ID   BIP_SPIOL               Reviewed;         668 AA.
AC   Q42434;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
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;
GN   Name=HSC70;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Bloomsdale; TISSUE=Leaf;
RX   PubMed=8115556; DOI=10.1104/pp.104.1.303;
RA   Anderson J.V., Neven L.G., Li Q.B., Haskell D.W., Guy C.L.;
RT   "A cDNA encoding the endoplasmic reticulum-luminal heat-shock protein from
RT   spinach (Spinacia oleracea L.).";
RL   Plant Physiol. 104:303-304(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Bloomsdale; TISSUE=Leaf;
RX   PubMed=8016266; DOI=10.1104/pp.104.4.1359;
RA   Anderson J.V., Li Q.B., Haskell D.W., Guy C.L.;
RT   "Structural organization of the spinach endoplasmic reticulum-luminal 70-
RT   kilodalton heat-shock cognate gene and expression of 70-kilodalton heat-
RT   shock genes during cold acclimation.";
RL   Plant Physiol. 104:1359-1370(1994).
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; L23551; AAA21808.1; -; mRNA.
DR   EMBL; L23552; AAA21806.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q42434; -.
DR   SMR; Q42434; -.
DR   PRIDE; Q42434; -.
DR   OrthoDB; 288077at2759; -.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; Endoplasmic reticulum; Glycoprotein; Nucleotide-binding;
KW   Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..668
FT                   /note="Luminal-binding protein"
FT                   /id="PRO_0000013593"
FT   REGION          643..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           665..668
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   668 AA;  73592 MW;  68043D93B56196A8 CRC64;
     MAVAWKSRAS SIAFGIVLLG SLFAFVSAKD EAPKLGTVIG IDLGTTYSCV GVYKDGKVEI
     IANDQGNRIT PSWVAFTNDE RLIGEAAKNQ AAANPERTIF DVKRLIGRKF EDKEVQKDMK
     LVPYKIVNRD GKPYIQVKVQ EGETKVFSPE EISAMILTKM KETAETFLGK KIKDAVVTVP
     AYFNDAQRQA TKDAGVIAGL NVARIINEPT AAAIAYGLDK RGGEKNILVF DLGGGTFDVS
     VLTIDNGVFE VLATNGDTHL GGEDFDQRLM EYFIKLIKKK HTKDISKDNR ALGKLRRECE
     RAKRALSSQH QVRVEIESLF DGVDFSEPLT RARFEELNND LFRKTMGPVK KAMDDAGLEK
     NQIDEIVLVG GSTRIPKVQQ LLKEFFNGKE PSKGVNPDEA VAFGAAVQGS ILSGEGGEET
     KEILLLDVAP LTLGIETVGG VMTKLIPRNT VIPTKKSQVF TTYQDQQTTV TIQVFEGERS
     LTKDCRLLGK FDLTGIAPAP RGTPQIEVTF EVDANGILNV KAEDKASGKS EKITITNDKG
     RLSQEEIERM VREAEEFAEE DKKVKEKIDA RNSLETYIYN MKNQISDADK LADKLESDEK
     EKIEGAVKEA LEWLDDNQSA EKEDYDEKLK EVEAVCNPII TAVYQRSGGP SGESGADSED
     SEEGHDEL