ID   BIP_PLAFA               Reviewed;         279 AA.
AC   P12794;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Endoplasmic reticulum chaperone BiP {ECO:0000250|UniProtKB:P11021};
DE            EC=3.6.4.10 {ECO:0000250|UniProtKB:P11021};
DE   AltName: Full=78 kDa glucose-regulated protein homolog {ECO:0000250|UniProtKB:P11021};
DE            Short=GRP-78 homolog {ECO:0000250|UniProtKB:P11021};
DE   AltName: Full=Binding-immunoglobulin protein homolog {ECO:0000250|UniProtKB:P11021};
DE            Short=BiP {ECO:0000250|UniProtKB:P11021};
DE   Flags: Fragment;
OS   Plasmodium falciparum.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3282854; DOI=10.1089/dna.1988.7.71;
RA   Peterson M.G., Crewther P.E., Thompson J.K., Corcoran L.M., Coppel R.L.,
RA   Brown G.V., Anders R.F., Kemp D.J.;
RT   "A second antigenic heat shock protein of Plasmodium falciparum.";
RL   DNA 7:71-78(1988).
CC   -!- FUNCTION: Endoplasmic reticulum chaperone that plays a key role in
CC       protein folding and quality control in the endoplasmic reticulum lumen.
CC       Involved in the correct folding of proteins and degradation of
CC       misfolded proteins (By similarity). Acts as a key repressor of the
CC       unfolded protein response (UPR) (By similarity).
CC       {ECO:0000250|UniProtKB:G3I8R9, ECO:0000250|UniProtKB:P11021,
CC       ECO:0000250|UniProtKB:P20029}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
CC         Evidence={ECO:0000250|UniProtKB:P11021};
CC   -!- ACTIVITY REGULATION: The chaperone activity is regulated by ATP-induced
CC       allosteric coupling of the nucleotide-binding (NBD) and substrate-
CC       binding (SBD) domains. In the ADP-bound and nucleotide-free (apo)
CC       states, the two domains have little interaction. In contrast, in the
CC       ATP-bound state the two domains are tightly coupled, which results in
CC       drastically accelerated kinetics in both binding and release of
CC       polypeptide substrates. J domain-containing co-chaperones stimulate the
CC       ATPase activity and are required for efficient substrate recognition.
CC       {ECO:0000250|UniProtKB:P11021}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000250|UniProtKB:P11021}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; M18836; AAA29502.1; -; mRNA.
DR   AlphaFoldDB; P12794; -.
DR   SMR; P12794; -.
DR   PRIDE; P12794; -.
DR   EnsemblProtists; CAD51861; CAD51861; PF3D7_0917900.
DR   VEuPathDB; PlasmoDB:PF3D7_0917900; -.
DR   VEuPathDB; PlasmoDB:Pf7G8-2_000266000; -.
DR   VEuPathDB; PlasmoDB:Pf7G8_090022800; -.
DR   VEuPathDB; PlasmoDB:PfCD01_090022300; -.
DR   VEuPathDB; PlasmoDB:PfDd2_090023000; -.
DR   VEuPathDB; PlasmoDB:PfGA01_090022200; -.
DR   VEuPathDB; PlasmoDB:PfGB4_090022900; -.
DR   VEuPathDB; PlasmoDB:PfGN01_090022800; -.
DR   VEuPathDB; PlasmoDB:PfHB3_090022600; -.
DR   VEuPathDB; PlasmoDB:PfIT_090022500; -.
DR   VEuPathDB; PlasmoDB:PfKE01_090022300; -.
DR   VEuPathDB; PlasmoDB:PfKH01_090022200; -.
DR   VEuPathDB; PlasmoDB:PfKH02_090022700; -.
DR   VEuPathDB; PlasmoDB:PfML01_090022400; -.
DR   VEuPathDB; PlasmoDB:PfNF135_090021600; -.
DR   VEuPathDB; PlasmoDB:PfNF166_090022000; -.
DR   VEuPathDB; PlasmoDB:PfNF54_090023100; -.
DR   VEuPathDB; PlasmoDB:PfSD01_090022900; -.
DR   VEuPathDB; PlasmoDB:PfSN01_090022500; -.
DR   VEuPathDB; PlasmoDB:PfTG01_090022300; -.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Endoplasmic reticulum; Hydrolase;
KW   Nucleotide-binding; Stress response.
FT   CHAIN           <1..279
FT                   /note="Endoplasmic reticulum chaperone BiP"
FT                   /id="PRO_0000078664"
FT   REGION          24..123
FT                   /note="Substrate-binding (SBD)"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   REGION          257..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           276..279
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   NON_TER         1
SQ   SEQUENCE   279 AA;  30657 MW;  E0F8A52FECB6544F CRC64;
     EFFNGKEPNR GINPDEAVAY GAAIQAGIIL GEELQDVVLL DVTPLTLGIE TVGGIMTQLI
     KRNTVIPTKK SQTFSTYQDN QPAVLIQVFE GERALTKDNH LLGKFELSGI PPAQRGVPKI
     EVTFTVDKNG ILHVEAEDKG TGKSRGITIT NDKGRLSKEQ IEKMINDAEK FADEDKNLRE
     KVEAKNNLDN YIQSMKATVE DKDKLADKIE KEDKNTILSA VKDAEDWLNN NSNADSEALK
     QKLKDLEAVC QPIIVKLYGQ PGGPSPQPSG DEDVDSDEL