BIP_ECHMU
ID BIP_ECHMU Reviewed; 649 AA.
AC Q24895;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 93.
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:0000303|PubMed:8719168};
DE Short=GRP-78 homolog {ECO:0000303|PubMed:8719168};
DE AltName: Full=Binding-immunoglobulin protein homolog {ECO:0000250|UniProtKB:P11021};
DE Short=BiP {ECO:0000250|UniProtKB:P11021};
DE Flags: Precursor;
GN Name=GRP78 {ECO:0000303|PubMed:8719168};
OS Echinococcus multilocularis (Fox tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX NCBI_TaxID=6211;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8719168; DOI=10.1016/0166-6851(95)02501-4;
RA Muhlschlegel F., Frosch P., Castro A., Apfel H., Muller A., Frosch M.;
RT "Molecular cloning and characterization of an Echinococcus multilocularis
RT and Echinococcus granulosus stress protein homologous to the mammalian 78
RT kDa glucose regulated protein.";
RL Mol. Biochem. Parasitol. 74:245-250(1995).
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; M63604; AAC37258.1; -; mRNA.
DR AlphaFoldDB; Q24895; -.
DR SMR; Q24895; -.
DR PRIDE; Q24895; -.
DR eggNOG; KOG0100; Eukaryota.
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 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Endoplasmic reticulum; Hydrolase;
KW Nucleotide-binding; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..649
FT /note="Endoplasmic reticulum chaperone BiP"
FT /id="PRO_0000013574"
FT REGION 125..279
FT /note="Nucleotide-binding (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 399..499
FT /note="Substrate-binding (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT MOTIF 646..649
FT /note="Prevents secretion from ER"
FT BINDING 36..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 226..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 292..299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 363..366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
SQ SEQUENCE 649 AA; 71675 MW; 057E7D617D1D8418 CRC64;
MGLSTYVGTF LLCILTLSHC KSGKEEYGTV IGIDLGTTYS CVGVFKNGRV EIIANDQGNR
ITPSYVAFSG DGERLIGDAA KNQLTSNPKN TLFDAKRLIG RDYDDKDVQG DIKRYPFKVI
NKNNKPYMKV QVGSEEKGFA PEEVSAMVLS KMKEIAEAYL GTEVTHAVVT VPAYFNDAQR
QATKDAGAIA GLTVLRIINE PTAAAIAYGL DKKDTEKNIL VFDLGGGTFD VSLLTIDNGV
FEVVATSGDT HLGGEDFDQR LIDYFVKLYK KKEGKDITKD DRAVQKLRRE VEKAKRTLST
EHSTMIEIDN LFEGKDFSEP LTRARFEELN NDLFRSTLKP VMKVMEDSGL KKEDIDDIVL
VGGSTRIPKI QQLVKEFFNV KEPSRGINPD EAVAYGAAVQ AGVISGVEDT GDIVLLDVCP
LTMGIETVGG VMTKLIPRNT VIPTKKSQIF STAADNQPTV TIQVFEGERP MTKDNHFLGK
FDLTGIPPAP RGLPQIEVTF EIDVNGILRV SAEDKGTGKK SNIVINKETN RLTPEEIERM
IQDAEKFSDQ DKQVKERVEV RNDLESLAYS IKNQVKDKEK MGGKLSDDEI KTIEDAADEA
IKWMENNPQA ETSDYKKQKA NLESVVQPIV SKLYEGAAPP TESTPKEEL
