BIP5_TOBAC
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 03-AUG-2022, entry version 97.
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=10.2307/3869163;
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; 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 PRIDE; Q03685; -.
DR GeneID; 107771425; -.
DR KEGG; nta:107771425; -.
DR OMA; DSKPCIE; -.
DR OrthoDB; 288077at2759; -.
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..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