ID   BIP2_TOBAC              Reviewed;         292 AA.
AC   Q03682;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=Luminal-binding protein 2;
DE            Short=BiP 2;
DE   AltName: Full=78 kDa glucose-regulated protein homolog 2;
DE            Short=GRP-78-2;
DE   Flags: Fragment;
GN   Name=BIP2;
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; X60059; CAA42661.1; -; mRNA.
DR   PIR; PQ0262; S21878.
DR   AlphaFoldDB; Q03682; -.
DR   SMR; Q03682; -.
DR   STRING; 4097.Q03682; -.
DR   GlyCosmos; Q03682; 1 site, No reported glycans.
DR   PaxDb; 4097-Q03682; -.
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; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
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; 1.
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.
PE   2: Evidence at transcript level;
KW   ATP-binding; Endoplasmic reticulum; Glycoprotein; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           <1..292
FT                   /note="Luminal-binding protein 2"
FT                   /id="PRO_0000078667"
FT   REGION          268..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           289..292
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   292 AA;  32260 MW;  6E7A4F5107C6E2D5 CRC64;
     KVQQLLKDYF DGKEPNKGVN PDEAVAFGAA VQGGILSGEG GDETKDILLL DVAPLTLGIE
     TVGGVMTKLI PRNTVIPTKK SQVFTTYQDQ QTTVSIQVFE GERSLTKDCR LLGKFDLTGI
     APAPRGTPQI EVTFEVDANG ILNVKAEDKG TGKSEKITIT NDKGRLSQEE IERMVREAEE
     FAEEDKKVKE RIDARNSLET YVYNMKNQIN DKDKLADKLE SDEKEKIETA TKEALEWLDD
     NQSAEKEDYE EKLKEVEAVC NPIITAVYQR SGGAPGGGSS EEEEEEDGHD EL
//