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Protein

Endoplasmic reticulum chaperone BiP

Gene

GRP78

Organism
Echinococcus multilocularis (Fox tapeworm)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins (By similarity). Acts as a key repressor of the unfolded protein response (UPR) (By similarity).By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.By similarity

Enzyme regulationi

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 by HSPA5/BiP.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei96ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi36 – 39ATPBy similarity4
Nucleotide bindingi226 – 228ATPBy similarity3
Nucleotide bindingi292 – 299ATPBy similarity8
Nucleotide bindingi363 – 366ATPBy similarity4

GO - Molecular functioni

Keywordsi

Molecular functionHydrolase
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 protein homolog1 Publication
Short name:
GRP-78 homolog1 Publication
Binding-immunoglobulin protein homologBy similarity
Short name:
BiPBy similarity
Gene namesi
Name:GRP781 Publication
OrganismiEchinococcus multilocularis (Fox tapeworm)
Taxonomic identifieri6211 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesCestodaEucestodaCyclophyllideaTaeniidaeEchinococcus

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 – 20Sequence analysisAdd BLAST20
ChainiPRO_000001357421 – 649Endoplasmic reticulum chaperone BiPAdd BLAST629

Proteomic databases

PRIDEiQ24895

Structurei

3D structure databases

ProteinModelPortaliQ24895
SMRiQ24895
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni125 – 279Nucleotide-binding (NBD)By similarityAdd BLAST155
Regioni399 – 499Substrate-binding (SBD)By similarityAdd BLAST101

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi646 – 649Prevents secretion from ER4

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Keywords - Domaini

Signal

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.

Q24895-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLSTYVGTF LLCILTLSHC KSGKEEYGTV IGIDLGTTYS CVGVFKNGRV
60 70 80 90 100
EIIANDQGNR ITPSYVAFSG DGERLIGDAA KNQLTSNPKN TLFDAKRLIG
110 120 130 140 150
RDYDDKDVQG DIKRYPFKVI NKNNKPYMKV QVGSEEKGFA PEEVSAMVLS
160 170 180 190 200
KMKEIAEAYL GTEVTHAVVT VPAYFNDAQR QATKDAGAIA GLTVLRIINE
210 220 230 240 250
PTAAAIAYGL DKKDTEKNIL VFDLGGGTFD VSLLTIDNGV FEVVATSGDT
260 270 280 290 300
HLGGEDFDQR LIDYFVKLYK KKEGKDITKD DRAVQKLRRE VEKAKRTLST
310 320 330 340 350
EHSTMIEIDN LFEGKDFSEP LTRARFEELN NDLFRSTLKP VMKVMEDSGL
360 370 380 390 400
KKEDIDDIVL VGGSTRIPKI QQLVKEFFNV KEPSRGINPD EAVAYGAAVQ
410 420 430 440 450
AGVISGVEDT GDIVLLDVCP LTMGIETVGG VMTKLIPRNT VIPTKKSQIF
460 470 480 490 500
STAADNQPTV TIQVFEGERP MTKDNHFLGK FDLTGIPPAP RGLPQIEVTF
510 520 530 540 550
EIDVNGILRV SAEDKGTGKK SNIVINKETN RLTPEEIERM IQDAEKFSDQ
560 570 580 590 600
DKQVKERVEV RNDLESLAYS IKNQVKDKEK MGGKLSDDEI KTIEDAADEA
610 620 630 640
IKWMENNPQA ETSDYKKQKA NLESVVQPIV SKLYEGAAPP TESTPKEEL
Length:649
Mass (Da):71,675
Last modified:November 1, 1996 - v1
Checksum:i057E7D617D1D8418
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63604 mRNA Translation: AAC37258.1

Similar proteinsi

Entry informationi

Entry nameiBIP_ECHMU
AccessioniPrimary (citable) accession number: Q24895
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: November 1, 1996
Last modified: April 25, 2018
This is version 76 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health