BIP3_TOBAC
ID BIP3_TOBAC Reviewed; 168 AA.
AC Q03683;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Luminal-binding protein 3;
DE Short=BiP 3;
DE AltName: Full=78 kDa glucose-regulated protein homolog 3;
DE Short=GRP-78-3;
DE Flags: Fragment;
GN Name=BIP3;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X60061; CAA42663.1; -; mRNA.
DR PIR; PQ0263; PQ0263.
DR AlphaFoldDB; Q03683; -.
DR SMR; Q03683; -.
DR STRING; 4097.Q03683; -.
DR PRIDE; Q03683; -.
DR Proteomes; UP000084051; Unplaced.
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 Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
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 PROSITE; PS00014; ER_TARGET; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Endoplasmic reticulum; Glycoprotein; Nucleotide-binding;
KW Reference proteome.
FT CHAIN <1..168
FT /note="Luminal-binding protein 3"
FT /id="PRO_0000078668"
FT REGION 148..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 165..168
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
SQ SEQUENCE 168 AA; 18839 MW; D0089CF2219C624E CRC64;
PAPRGTPQIE VTFEVDANGI LNVKAEDKGT GKSEKITITN DKGRLSQEEI ERMVREAEEF
AEEDKKVKER IDARNGLETY VYNMKNQIND KDKLADKLES DEKEKIETAV KEALEWLDDN
QSAEKEDYEE KLKEVEAVCN PIITAVYQRS GGASGGSSSS EEDGHDEL