BIBH_CAEEL
ID BIBH_CAEEL Reviewed; 657 AA.
AC P20163; O02085;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Endoplasmic reticulum chaperone BiP homolog {ECO:0000305};
DE AltName: Full=Heat shock 70 kDa protein D;
DE EC=3.6.4.10 {ECO:0000250|UniProtKB:P11021};
DE Flags: Precursor;
GN Name=hsp-4; Synonyms=hsp70d; ORFNames=F43E2.8;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 370-657.
RX PubMed=2744444; DOI=10.1139/g89-428;
RA Heschl M.F.P., Baillie D.L.;
RT "Identification of a heat-shock pseudogene from Caenorhabditis elegans.";
RL Genome 32:190-195(1989).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15716356; DOI=10.1091/mbc.e04-08-0726;
RA Poteryaev D., Squirrell J.M., Campbell J.M., White J.G., Spang A.;
RT "Involvement of the actin cytoskeleton and homotypic membrane fusion in ER
RT dynamics in Caenorhabditis elegans.";
RL Mol. Biol. Cell 16:2139-2153(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 420-568.
RA Osipiuk J., Duggan E., Gu M., Voisine C., Morimoto R.I., Joachimiak A.;
RT "X-ray structure of peptide-binding domain of Heat shock 70 kDa protein D
RT precursor from C.elegans.";
RL Submitted (JAN-2007) to the PDB data bank.
CC -!- FUNCTION: Endoplasmic reticulum chaperone that plays a key role in
CC protein folding and quality control in the endoplasmic reticulum lumen
CC (By similarity). Required for ER dynamics during the first embryonic
CC cell divisions (PubMed:15716356). Specifically, controls ER transition
CC into sheet-like structures at the onset of mitosis, possibly by
CC regulating homotypic membrane fusion (PubMed:15716356).
CC {ECO:0000250|UniProtKB:P11021, ECO:0000269|PubMed:15716356}.
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:P11021}.
CC -!- INDUCTION: By endoplasmic reticulum stress.
CC {ECO:0000250|UniProtKB:P11021}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown prevents the formation of
CC ER sheet-like structures during mitosis in the 1-cell embryo. ER
CC accumulates in foci throughout mitosis and partially fails to disperse
CC at the end of mitosis. {ECO:0000269|PubMed:15716356}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; FO080417; CCD63548.1; -; Genomic_DNA.
DR EMBL; M28528; AAA28076.1; -; Genomic_DNA.
DR PIR; T34037; T34037.
DR RefSeq; NP_495536.1; NM_063135.6.
DR PDB; 2OP6; X-ray; 1.85 A; A=420-568.
DR PDBsum; 2OP6; -.
DR AlphaFoldDB; P20163; -.
DR SMR; P20163; -.
DR BioGRID; 39538; 13.
DR DIP; DIP-26704N; -.
DR IntAct; P20163; 3.
DR STRING; 6239.F43E2.8.1; -.
DR World-2DPAGE; 0020:P20163; -.
DR EPD; P20163; -.
DR PaxDb; P20163; -.
DR PeptideAtlas; P20163; -.
DR PRIDE; P20163; -.
DR EnsemblMetazoa; F43E2.8a.1; F43E2.8a.1; WBGene00002008.
DR EnsemblMetazoa; F43E2.8a.2; F43E2.8a.2; WBGene00002008.
DR GeneID; 174203; -.
DR UCSC; F43E2.8.1; c. elegans.
DR CTD; 174203; -.
DR WormBase; F43E2.8a; CE07244; WBGene00002008; hsp-4.
DR eggNOG; KOG0100; Eukaryota.
DR HOGENOM; CLU_005965_3_0_1; -.
DR InParanoid; P20163; -.
DR OMA; DSKPCIE; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; P20163; -.
DR EvolutionaryTrace; P20163; -.
DR PRO; PR:P20163; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00002008; Expressed in adult organism and 4 other tissues.
DR ExpressionAtlas; P20163; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; ISS:WormBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:WormBase.
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:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
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; IEP:WormBase.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Endoplasmic reticulum; Hydrolase;
KW Nucleotide-binding; Reference proteome; Signal; Stress response.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..657
FT /note="Endoplasmic reticulum chaperone BiP homolog"
FT /id="PRO_0000013542"
FT REGION 128..282
FT /note="Nucleotide-binding (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 402..502
FT /note="Substrate-binding (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 607..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 654..657
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT BINDING 38..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 229..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 295..302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 366..369
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT CONFLICT 454
FT /note="S -> P (in Ref. 2; AAA28076)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="M -> I (in Ref. 2; AAA28076)"
FT /evidence="ECO:0000305"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:2OP6"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:2OP6"
FT STRAND 434..439
FT /evidence="ECO:0007829|PDB:2OP6"
FT STRAND 444..457
FT /evidence="ECO:0007829|PDB:2OP6"
FT STRAND 463..471
FT /evidence="ECO:0007829|PDB:2OP6"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:2OP6"
FT STRAND 478..486
FT /evidence="ECO:0007829|PDB:2OP6"
FT STRAND 499..505
FT /evidence="ECO:0007829|PDB:2OP6"
FT STRAND 511..517
FT /evidence="ECO:0007829|PDB:2OP6"
FT TURN 518..520
FT /evidence="ECO:0007829|PDB:2OP6"
FT STRAND 523..528
FT /evidence="ECO:0007829|PDB:2OP6"
FT STRAND 530..533
FT /evidence="ECO:0007829|PDB:2OP6"
FT HELIX 537..549
FT /evidence="ECO:0007829|PDB:2OP6"
FT HELIX 551..560
FT /evidence="ECO:0007829|PDB:2OP6"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:2OP6"
SQ SEQUENCE 657 AA; 72288 MW; 0C046D3EF1B5592F CRC64;
MKVFSLILIA FVANAYCDEG ASTEKEEKMG TIIGIDLGTT YSCVGVFKNG RVEIIANDQG
NRITPSYVAF SGDQGERLIG DAAKNQLTIN PENTIFDAKR LIGRFYNEKT VQQDIKHWPF
KIVDKSNKPN VEVKVGSETK QFTPEEVSAM VLTKMKQIAE SYLGHEVKNA VVTVPAYFND
AQKQATKDAG SIAGLNVVRI INEPTAAAIA YGLDKKDGER NILVFDLGGG TFDVSLLTID
SGVFEVLATN GDTHLGGEDF DQRVMEYFIK LYKKKSGKDL RKDNRAVQKL RREVEKAKRA
LSTQHQTKIE IESLFDGEDF SETLTRAKFE ELNMDLFRAT LKPVQKVLED ADMKKTDVHE
IVLVGGSTRI PKVQQLIKDY FNGKEPSRGI NPDEAVAYGA AVQAGVIGGV ENTGDVVLLD
VNPLTLGIET VGGVMTKLIG RNTVIPTKKS QVFSTAADSQ SAVSIVIYEG ERPMVMDNHK
LGNFDVTGIP PAPRGVPQIE VTFEIDVNGI LHVSAEDKGT GNKNKLTITN DHNRLSPEDI
ERMINDADKF AADDQAQKEK VESRNELEAY AYQMKTQIAD KEKLGGKLTD EDKVSIESAV
ERAIEWLGSN QDASTEENKE QKKELESVVQ PIVSKLYSAG GQGEQASEEP SEDHDEL
