BIP_ASPKA
ID BIP_ASPKA Reviewed; 672 AA.
AC P83617; O13280; O14453;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2003, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Endoplasmic reticulum chaperone BiP {ECO:0000305};
DE EC=3.6.4.10 {ECO:0000250|UniProtKB:P11021};
DE AltName: Full=Immunoglobulin heavy chain-binding protein homolog {ECO:0000305};
DE Short=BiP {ECO:0000305};
DE Flags: Precursor;
GN Name=bipA;
OS Aspergillus kawachii (White koji mold) (Aspergillus awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1069201 {ECO:0000305};
RN [1] {ECO:0000312|EMBL:AAG10649.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ORI-1 {ECO:0000312|EMBL:AAG10649.1};
RA Goto M., Shinoda N., Furukawa K.;
RT "Molecular cloning of the bipA gene of Aspergillus awamori var. kawachi.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably plays a role in facilitating the assembly of
CC multimeric protein complexes inside the ER. Is required for secretory
CC polypeptide translocation. May physically associate with SEC63 protein
CC in the endoplasmic reticulum and this interaction may be regulated by
CC ATP hydrolysis. {ECO:0000250|UniProtKB:P16474}.
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 -!- ACTIVITY REGULATION: The chaperone activity is regulated by ATP-induced
CC allosteric coupling of the nucleotide-binding (NBD) and substrate-
CC binding (SBD) domains. In the ADP-bound and nucleotide-free (apo)
CC states, the two domains have little interaction. In contrast, in the
CC ATP-bound state the two domains are tightly coupled, which results in
CC drastically accelerated kinetics in both binding and release of
CC polypeptide substrates. J domain-containing co-chaperones stimulate the
CC ATPase activity and are required for efficient substrate recognition.
CC {ECO:0000250|UniProtKB:P11021}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:P16474, ECO:0000255|PROSITE-ProRule:PRU10138}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000255|RuleBase:RU003322, ECO:0000305}.
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DR EMBL; AF183893; AAG10649.1; -; Genomic_DNA.
DR AlphaFoldDB; P83617; -.
DR SMR; P83617; -.
DR VEuPathDB; FungiDB:AKAW_01955; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006986; P:response to unfolded protein; 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 3: Inferred from homology;
KW ATP-binding; Chaperone; Endoplasmic reticulum; Hydrolase;
KW Nucleotide-binding; Signal; Stress response.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..672
FT /note="Endoplasmic reticulum chaperone BiP"
FT /id="PRO_0000013579"
FT REGION 145..299
FT /note="Nucleotide-binding (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 419..519
FT /note="Substrate-binding (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT MOTIF 669..672
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT BINDING 57..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 246..248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 312..319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 383..386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
SQ SEQUENCE 672 AA; 73459 MW; C701807FCE08C175 CRC64;
MARISHQGAA KPFTAWTTIF YLLLVFIAPL AFFGTAHAQD ETSPQESYGT VIGIDLGTTY
SCVGVMQNGK VEILVNDQGN RITPSYVAFT DEERLVGDAA KNQYAANPRR TIFDIKRLIG
RKFDDKDVQK DAKHFPYKVV NKDGKPHVKV DVNQTPKTLT PEEVSAMVLG KMKEIAEGYL
GKKVTHAVVT VPAYFNDAQR QATKDAGTIA GLNVLRVVNE PTAAAIAYGL DKTGDERQVI
VYDLGGGTFD VSLLSIDNGV FEVLATAGDT HLGGEDFDQR VMDHFVKLYN KKNNVDVTKD
LKAMGKLKRE VEKAKRTLSS QMSTRIEIEA FHNGEDFSET LTRAKFEELN MDLFKKTLKP
VEQVLKDAKV KKSEVDDIVL VGGSTRIPKV QALLEEFFGG KKASKGINPD EAVAFGAAVQ
GGVLSGEEGT GDVVLMDVNP LTLGIETTGG VMTKLIPRNT VIPTRKSQIF STAADNQPTV
LIQVYEGERS LTKDNNLLGK FELTGIPPAP RGVPQIEVSF DLDANGILKV HASDKGTGKA
ESITITNDKG RLSQEEIDRM VAEAEEFAEE DKAIKAKIEA RNTLENYAFS LKNQVNDENG
LGGQIDEDDK QTILDAVKEV TEWLEDNAAT ATTEDFEEQK EQLSNVAYPI TSKLYGSAPA
DEDDEPSGHD EL
