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   02-SEP-2026, entry version 118.
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:Q05866};
DE            Short=GRP-78 homolog {ECO:0000250|UniProtKB:Q05866};
DE            Short=Pfgrp {ECO:0000250|UniProtKB:Q05866};
DE   AltName: Full=Binding-immunoglobulin protein homolog {ECO:0000250|UniProtKB:P11021};
DE            Short=BiP {ECO:0000250|UniProtKB:P11021};
DE   AltName: Full=Heat shock protein 70-2 {ECO:0000303|PubMed:3282854};
DE            Short=Pfhsp70-2 {ECO:0000303|PubMed:3282854};
DE   Flags: Fragment;
GN   Name=BIP {ECO:0000250|UniProtKB:A0A509AJG0};
OS   Plasmodium falciparum.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Laverania.
OX   NCBI_TaxID=5833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=Isolate NF7 {ECO:0000312|EMBL:AAA29502.1};
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 + phosphate + H(+); 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   -!- SUBUNIT: Interacts with PK4; the interaction is disrupted in response
CC       to stress. {ECO:0000250|UniProtKB:A0A509AJG0}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:A0A509AJG0}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during the asexual blood stage;
CC       expression starts in trophozoites and increases in schizonts and
CC       merozoites (at protein level). {ECO:0000269|PubMed:3282854}.
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   EnsemblProtists; PF3D7_0917900.1; PF3D7_0917900.1-p1; 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:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR   FunFam; 2.60.34.10:FF:000002; Heat shock 70 kDa; 1.
DR   FunFam; 1.20.1270.10:FF:000023; Heat shock protein 70; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 2.60.34.10; Substrate Binding Domain Of DNAk, Chain A, domain 1; 1.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   1: Evidence at protein 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   COMPBIAS        270..279
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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
//