BIP_YARLI
ID BIP_YARLI Reviewed; 670 AA.
AC Q99170;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=YALI0E13706g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 32338 / CX-161-1B;
RX PubMed=9178502;
RX DOI=10.1002/(sici)1097-0061(199705)13:6<499::aid-yea100>3.0.co;2-m;
RA Lee I.H., Ogrydziak D.M.;
RT "Yarrowia lipolytica SRP54 homolog and translocation of Kar2p.";
RL Yeast 13:499-513(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; U63136; AAC49736.1; -; Genomic_DNA.
DR EMBL; CR382131; CAG79506.1; -; Genomic_DNA.
DR RefSeq; XP_503913.1; XM_503913.1.
DR AlphaFoldDB; Q99170; -.
DR SMR; Q99170; -.
DR IntAct; Q99170; 1.
DR MINT; Q99170; -.
DR STRING; 4952.CAG79506; -.
DR PRIDE; Q99170; -.
DR EnsemblFungi; CAG79506; CAG79506; YALI0_E13706g.
DR GeneID; 2912786; -.
DR KEGG; yli:YALI0E13706g; -.
DR VEuPathDB; FungiDB:YALI0_E13706g; -.
DR HOGENOM; CLU_005965_7_0_1; -.
DR InParanoid; Q99170; -.
DR OMA; AYTKNQD; -.
DR Proteomes; UP000001300; Chromosome E.
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: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:0036498; P:IRE1-mediated unfolded protein response; IEA:EnsemblFungi.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0006986; P:response to unfolded protein; ISS:UniProtKB.
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; Glycoprotein; Hydrolase;
KW Nucleotide-binding; Reference proteome; Signal; Stress response.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..670
FT /note="Endoplasmic reticulum chaperone BiP"
FT /id="PRO_0000013586"
FT REGION 133..287
FT /note="Nucleotide-binding (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 407..507
FT /note="Substrate-binding (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 642..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 667..670
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT BINDING 45..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 104
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 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 670 AA; 73524 MW; 2C2DFB436BCC9C0E CRC64;
MKFSMPSWGV VFYALLVCLL PFLSKAGVQA DDVDSYGTVI GIDLGTTYSC VGVMKGGRVE
ILANDQGSRI TPSYVAFTED ERLVGDAAKN QAANNPFNTI FDIKRLIGLK YKDESVQRDI
KHFPYKVKNK DGKPVVVVET KGEKKTYTPE EISAMILTKM KDIAQDYLGK KVTHAVVTVP
AYFNDAQRQA TKDAGIIAGL NVLRIVNEPT AAAIAYGLDH TDDEKQIVVY DLGGGTFDVS
LLSIESGVFE VLATAGDTHL GGEDFDYRVI KHFVKQYNKK HDVDITKNAK TIGKLKREVE
KAKRTLSSQM STRIEIESFF DGEDFSETLT RAKFEELNID LFKRTLKPVE QVLKDSGVKK
EDVHDIVLVG GSTRIPKVQE LLEKFFDGKK ASKGINPDEA VAYGAAVQAG VLSGEDGVED
IVLLDVNPLT LGIETTGGVM TKLINRNTNI PTKKSQIFST AVDNQSTVLI QVFEGERTMS
KDNNLLGKFE LKGIPPAPRG VPQIEVTFEL DANGILRVTA HDKGTGKSET ITITNDKGRL
SKDEIERMVE EAERFAEEDA LIRETIEAKN SLENYAHSLR NQVADKSGLG GKISADDKEA
LNDAVTETLE WLEANSVSAT KEDFEEKKEA LSAIAYPITS KIYEGGEGGD ESNDGGFYAD
DDEAPFHDEL
