEGGigga:396487

Organism-specific databases

CTDi3309

Phylogenomic databases

eggNOGiKOG0101 Eukaryota
COG0443 LUCA
GeneTreeiENSGT00930000150862
HOGENOMiHOG000228135
HOVERGENiHBG051845
InParanoidiQ90593
KOiK09490
OMAiCVGVMQK
OrthoDBiEOG091G0352
PhylomeDBiQ90593
TreeFamiTF105044

Miscellaneous databases

PROiPR:Q90593

Gene expression databases

BgeeiENSGALG00000001000 Expressed in 11 organ(s), highest expression level in liver

Family and domain databases

Gene3Di1.20.1270.10, 1 hit
2.60.34.10, 1 hit
InterProiView protein in InterPro
IPR018181 Heat_shock_70_CS
IPR029048 HSP70_C_sf
IPR029047 HSP70_peptide-bd_sf
IPR013126 Hsp_70_fam
PANTHERiPTHR19375 PTHR19375, 1 hit
PfamiView protein in Pfam
PF00012 HSP70, 1 hit
PRINTSiPR00301 HEATSHOCK70
SUPFAMiSSF100920 SSF100920, 1 hit
SSF100934 SSF100934, 1 hit
PROSITEiView protein in PROSITE
PS00014 ER_TARGET, 1 hit
PS00297 HSP70_1, 1 hit
PS00329 HSP70_2, 1 hit
PS01036 HSP70_3, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiBIP_CHICK
AccessioniPrimary (citable) accession number: Q90593
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: November 7, 2018
This is version 132 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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