BIP4_TOBAC
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 03-AUG-2022, entry version 99.
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=10.2307/3869163;
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; 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 PRIDE; Q03684; -.
DR ProMEX; Q03684; -.
DR GeneID; 107818867; -.
DR KEGG; nta:107818867; -.
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 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..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