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Protein

Endoplasmic reticulum chaperone BiP

Gene
N/A
Organism
Plasmodium falciparum (isolate NF54)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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 sitei95ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi36 – 39ATPBy similarity4
Nucleotide bindingi225 – 227ATPBy similarity3
Nucleotide bindingi291 – 298ATPBy similarity8
Nucleotide bindingi362 – 365ATPBy similarity4

GO - Molecular functioni

Keywordsi

Molecular functionHydrolase
Biological processStress response
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 homologBy similarity
Short name:
GRP-78 homologBy similarity
Binding-immunoglobulin protein homologBy similarity
Short name:
BiPBy similarity
OrganismiPlasmodium falciparum (isolate NF54)
Taxonomic identifieri5843 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)

Subcellular locationi

  • Endoplasmic reticulum lumen By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000001357525 – 655Endoplasmic reticulum chaperone BiPAdd BLAST631

Proteomic databases

PRIDEiQ05866

Structurei

3D structure databases

ProteinModelPortaliQ05866
SMRiQ05866
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni124 – 278Nucleotide-binding (NBD)By similarityAdd BLAST155
Regioni400 – 499Substrate-binding (SBD)By similarityAdd BLAST100

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi652 – 655Prevents secretion from ERPROSITE-ProRule annotation4

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.

Q05866-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQIRPYILL LIVSLLKFIS AVDSNIEGPV IGIDLGTTYS CVGVFKNGRV
60 70 80 90 100
EILNNELGNR ITPSYVSFVD GERKVGEAAK LEATVHPTQT VFDVKRLIGR
110 120 130 140 150
KFDDQEVVKD RSLLPYEIVN NQGKPNIKVQ IKDKDTTFAP EQISAMVLEK
160 170 180 190 200
MKEIAQSFLG KPVKNAVVTV PAYFNDAQRQ ATKDAGTIAG LNIVRIIINQ
210 220 230 240 250
PTAAALAYAL DKKEETSILV YDLGGGTFDV SILVIDNGVF EVYATAGNTH
260 270 280 290 300
LGGEDFDQRV MDYFIKMFKK KNNIDLRTDK RAIQKLRKEV EIAKRNLSVV
310 320 330 340 350
HSTQIEIEDI VEGHNFSETL TRAKFEELND DLFRETLEPV KKVLDDAKYE
360 370 380 390 400
KSKIDEIVLV GGSTRIPKIQ QIIKEFEFFN GKEPNRGINP DEAVAYGAAI
410 420 430 440 450
QAGIILGEEL QDVVLLDVTP LTLGIETVGG IMTQLIKRNT VIPTKKSQTF
460 470 480 490 500
STYQDNQPAV LIQVFEGERA LTKDNHLLGK FELSGIPPAQ RGVPKIEVTF
510 520 530 540 550
TVDKNGILHV EAEDKGTGKS RGITITNDKG RLSKEQIEKM INDAEKFADE
560 570 580 590 600
DKNLREKVEA KNKLDNYIQS MKATVEDKDK LADKIEKEDK NTILSAVKDA
610 620 630 640 650
EDWLNNNSNA DSEALKQKLK DLEAVCQPII VKLYGQPGGP SPQPSGDEDV

DSDEL
Length:655
Mass (Da):72,776
Last modified:November 1, 1995 - v1
Checksum:i4957A9CE9D725996
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02822 Genomic DNA Translation: AAA29623.1
PIRiA48468

Similar proteinsi

Entry informationi

Entry nameiBIP_PLAFO
AccessioniPrimary (citable) accession number: Q05866
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 25, 2018
This is version 82 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