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BIP_ECHGR
ID   BIP_ECHGR               Reviewed;         651 AA.
AC   Q24798;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
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 granulosus (Hydatid tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC   Echinococcus granulosus group.
OX   NCBI_TaxID=6210;
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; M63605; AAC37259.1; -; mRNA.
DR   AlphaFoldDB; Q24798; -.
DR   SMR; Q24798; -.
DR   PRIDE; Q24798; -.
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..651
FT                   /note="Endoplasmic reticulum chaperone BiP"
FT                   /id="PRO_0000013573"
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           648..651
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   651 AA;  71921 MW;  E98DC737F54A16B4 CRC64;
     MGLSTYVGIF LLCILTLSRC KSGKEEYGTV IGIDLGTTYS CVGVFKNGRV EIIANDQGNR
     ITPSYVAFSG DGERLIGDAA KNQLTSNPKN TLFDAKRLIG RDYHDKDVQG DIKRYPFKVI
     NKNNKPYMKV QVGSEEKGFA PEEVSAMVLS KMKEIAEAYL GTEVTHAVVT VPAYFNDAQR
     QATKDAGAIA GLTVLRIINE PTAAAIAYGL EKKDTEKNIL VFDLGGGTFD VSLLTIDNGV
     FEVVATSGDT HLGGEDFDQR LIDYFVKLYK KKEGKDITKD DRAVQKLRRE VEKAKRTLST
     EHSTMIEIDN LFEGKDFSEP LTRARFEELN NDLFRSTLKP VMKVMEDSGL KKEDIDDIVL
     VGGSTRIPKI QQLVKEFFNG KEPIRGINPD EAVAYGAAVQ AGVISGVEDT GDIVLLDVCP
     LTMGIETVGG VMTKLIPRNT VIPTKKSQIF STAADNQPTV TIQVFEGERP MTKDNHFLGK
     FDLTGIPPAP RGLPQIEVTF EIDVNGILRV SAEDKGTGKK SNIVINKETN RITPEEIERM
     IQDAEKFSDQ DKQVKERVEV RNDLESLAYS IKNQVKDKEK MGGKLSDDEI KTIEDAADEA
     IKWMENNPQA ETSDYKKQKA NLESVVQPIV SKLYEGAAPP PPTESTPKEE L
 
 
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