BIP_PICAN
ID BIP_PICAN Reviewed; 665 AA.
AC Q9HG01;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=BiP;
OS Pichia angusta (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=870730;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14754 / CBS 1976 / JCM 3620 / NBRC 0799 / NCYC 495 / NRRL
RC Y-1798 / VKM Y-1397;
RX PubMed=11954796; DOI=10.1007/s00253-001-0907-2;
RA van der Heide M., Hollenberg C.P., van der Klei I.J., Veenhuis M.;
RT "Overproduction of BiP negatively affects the secretion of Aspergillus
RT niger glucose oxidase by the yeast Hansenula polymorpha.";
RL Appl. Microbiol. Biotechnol. 58:487-494(2002).
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. {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; AF245405; AAG09776.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9HG01; -.
DR SMR; Q9HG01; -.
DR PRIDE; Q9HG01; -.
DR PhylomeDB; Q9HG01; -.
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..33
FT /evidence="ECO:0000255"
FT CHAIN 34..665
FT /note="Endoplasmic reticulum chaperone BiP"
FT /id="PRO_0000013584"
FT REGION 136..290
FT /note="Nucleotide-binding (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 410..510
FT /note="Substrate-binding (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 644..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 662..665
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 651..665
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 237..239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 303..310
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 374..377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
SQ SEQUENCE 665 AA; 73222 MW; 9A23F7BCCC0364B7 CRC64;
MLTFNKSVVS CAAIIYALLL VVLPLTTQQF VKAESNENYG TVIGIDLGTT YSCVGVMKAG
RVEIIPNDQG NRITPSYVAF TEDERLVGDA AKNQIASNPT NTIFDIKRLI GHRFDDKVIQ
KEIKHLPYKV KDQDGRPVVE AKVNGELKTF TAEEISAMIL GKMKQIAEDY LGKKVTHAVV
TVPAYFNDAQ RQATKDAGTI AGLEVLRIVN EPTAAAIAYG LDKTDEEKHI IVYDLGGGTF
DVSLLTIAGG AFEVLATAGD THLGGEDFDY RVVRHFIKVF KKKHGIDISD NSKALAKLKR
EVEKAKRTLS SQMSTRIEID SFVDGIDFSE SLSRAKFEEL NMDLFKKTLK PVQQVLDDAK
MKPDEIDDVV FVGGSTRIPK VQELIENFFN GKKISKGINP DEAVAFGAAV QGGVLSGEEG
VEDIVLIDVN PLTLGIETSG GVMTTLIKRN TPIPTQKSQI FSTAADNQPV VLIQVYEGER
AMAKDNNLLG KFELTGIPPA PRGVPQIEVT FTLDSNGILK VSATDKGTGK SNSITITNDK
GRLSKEEIEK KIEEAEKFAQ QDKELREKVE SRNALENYAH SLKNQANDEN GFGAKLEEDD
KETLLDAINE ALEFLEDNFD TATKDEFDEQ KEKLSKVAYP ITSKLYDAPP TSDEEDEDDW
DHDEL
