(data stored in ACNUC7421 zone)

SWISSPROT: BIP_ASHGO

ID   BIP_ASHGO               Reviewed;         674 AA.
AC   Q75C78;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 97.
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   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium 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}.
DR   EMBL; AE016816; AAS51265.1; -; Genomic_DNA.
DR   RefSeq; NP_983441.1; NM_208794.1.
DR   SMR; Q75C78; -.
DR   STRING; 33169.AAS51265; -.
DR   PRIDE; Q75C78; -.
DR   EnsemblFungi; AAS51265; AAS51265; AGOS_ACR038W.
DR   GeneID; 4619566; -.
DR   KEGG; ago:AGOS_ACR038W; -.
DR   HOGENOM; HOG000228135; -.
DR   InParanoid; Q75C78; -.
DR   KO; K09490; -.
DR   OMA; CVGVMQK; -.
DR   Proteomes; UP000000591; Chromosome III.
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:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATPase activity; IBA:GO_Central.
DR   GO; GO:0042623; F:ATPase activity, coupled; IBA:GO_Central.
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:0034605; P:cellular response to heat; 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:0000742; P:karyogamy involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR   GO; GO:0031204; P:posttranslational protein targeting to membrane, translocation; IEA:EnsemblFungi.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0006986; P:response to unfolded protein; 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; 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   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;
DR   PRODOM; Q75C78.
DR   SWISS-2DPAGE; Q75C78.
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   NP_BIND         55..58
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   NP_BIND         244..246
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   NP_BIND         310..317
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   NP_BIND         381..384
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
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   MOTIF           671..674
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   BINDING         114
FT                   /note="ATP"
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
//

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