BIP_APLCA
ID BIP_APLCA Reviewed; 667 AA.
AC Q16956;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 AltName: Full=Protein 1603 {ECO:0000303|PubMed:1360013};
DE Flags: Precursor;
OS Aplysia californica (California sea hare).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC Aplysiidae; Aplysia.
OX NCBI_TaxID=6500;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 368-382.
RX PubMed=1360013; DOI=10.1083/jcb.119.5.1069;
RA Kuhl D., Kennedy T., Barzilai A., Kandel E.;
RT "Long-term sensitization training in Aplysia leads to an increase in the
RT expression of BiP, the major protein chaperon of the ER.";
RL J. Cell Biol. 119:1069-1076(1992).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z15041; CAA78759.1; -; mRNA.
DR PIR; D44261; D44261.
DR PIR; S24782; S24782.
DR RefSeq; NP_001191581.1; NM_001204652.1.
DR AlphaFoldDB; Q16956; -.
DR SMR; Q16956; -.
DR GeneID; 100533358; -.
DR OrthoDB; 288077at2759; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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 ATP-binding; Chaperone; Direct protein sequencing; Endoplasmic reticulum;
KW Hydrolase; Nucleotide-binding; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..667
FT /note="Endoplasmic reticulum chaperone BiP"
FT /id="PRO_0000013572"
FT REGION 135..289
FT /note="Nucleotide-binding (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 409..509
FT /note="Substrate-binding (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 641..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 664..667
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT BINDING 46..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 236..238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 302..309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 373..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
SQ SEQUENCE 667 AA; 73698 MW; A59EC27AF188141D CRC64;
MDRFTPFFLL VILFSSNLLV RADGDEEDEG DKKKSEVGTV IGIDLGTTYS CVGVFKNGRV
DIIANDQGNR ITPSYVAFTA DGERLIGDAA KNQLTSNPEN TIFDVKRLIG RTFDDKSVQH
DIKFYPFKVT NANNKPHIQA ATGEGDRSFA PEEISAMVLS KMRDIAEEYL GKKITNAVVT
VPAYFNDAQR QATKDAGTIA GLNVMRIINE PTAAAIAYGL DKKEGEKNIL VFDLGGGTFD
VSLLTIDNGV FEVVSTNGDT HLGGEDFDQR VMEHFIKLYK KKKGKDIRKD NRAVQKLRRE
VEKAKRALSS AHQVRLEIES FFDGEDFSES LTRAKFEELN MDLFRSTMKP VKQVLEDADL
KTDDIDEIVL VGGSTRIPKV QQLVKEYFNG KEPSRGINPD EAVAYGAAVQ AGVLSGEEDT
GDLVLLDVNP LTMGIETVGG VMTKLIPRNT VIPTKKSQIF STAADNQPTV TIQVYEGERS
MTKDNHLLGK FDLTGIPPAP RGVPQIEVTF EIDVNGILKV TAEDKGTGSK NQIVIQNDQN
RLSPEDIERM INDAEKYADE DKKVKEKVDA KNELESYAYS LKNQIGDKEK LGAKLSDEDK
EKITEAVDEA IKWLESNAEA ESEAFNEKKT ELEGIVQPIM TKLYEQSGGA PPPSGEEESE
EAEKDEL
