ID   BIP3_MAIZE              Reviewed;         663 AA.
AC   O24581;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Luminal-binding protein 3;
DE            Short=BiP3;
DE   Flags: Precursor;
GN   Name=BIPE3;
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].
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).
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; U58209; AAC49900.1; -; mRNA.
DR   PIR; T04080; T04080.
DR   RefSeq; NP_001105894.1; NM_001112424.1.
DR   AlphaFoldDB; O24581; -.
DR   SMR; O24581; -.
DR   STRING; 4577.GRMZM2G415007_P01; -.
DR   PaxDb; O24581; -.
DR   PRIDE; O24581; -.
DR   GeneID; 732809; -.
DR   KEGG; zma:732809; -.
DR   eggNOG; KOG0100; Eukaryota.
DR   OrthoDB; 288077at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; O24581; baseline and differential.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..663
FT                   /note="Luminal-binding protein 3"
FT                   /id="PRO_0000013592"
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;  73157 MW;  A710278D9F692723 CRC64;
     MDRVRGSAFL LGVLLAGSLF AFSVAKEETK KLGTVIGIDL GTTYSCVGVY KNGHVEIIAN
     DQGNRITPSW VAFTDSERLI GEAAKNQAAV NPERTIFDVK RLIGRKFQDK 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 RIPKVQQLLK DYFNGKEPNK GVNPDEAVAF GAAVQGSILS GEGGDETKDI
     LLLDVAPLTL GIETVGGVMT KLIPRNTVIP TKKSQVFTTY QDQQTTVSIQ VFEGERSMTK
     DCRLLGKFDL NGIPSAPRGT PQIEVTFEVD ANGILNVKAE DKGTGKSEKI TITNEKGRLS
     QEEIDRMVRE AEEFAEEDKK VKERIDARNQ LETYVYNMKN TVGDKDKLAD KLEAEEKEKV
     EEALKEALEW LDDNQSAEKE DYEEKLKEVE AVCNPIVSAV YQRSGGAPGG DADGGVDDDH
     DEL