ID   BIP_EREGS               Reviewed;         674 AA.
AC   Q75C78;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 116.
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=KAR2; OrderedLocusNames=ACR038W;
OS   Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS   Y-1056) (Yeast) (Ashbya gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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}.
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DR   EMBL; AE016816; AAS51265.1; -; Genomic_DNA.
DR   RefSeq; NP_983441.1; NM_208794.1.
DR   AlphaFoldDB; Q75C78; -.
DR   SMR; Q75C78; -.
DR   STRING; 284811.Q75C78; -.
DR   EnsemblFungi; AAS51265; AAS51265; AGOS_ACR038W.
DR   GeneID; 4619566; -.
DR   KEGG; ago:AGOS_ACR038W; -.
DR   eggNOG; KOG0100; Eukaryota.
DR   HOGENOM; CLU_005965_7_0_1; -.
DR   InParanoid; Q75C78; -.
DR   OMA; AYTKNQD; -.
DR   OrthoDB; 143at2759; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0099021; C:cortical endoplasmic reticulum lumen; IEA:EnsemblFungi.
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:0034099; C:luminal surveillance complex; IEA:EnsemblFungi.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0031965; C:nuclear membrane; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0099020; C:perinuclear endoplasmic reticulum lumen; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0015450; F:protein-transporting ATPase activity; IEA:EnsemblFungi.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
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:0070880; P:fungal-type cell wall beta-glucan biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0036498; P:IRE1-mediated unfolded protein response; IEA:EnsemblFungi.
DR   GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR   GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IEA:EnsemblFungi.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IEA:EnsemblFungi.
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; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
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:SF144; ENDOPLASMIC RETICULUM CHAPERONE BIP; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
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; Reference proteome; Signal; Stress response.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..674
FT                   /note="Endoplasmic reticulum chaperone BiP"
FT                   /id="PRO_0000013576"
FT   REGION          143..297
FT                   /note="Nucleotide-binding (NBD)"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   REGION          416..516
FT                   /note="Substrate-binding (SBD)"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   REGION          651..674
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           671..674
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   COMPBIAS        656..674
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         55..58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   BINDING         114
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   BINDING         244..246
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   BINDING         310..317
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   BINDING         381..384
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
SQ   SEQUENCE   674 AA;  73898 MW;  EA3DCF15A5A48547 CRC64;
     MAFGKVSNWA VPLTALMYAM ALVCLPMFAG GSRGLVYAAD TDAENYGTVI GIDLGTTYSC
     VALMRNGKTE ILANEQGNRI TPSYVAFTDD ERLIGDAAKN QVANNPKNTI FDIKRLIGLK
     YNDKTVQREI KHLPFEVVDK NGMPAVAVTV KGERKLFTPE EISGMVLGKM KQIAEEYLGK
     KVTHAVVTVP AYFNDAQRQA TKDAGAIAGL NILRIVNEPT AAAIAYGLDK TEDEHRIVVY
     DLGGGTFDVS LLSIENGVFE VQATAGDTHL GGEDFDYKLV RHFLKVFKKK HGVDVSSNAK
     AMAKLKREAE KAKRALSSQM STRVEIDSFV DGIDFSETLT RAKFEEMNLD LFKRTLKPVE
     KVLQDAGLKK EDIDDIVLVG GSTRIPKVQE LLENFFNKKA SKGINPDEAV AYGAAVQAGV
     LSGEEGVEDI VLLDVNPLTL GIEVTGGIMT PLIKRNTPIP TKKSQIFSTA VDNQKTVMIQ
     VYEGERAMAK DNNHLGKFEL SGIPPAPRGI PQIEVTFALD ANGILKVSAT DKGTGKSESV
     TITNEKGRLS KDDIERMVAE AENYQKEDEE IRAKVEARHK LENYAHSLKN QVNGDLGDKL
     EEDDKETLLE AANDVLEWLE DNSDSATKEE FNEKFESLSQ TAYPITSKLY GAGASDATDD
     EDDESDDYFD HDEL
//