ID   BIP_SCHPO               Reviewed;         663 AA.
AC   P36604; O13906;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   27-MAR-2024, entry version 178.
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=bip1; Synonyms=bip; ORFNames=SPAC22A12.15c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1373379; DOI=10.1002/j.1460-2075.1992.tb05203.x;
RA   Pidoux A.L., Armstrong J.;
RT   "Analysis of the BiP gene and identification of an ER retention signal in
RT   Schizosaccharomyces pombe.";
RL   EMBO J. 11:1583-1591(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(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   -!- PTM: Partially N-glycosylated.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; X64416; CAA45762.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB16585.1; -; Genomic_DNA.
DR   PIR; S20877; S20877.
DR   PIR; T38155; T38155.
DR   RefSeq; NP_593245.1; NM_001018642.2.
DR   AlphaFoldDB; P36604; -.
DR   SMR; P36604; -.
DR   BioGRID; 278306; 9.
DR   ELM; P36604; -.
DR   IntAct; P36604; 2.
DR   STRING; 284812.P36604; -.
DR   GlyCosmos; P36604; 1 site, No reported glycans.
DR   iPTMnet; P36604; -.
DR   MaxQB; P36604; -.
DR   PaxDb; 4896-SPAC22A12-15c-1; -.
DR   EnsemblFungi; SPAC22A12.15c.1; SPAC22A12.15c.1:pep; SPAC22A12.15c.
DR   GeneID; 2541815; -.
DR   KEGG; spo:SPAC22A12.15c; -.
DR   PomBase; SPAC22A12.15c; bip1.
DR   VEuPathDB; FungiDB:SPAC22A12.15c; -.
DR   eggNOG; KOG0100; Eukaryota.
DR   HOGENOM; CLU_005965_2_1_1; -.
DR   InParanoid; P36604; -.
DR   OMA; AYTKNQD; -.
DR   PhylomeDB; P36604; -.
DR   PRO; PR:P36604; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0099021; C:cortical endoplasmic reticulum lumen; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:CACAO.
DR   GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:PomBase.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0031965; C:nuclear membrane; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0099020; C:perinuclear endoplasmic reticulum lumen; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IC:PomBase.
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:0051082; F:unfolded protein binding; ISO:PomBase.
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; IMP:PomBase.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:PomBase.
DR   CDD; cd10241; HSPA5-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 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; Glycoprotein; Hydrolase;
KW   Nucleotide-binding; Reference proteome; Signal; Stress response.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..663
FT                   /note="Endoplasmic reticulum chaperone BiP"
FT                   /id="PRO_0000013585"
FT   REGION          131..285
FT                   /note="Nucleotide-binding (NBD)"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   REGION          404..504
FT                   /note="Substrate-binding (SBD)"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   REGION          639..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           660..663
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   COMPBIAS        646..663
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         43..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   BINDING         102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   BINDING         232..234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   BINDING         298..305
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   BINDING         369..372
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        173
FT                   /note="A -> S (in Ref. 1; CAA45762)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        301..302
FT                   /note="KR -> NG (in Ref. 1; CAA45762)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        336..345
FT                   /note="NMDLFKKTLK -> KHGSLQEDFE (in Ref. 1; CAA45762)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   663 AA;  73227 MW;  9DB80112E6C35742 CRC64;
     MKKFQLFSIL SYFVALFLLP MAFASGDDNS TESYGTVIGI DLGTTYSCVA VMKNGRVEII
     ANDQGNRITP SYVAFTEDER LVGEAAKNQA PSNPENTIFD IKRLIGRKFD EKTMAKDIKS
     FPFHIVNDKN RPLVEVNVGG KKKKFTPEEI SAMILSKMKQ TAEAYLGKPV THAVVTVPAY
     FNDAQRQATK DAGTIAGLNV IRIVNEPTAA AIAYGLDKTD TEKHIVVYDL GGGTFDVSLL
     SIDNGVFEVL ATSGDTHLGG EDFDNRVINY LARTYNRKNN VDVTKDLKAM GKLKREVEKA
     KRTLSSQKSV RIEIESFFNG QDFSETLSRA KFEEINMDLF KKTLKPVEQV LKDSNLKKSE
     IDDIVLVGGS TRIPKVQELL ESFFGKKASK GINPDEAVAY GAAVQAGVLS GEEGSDNIVL
     LDVIPLTLGI ETTGGVMTKL IGRNTPIPTR KSQIFSTAVD NQNTVLIQVY EGERTLTKDN
     NLLGKFDLRG IPPAPRGVPQ IEVTFEVDAN GVLTVSAVDK SGKGKPEKLV IKNDKGRLSE
     EDIERMVKEA EEFAEEDKIL KERIEARNTL ENYAYSLKGQ FDDDEQLGGK VDPEDKQAVL
     DAVEDVAEWL EIHGEDASKE EFEDQRQKLD AVVHPITQKL YSEGAGDADE EDDDYFDDEA
     DEL
//