ID   BIP8_TOBAC              Reviewed;         293 AA.
AC   Q03686;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Luminal-binding protein 8;
DE            Short=BiP 8;
DE   AltName: Full=78 kDa glucose-regulated protein homolog 8;
DE            Short=GRP-78-8;
DE   Flags: Fragment;
GN   Name=BIP8;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1822990; DOI=10.2307/3869163;
RA   Denecke J., Goldman M.H., Demolder J., Seurinck J., Botterman J.;
RT   "The tobacco luminal binding protein is encoded by a multigene family.";
RL   Plant Cell 3:1025-1035(1991).
RN   [2]
RP   ERRATUM OF PUBMED:1822990.
RA   Denecke J., Goldman M.H., Demolder J., Seurinck J., Botterman J.;
RL   Plant Cell 3:1251-1251(1991).
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; X60062; CAA42664.1; -; mRNA.
DR   PIR; S21881; S21881.
DR   AlphaFoldDB; Q03686; -.
DR   SMR; Q03686; -.
DR   STRING; 4097.Q03686; -.
DR   Proteomes; UP000084051; Unplaced.
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   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
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; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Endoplasmic reticulum; Glycoprotein; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           <1..293
FT                   /note="Luminal-binding protein 8"
FT                   /id="PRO_0000078669"
FT   REGION          270..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           290..293
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   CARBOHYD        244
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   293 AA;  32342 MW;  44939595E45650E6 CRC64;
     RIPKVQQLLK DYFDGKEPNK GVNPDEAVAY GAAVQGGILS GEGGDETKDI LLLDVAPLTL
     GIETVGGVMT KLIPRNTVIP SKKSQVFTTY QDQQTTVTIQ VFEGERSLTK DCRLLGKFDL
     TGIAPAPRGT PQIEVTFEVD ANGILNVKAE DKASGKSEKI TITNDKGRLS QEEIERMVKE
     AEEFAEEDKK VKERIDARNS LETYVYNMRN QINDKDKLAD KLESDEKEKI ETATKEALEW
     LDDNQSAEKE DYEEKLKEVE AVCNPIITAV YQKSGGAPGG ESGASEDDDH DEL