BIP_SCHPO
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 03-AUG-2022, entry version 171.
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; 8.
DR ELM; P36604; -.
DR IntAct; P36604; 2.
DR STRING; 4896.SPAC22A12.15c.1; -.
DR iPTMnet; P36604; -.
DR MaxQB; P36604; -.
DR PaxDb; P36604; -.
DR PRIDE; P36604; -.
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; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:PomBase.
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; ISO:PomBase.
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; 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; 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..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
