BIP_PLAFO
ID BIP_PLAFO Reviewed; 655 AA.
AC Q05866;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 97.
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: Precursor;
OS Plasmodium falciparum (isolate NF54).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5843;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1484559; DOI=10.1016/0166-6851(92)90187-o;
RA Kumar N., Zheng H.;
RT "Nucleotide sequence of a Plasmodium falciparum stress protein with
RT similarity to mammalian 78-kDa glucose-regulated protein.";
RL Mol. Biochem. Parasitol. 56:353-356(1992).
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; L02822; AAA29623.1; -; Genomic_DNA.
DR PIR; A48468; A48468.
DR AlphaFoldDB; Q05866; -.
DR SMR; Q05866; -.
DR PRIDE; Q05866; -.
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 CDD; cd10241; HSPA5-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR042050; BIP_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
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 SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Endoplasmic reticulum; Hydrolase;
KW Nucleotide-binding; Signal; Stress response.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..655
FT /note="Endoplasmic reticulum chaperone BiP"
FT /id="PRO_0000013575"
FT REGION 124..278
FT /note="Nucleotide-binding (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 400..499
FT /note="Substrate-binding (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 633..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 652..655
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT BINDING 36..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 225..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 291..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 362..365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
SQ SEQUENCE 655 AA; 72776 MW; 4957A9CE9D725996 CRC64;
MNQIRPYILL LIVSLLKFIS AVDSNIEGPV IGIDLGTTYS CVGVFKNGRV EILNNELGNR
ITPSYVSFVD GERKVGEAAK LEATVHPTQT VFDVKRLIGR KFDDQEVVKD RSLLPYEIVN
NQGKPNIKVQ IKDKDTTFAP EQISAMVLEK MKEIAQSFLG KPVKNAVVTV PAYFNDAQRQ
ATKDAGTIAG LNIVRIIINQ PTAAALAYAL DKKEETSILV YDLGGGTFDV SILVIDNGVF
EVYATAGNTH LGGEDFDQRV MDYFIKMFKK KNNIDLRTDK RAIQKLRKEV EIAKRNLSVV
HSTQIEIEDI VEGHNFSETL TRAKFEELND DLFRETLEPV KKVLDDAKYE KSKIDEIVLV
GGSTRIPKIQ QIIKEFEFFN GKEPNRGINP DEAVAYGAAI QAGIILGEEL QDVVLLDVTP
LTLGIETVGG IMTQLIKRNT VIPTKKSQTF STYQDNQPAV LIQVFEGERA LTKDNHLLGK
FELSGIPPAQ RGVPKIEVTF TVDKNGILHV EAEDKGTGKS RGITITNDKG RLSKEQIEKM
INDAEKFADE DKNLREKVEA KNKLDNYIQS MKATVEDKDK LADKIEKEDK NTILSAVKDA
EDWLNNNSNA DSEALKQKLK DLEAVCQPII VKLYGQPGGP SPQPSGDEDV DSDEL
