BIP_NEUCR
ID BIP_NEUCR Reviewed; 661 AA.
AC P78695; Q7RV55;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 3.
DT 03-AUG-2022, entry version 153.
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=grp78; ORFNames=NCU03982;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bd-A / FGSC 1858;
RX PubMed=9545520; DOI=10.1016/s0167-4781(98)00005-0;
RA Techel D., Hafker T., Muschner S., Reimann M., Li Y., Monnerjahn C.,
RA Rensing L.;
RT "Molecular analysis of a glucose-regulated gene (grp78) of Neurospora
RT crassa.";
RL Biochim. Biophys. Acta 1397:21-26(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; Y09011; CAA70214.1; -; Genomic_DNA.
DR EMBL; CM002241; EAA27331.1; -; Genomic_DNA.
DR PIR; T50464; T50464.
DR RefSeq; XP_956567.1; XM_951474.3.
DR AlphaFoldDB; P78695; -.
DR SMR; P78695; -.
DR IntAct; P78695; 4.
DR MINT; P78695; -.
DR STRING; 5141.EFNCRP00000003679; -.
DR PRIDE; P78695; -.
DR EnsemblFungi; EAA27331; EAA27331; NCU03982.
DR GeneID; 3872714; -.
DR KEGG; ncr:NCU03982; -.
DR VEuPathDB; FungiDB:NCU03982; -.
DR HOGENOM; CLU_005965_7_0_1; -.
DR InParanoid; P78695; -.
DR OMA; AYTKNQD; -.
DR Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
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; 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: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; 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; Reference proteome; Signal; Stress response.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..661
FT /note="Endoplasmic reticulum chaperone BiP"
FT /id="PRO_0000013583"
FT REGION 135..289
FT /note="Nucleotide-binding (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 409..509
FT /note="Substrate-binding (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT MOTIF 658..661
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT BINDING 47..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 236..238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 302..309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 373..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT CONFLICT 127
FT /note="Y -> N (in Ref. 1; CAA70214)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="T -> N (in Ref. 1; CAA70214)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="D -> E (in Ref. 1; CAA70214)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="N -> ND (in Ref. 1; CAA70214)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 661 AA; 72332 MW; 90963337AF327DEA CRC64;
MEHRTRSWAL GLSILGFFAL LFSAGFVQQA HANDTEAMGT VIGIDLGTTY SCVGVMQKGK
VEILVNDQGN RITPSYVAFT DEERLVGDAA KNQAAANPHR TIFDIKRLIG RKFSDKDVQN
DIKHFPYKVV SKDDKPVVKV EVKGEEKTFT PEEISAMILG KMKETAEGYL GKKVTHAVVT
VPAYFNDNQR QATKDAGMIA GLNVLRIVNE PTAAAIAYGL DKTGEERQII VYDLGGGTFD
VSLLSIEQGV FEVLSTAGDT HLGGEDFDQR IINHFAKLFN KKHGVDVTKD AKAMGKLKRE
AEKAKRTLSS QMSTRIEIEA FYDGKDFSET LTRAKFEELN NDLFKKTLKP VEQVLKDAKV
SKSEIDDIVL VGGSTRIPKV QALIEEFFNG KKASKGINPD EAVAFGAAVQ AGVLSGEEGT
EDIVLMDVNP LTLGIETTGG VMTKLIPRNT PIPTRKSQIF STAADNQPVV LIQVYEGERS
MTKDNNLLGK FELTGIPPAP RGVPQIEVSF ELDANGILKV SAHDKGTGKA ESITITNDKG
RLTQEEIDRM VAEAEKYAEE DKATRERIEA RNGLENYAFS LKNQVNDEDG LGGKIDEEDK
ETILDAVKEA QDWLEENAAT ASAEDFDEQK EKLSNVAYPI TSKLYSQGGA GDDEPAGHDE
L
