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Protein

Endoplasmic reticulum chaperone BiP

Gene
N/A
Organism
Plasmodium falciparum
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

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
Taxonomic identifieri5833 [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
ChainiPRO_0000078664‹1 – 279Endoplasmic reticulum chaperone BiPAdd BLAST›279

Proteomic databases

PRIDEiP12794

Structurei

3D structure databases

ProteinModelPortaliP12794
SMRiP12794
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni24 – 123Substrate-binding (SBD)By similarityAdd BLAST100

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi276 – 279Prevents secretion from ERPROSITE-ProRule annotation4

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiKOG0100 Eukaryota
COG0443 LUCA

Family and domain databases

Gene3Di1.20.1270.10, 1 hit
2.60.34.10, 1 hit
InterProiView protein in InterPro
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

Sequencei

Sequence statusi: Fragment.

P12794-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
EFFNGKEPNR GINPDEAVAY GAAIQAGIIL GEELQDVVLL DVTPLTLGIE
60 70 80 90 100
TVGGIMTQLI KRNTVIPTKK SQTFSTYQDN QPAVLIQVFE GERALTKDNH
110 120 130 140 150
LLGKFELSGI PPAQRGVPKI EVTFTVDKNG ILHVEAEDKG TGKSRGITIT
160 170 180 190 200
NDKGRLSKEQ IEKMINDAEK FADEDKNLRE KVEAKNNLDN YIQSMKATVE
210 220 230 240 250
DKDKLADKIE KEDKNTILSA VKDAEDWLNN NSNADSEALK QKLKDLEAVC
260 270
QPIIVKLYGQ PGGPSPQPSG DEDVDSDEL
Length:279
Mass (Da):30,657
Last modified:October 1, 1989 - v1
Checksum:iE0F8A52FECB6544F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18836 mRNA Translation: AAA29502.1

Similar proteinsi

Entry informationi

Entry nameiBIP_PLAFA
AccessioniPrimary (citable) accession number: P12794
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: April 25, 2018
This is version 94 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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