ID   BIP_SOLLC               Reviewed;         666 AA.
AC   P49118;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Luminal-binding protein;
DE            Short=BiP;
DE   AltName: Full=78 kDa glucose-regulated protein homolog;
DE            Short=GRP-78;
DE   Flags: Precursor;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=cv. VFNT Cherry;
RA   Meyer D.J., Ewing N.N., Rosichan J.L., Bennett A.B.;
RT   "Characterization of the tomato endoplasmic reticulum-localized BiP/GRP78
RT   homolog.";
RL   Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probably plays a role in facilitating the assembly of
CC       multimeric protein complexes inside the ER.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; L08830; AAA34139.1; -; mRNA.
DR   EMBL; L08829; AAA99920.1; -; Genomic_DNA.
DR   AlphaFoldDB; P49118; -.
DR   SMR; P49118; -.
DR   STRING; 4081.Solyc08g082820.2.1; -.
DR   PaxDb; P49118; -.
DR   PRIDE; P49118; -.
DR   ProMEX; P49118; -.
DR   eggNOG; KOG0100; Eukaryota.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; P49118; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR   GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
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; Endoplasmic reticulum; Glycoprotein; Nucleotide-binding;
KW   Reference proteome; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..666
FT                   /note="Luminal-binding protein"
FT                   /id="PRO_0000013590"
FT   REGION          644..666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           663..666
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   CARBOHYD        617
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   666 AA;  73235 MW;  A2EB7C9459BD9FCC CRC64;
     MAACSRRGNS LVVLAIVLLG CLSALSNAKE EATKLGTVIG IDLGTTYSCV GVYKNGHVEI
     IANDQGNRIT PSWVAFTDNE RLIGEAAKNL AAVNPERTIF DVKRLIGRKF EDKEVQRDMK
     LVPYKIVSKD GKPYIQVKIK DGEVKVFSPE EISAMILTKM KETAEAFLGK TIKDAVVTVP
     AYFNDAQRQA TKDAGVIAGL NVARIINEPT AAAIAYGLDK KGGEKNILVF DLGGGTFDVS
     ILTIDNGVFE VLATNGDTHL GGEDFDQRIM EYFIKLIKKK HGKDISKDNR ALGKLRREAE
     RAKRSLSSQH QVRVEIESLF DGTDFSEPLT RARFEELNND LFRKTMGPVK KAMDDAGLQK
     NQIDEIVLVG GSTRIPKVQQ LLKDYFDGKE PSKGVNPDEA VAYGAAVQGG ILSGEGGDET
     KDILLLDVAP LTLGIETVGG VMTKFIPRNT VIPTKKSQVF TTYQDQQTTV SIQVFEGERS
     LTKDCRNLGK FDLTGIPPAP RGTPQIEVTF EVDANGILNV KAEDKGTGKA EKITITNDKG
     RLSQEEIERM VREAEEFAEE DKKVKEKIDA RNALETYVYN MKNQINDKDK LADKLESDEK
     EKIETATKEA LEWLDDNQSA EKEDYDEKLK EVEAVCNPII TAVYQRSGGA PGGGASEEED
     DSHDEL