BIP_CORAV
ID BIP_CORAV Reviewed; 668 AA.
AC Q9FSY7;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Endoplasmic reticulum chaperone BiP {ECO:0000305};
DE EC=3.6.4.10 {ECO:0000250|UniProtKB:P11021};
DE AltName: Full=78 kDa glucose-regulated protein homolog {ECO:0000305};
DE Short=GRP-78 homolog {ECO:0000305};
DE AltName: Full=Binding-immunoglobulin protein {ECO:0000305};
DE Short=BiP {ECO:0000303|PubMed:12811017};
DE AltName: Full=Heat shock protein 70 family protein {ECO:0000305};
DE Short=HSP70 family protein {ECO:0000305};
DE AltName: Full=Luminal-binding protein {ECO:0000303|PubMed:12811017};
DE AltName: Allergen=Cor a 10.0101 {ECO:0000305};
DE Flags: Precursor;
OS Corylus avellana (European hazel) (Corylus maxima).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Betulaceae; Corylus.
OX NCBI_TaxID=13451 {ECO:0000312|EMBL:CAC14168.1};
RN [1] {ECO:0000312|EMBL:CAC14168.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PTM,
RP AND ALLERGEN.
RC TISSUE=Pollen {ECO:0000303|PubMed:12811017};
RX PubMed=12811017; DOI=10.1159/000070924;
RA Gruehn S., Suphioglu C., O'Hehir R.E., Volkmann D.;
RT "Molecular cloning and characterization of hazel pollen protein (70 kD) as
RT a luminal binding protein (BiP): a novel cross-reactive plant allergen.";
RL Int. Arch. Allergy Immunol. 131:91-100(2003).
CC -!- FUNCTION: Probably plays a role in facilitating the assembly of
CC multimeric protein complexes inside the ER. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
CC Evidence={ECO:0000250|UniProtKB:P11021};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:Q6Z7B0}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen and nuts (at protein level).
CC {ECO:0000269|PubMed:12811017}.
CC -!- DEVELOPMENTAL STAGE: Expressed during pollen development. At the
CC immature, bicellular stage, expressed exclusively in the intine. At the
CC mature, tricellular stage, expressed at the boundary of cytoplasm and
CC intine of the pollen grains, specifically in the region of the germinal
CC apertures. The strongest expression at the mature stage is shown under
CC normal environmental conditions. After germination, expressed at the
CC tip region of the pollen tube. {ECO:0000269|PubMed:12811017}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:12811017}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 71% of
CC the 7 patients tested allergic to tree pollen, including hazel and
CC birch pollen. {ECO:0000269|PubMed:12811017}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000255|RuleBase:RU003322, ECO:0000305}.
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DR EMBL; AJ295617; CAC14168.1; -; mRNA.
DR AlphaFoldDB; Q9FSY7; -.
DR SMR; Q9FSY7; -.
DR Allergome; 243; Cor a 10.
DR Allergome; 3215; Cor a 10.0101.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0009555; P:pollen development; IEP:UniProtKB.
DR GO; GO:0009846; P:pollen germination; IEP:UniProtKB.
DR GO; GO:0009860; P:pollen tube growth; IEP:UniProtKB.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; ISS:UniProtKB.
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 Allergen; ATP-binding; Chaperone; Endoplasmic reticulum; Glycoprotein;
KW Hydrolase; Nucleotide-binding; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..668
FT /note="Endoplasmic reticulum chaperone BiP"
FT /evidence="ECO:0000255"
FT /id="PRO_5004326528"
FT REGION 132..287
FT /note="Nucleotide-binding (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 644..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 665..668
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT BINDING 44..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 234..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 300..307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 371..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 668 AA; 73564 MW; 8243BA3FCF9C10D9 CRC64;
MAGSWRARGS LVVLAILLFG CLFAISIAKE EATKLGTVIG IDLGTTYSCV GVYKNGHVEI
IANDQGNRIT PSWVGFTDGE RLIGEAAKNQ AAVNPERTIF DVKRLIGRKF EDKEVQKDMK
LVPYKIVNKD GKPYIQVKIK DGETKVFSPE EISAMILIKM KETAEAFLGK KIKDAVVTVP
AYFNDAQRQA TKDAGIIAGL NVARIINEPT AAAIAYGLDK KGGEKNILVF DLGGGTFDVS
ILTIDNGVFE VLSTNGDTHL GGEDFDMRIM EYFIKLIKKK HGKDISKDNR AIGKLRREAE
RAKRALSSQH QVRVEIESLF DGVDFSEPLT RARFEELNND FVQKDHGTRE EAMEDAGLAK
NQIDEIVLVG GSTRIPKVQQ LLKDYFDGKE PNKGVNPDEA VAYGAAVQGS ILSGEGGEET
KDILLLDVAP LTLGIETVGG VMTKLIPRNT VIPTKKSQVF TTYQDQQTTV SIQVFEGERS
LTKDCRNLGK FDLTGVPPAP RGTPQIEVTF EVDANGILNV KAEDKGTGKS EKITITNDKG
RLSQEEIDRM VQEAEEFAEE DKKVKERIDA RNTLETYVYN MKNQVNDKDK LADKLESDEK
DKIESAVKDA LEWLDDNQSA EKEDYDEKLK EVEAVCNPII TAVYQRSGGA PGGGSGEEDE
DSESHDEL
