BIP_PHAVU
ID BIP_PHAVU Reviewed; 20 AA.
AC P80089;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Luminal-binding protein;
DE AltName: Full=78 kDa glucose-regulated protein homolog;
DE Short=GRP-78;
DE Flags: Fragment;
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=cv. Greensleeves; TISSUE=Cotyledon;
RX PubMed=1344885; DOI=10.1111/j.1365-313x.1992.00443.x;
RA D'Amico L., Valsasina B., Daminati M.G., Fabbrini M.S., Nitti G.,
RA Bollini R., Ceriotti A., Vitale A.;
RT "Bean homologs of the mammalian glucose-regulated proteins: induction by
RT tunicamycin and interaction with newly synthesized seed storage proteins in
RT the endoplasmic reticulum.";
RL Plant J. 2:443-455(1992).
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 -!- INDUCTION: By tunicamycin.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR AlphaFoldDB; P80089; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Endoplasmic reticulum;
KW Nucleotide-binding.
FT CHAIN 1..>20
FT /note="Luminal-binding protein"
FT /id="PRO_0000078665"
FT UNSURE 4
FT /note="A or T"
FT UNSURE 18
FT /note="Q or T"
FT NON_TER 20
SQ SEQUENCE 20 AA; 2147 MW; 809D43AF21A21476 CRC64;
KEEAKVLGTV IGIDLGTQYL