ID   BIP5_TOBAC              Reviewed;         668 AA.
AC   Q03685;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Luminal-binding protein 5;
DE            Short=BiP 5;
DE   AltName: Full=78 kDa glucose-regulated protein homolog 5;
DE            Short=GRP-78-5;
DE   Flags: Precursor;
GN   Name=BIP5;
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=10.1105/tpc.3.9.1025;
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; X60058; CAA42660.1; -; mRNA.
DR   PIR; S21880; S21880.
DR   RefSeq; NP_001312029.1; NM_001325100.1.
DR   RefSeq; XP_016446271.1; XM_016590785.1.
DR   AlphaFoldDB; Q03685; -.
DR   SMR; Q03685; -.
DR   STRING; 4097.Q03685; -.
DR   GlyCosmos; Q03685; 1 site, No reported glycans.
DR   PaxDb; 4097-Q03685; -.
DR   GeneID; 107771425; -.
DR   KEGG; nta:107771425; -.
DR   OMA; DSKPCIE; -.
DR   OrthoDB; 143at2759; -.
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; IEA:UniProtKB-KW.
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:0044183; F:protein folding chaperone; 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; 3.30.420.40; -; 2.
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; PTHR45639:SF4; HSC70CB, ISOFORM G; 1.
DR   PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..668
FT                   /note="Luminal-binding protein 5"
FT                   /id="PRO_0000013595"
FT   REGION          645..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;  73744 MW;  7980231A991DC590 CRC64;
     MAGAWKRRAS LIVFAIVLFG SLFAFSIAKE EATKLGTVIG IDLGTTYSCV GVYKNGHVEI
     IANDQGNRIT PSWVAFTDGE RLIGEAAKNQ AAVNPERTIF DVKRLIGRKF DDKEVQRDKK
     LVPYEIVNKD GKPYIQVKIK DGETKVFSPE EISAMILTKM KETAEAYLGK KIKDAVVTVP
     AYFNDAQRQA TKDAGVIAGL NVARIINEPT AAAIAYGLDK KGGEKNILVF DLGGGTFDVS
     ILTIDNGVFE VLATNGDTHL GGEDFDQRIM EYFIKLIKKK HGKDISKDNR ALGKLRREAE
     RAKRALSSQH QVRVEIESLF DGVDFSEPLT RARFEELNND LFRKTMGPVK KAMEDAGLEK
     NQIDEIVLVG GSTRIPKVQQ LLKDYFDGKE PNKGVNPDEA VAYGAAVQGG ILSGEGGDET
     KDILLLDVAP LTLGIETVGG VMTKLIPRNT VIPTKKSQVF TTYQDQQTTV TISVFEGERS
     LTKDCRLLGK FDLTGIAPAP RGTPQIEVTF EVDANGILNV KAEDKASGKS EKITITNDKG
     RLSQEEIERM VKEAEEFAEE DKKVKERIDA RNSLETYVYN MRNQINDKDK LADKLESDEK
     EKIETATKEA LEWLDDNQSA EKEDYDEKLK EVEAVCNPII TAVYQRSGGA PGGASEESNE
     DDDSHDEL
//