ID   BIP4_TOBAC              Reviewed;         667 AA.
AC   Q03684;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Luminal-binding protein 4;
DE            Short=BiP 4;
DE   AltName: Full=78 kDa glucose-regulated protein homolog 4;
DE            Short=GRP-78-4;
DE   Flags: Precursor;
GN   Name=BIP4;
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; X60057; CAA42659.1; -; mRNA.
DR   PIR; JQ1360; S21879.
DR   RefSeq; NP_001312963.1; NM_001326034.1.
DR   AlphaFoldDB; Q03684; -.
DR   SMR; Q03684; -.
DR   STRING; 4097.Q03684; -.
DR   GlyCosmos; Q03684; 1 site, No reported glycans.
DR   PaxDb; 4097-Q03684; -.
DR   ProMEX; Q03684; -.
DR   GeneID; 107818867; -.
DR   KEGG; nta:107818867; -.
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..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..667
FT                   /note="Luminal-binding protein 4"
FT                   /id="PRO_0000013594"
FT   REGION          644..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           664..667
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   CARBOHYD        618
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   667 AA;  73522 MW;  D99278756EF7B2CA CRC64;
     MAGGAWNRRT SLIVFGIVLF GCLFAFSIAT EEATKLGTVI GIDLGTTYSC VGVYKNGHVE
     IIANDQGNRI TPSWVAFTDG ERLIGEAAKN LAAVNPERTV FDVKRLIGRK FDDKEVQRDM
     KLVPYKIVNK DGKPYIQVKI KDGETKIFSP EEISAMILTK MKETAEAYLG KKIKDAVVTV
     PAYFNDAQRQ ATKDAGVIAG LNVARIINEP TAAAIAYGLD KKGGEKNILV FDLGGGTFDV
     SILTIDNGVF EVLSTNGDTH LGGEDFDQRI MEYFIKLIKK KHGKDISKDN RALGKLRREA
     ERAKRALSSQ HQVRVEIESL FDGVDFSEPL TRARFEELNN DLFRKTMGPV KKAMDDAGLE
     KTQIDEIVLV GGSTRIPKVQ QLLKDYFDGK EPNKGVNPDE AVAYGAAVQG GILSGEGGDE
     TKDILLLDVA PLTLGIETVG GVMTKLIPRN TVIPTKKSQV FTTYQDQQTT VTIQVFEGER
     SLTKDCRLLG KFDLTGIAPA PRGTPQIEVT FEVDANGILN VKAEDKASGK SEKITITNDK
     GRLSQEEIER MVKEAEEFAE EDKKVKERID ARNSLETYVY NMRNQINDKD KLADKLESDE
     KEKIETATKE ALEWLDDNQS AEKEDYEEKL KEVEAVCNPI ITAVYQKSGG APGGESGASE
     DDDHDEL
//