BIP2_MAIZE
ID BIP2_MAIZE Reviewed; 663 AA.
AC P24067;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Luminal-binding protein 2;
DE Short=BiP2;
DE AltName: Full=B-70;
DE Short=B70;
DE AltName: Full=Heat shock protein 70 homolog 2;
DE Flags: Precursor;
GN Name=BIPE2;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC STRAIN=cv. Floury-2; TISSUE=Kernel;
RX PubMed=9434171; DOI=10.1016/s0378-1119(97)00529-5;
RA Wrobel R.L., Obrian G.R., Boston R.S.;
RT "Comparative analysis of BiP gene expression in maize endosperm.";
RL Gene 204:105-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 197-663, AND CHARACTERIZATION.
RC STRAIN=cv. Floury-2; TISSUE=Kernel;
RX PubMed=1840923; DOI=10.2307/3869354;
RA Fontes E.B.P., Shank B.B., Wrobel R.L., Moose S.P., Obrian G.R.,
RA Wurtzel E.T., Boston R.S.;
RT "Characterization of an immunoglobulin binding protein homolog in the maize
RT floury-2 endosperm mutant.";
RL Plant Cell 3:483-496(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 -!- INDUCTION: By treatment with tunicamycin. Overproduced in fl2,
CC defective endosperm-b30, and mucronate mutants.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA92743.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={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; U58208; AAC49899.1; -; mRNA.
DR EMBL; M59449; AAA92743.1; ALT_SEQ; mRNA.
DR PIR; JQ0966; JQ0966.
DR PIR; T04078; T04078.
DR RefSeq; NP_001105893.1; NM_001112423.1.
DR RefSeq; NP_001278725.1; NM_001291796.1.
DR AlphaFoldDB; P24067; -.
DR SMR; P24067; -.
DR STRING; 4577.GRMZM2G114793_P01; -.
DR PaxDb; P24067; -.
DR PRIDE; P24067; -.
DR ProMEX; P24067; -.
DR EnsemblPlants; Zm00001eb229930_T002; Zm00001eb229930_P002; Zm00001eb229930.
DR GeneID; 732808; -.
DR Gramene; Zm00001eb229930_T002; Zm00001eb229930_P002; Zm00001eb229930.
DR KEGG; zma:732808; -.
DR MaizeGDB; 66083; -.
DR eggNOG; KOG0100; Eukaryota.
DR HOGENOM; CLU_005965_7_2_1; -.
DR OMA; AEEDNIC; -.
DR OrthoDB; 288077at2759; -.
DR Proteomes; UP000007305; Chromosome 5.
DR ExpressionAtlas; P24067; baseline and differential.
DR Genevisible; P24067; ZM.
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 1: Evidence at protein level;
KW ATP-binding; Endoplasmic reticulum; Glycoprotein; Nucleotide-binding;
KW Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..663
FT /note="Luminal-binding protein 2"
FT /id="PRO_0000013591"
FT REGION 641..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 660..663
FT /note="Prevents secretion from ER"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 663 AA; 73085 MW; 6769B7D19A0D918A CRC64;
MDRARGSAFL LGVLLAGSLF AFSVAKEETK KLGTVIGIDL GTTYSCVGVY KNGHVEIIAN
DQGNRITPSW VAFTDSERLI GEAAKNQAAV NPERTIFDVK RLIGRKFADK EVQRDMKLVP
YKIINKDGKP YIQVKIKDGE NKVFSPEEIS AMILGKMKDT AEAYLGKKIN DAVVTVPAYF
NDAQRQATKD AGVIAGLNVA RIINEPTAAA IAYGLDKKGG EKNILVFDLG GGTFDVSILT
IDNGVFEVLA TNGDTHLGGE DFDQRIMEYF IKLIKKKYSK DISKDNRALG KLRREAERAK
RALSNQHQVR VEIESLFDGT DFSEPLTRAR FEELNNDLFR KTMGPVKKAM EDAGLEKSQI
HEIVLVGGST RIPKVQQLLR DYFDGKEPNK GVNPDEAVAF GAAVQGSILS GEGGDETKDI
LLLDVAPLTL GIETVGGVMT KLIPRNTVIP TKKSQVFTTY QDQQTTVSIQ VFEGERSMTK
DCRLLGKFDL NGIAPAPRGT PQIEVTFEVD ANGILNVKAE DKGTGKSEKI TITNEKGRLS
QEEIDRMVRE AEEFAEEDKK VKERIDARNQ LETYVYNMKN TVGDKDKLAD KLEAEEKEKV
EEALKEALEW LDDNQSAEKE DYEEKLKEVE AVCNPIVSAV YQRSGGAPGG DADGGVDDDH
DEL
