ENPL_RABIT
ID ENPL_RABIT Reviewed; 716 AA.
AC O18750;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Endoplasmin;
DE AltName: Full=94 kDa glucose-regulated protein;
DE Short=GRP-94;
DE AltName: Full=Heat shock protein 90 kDa beta member 1;
DE Flags: Fragment;
GN Name=HSP90B1; Synonyms=GRP94 {ECO:0000303|PubMed:9601063};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=New Zealand white;
RX PubMed=9601063; DOI=10.1042/bj3320351;
RA Vitadello M., Colpo P., Gorza L.;
RT "Rabbit cardiac and skeletal myocytes differ in constitutive and inducible
RT expression of the glucose-regulated protein GRP94.";
RL Biochem. J. 332:351-359(1998).
CC -!- FUNCTION: Molecular chaperone that functions in the processing and
CC transport of secreted proteins. When associated with CNPY3, required
CC for proper folding of Toll-like receptors. Functions in endoplasmic
CC reticulum associated degradation (ERAD). Has ATPase activity. May
CC participate in the unfolding of cytosolic leaderless cargos (lacking
CC the secretion signal sequence) such as the interleukin 1/IL-1 to
CC facilitate their translocation into the ERGIC (endoplasmic reticulum-
CC Golgi intermediate compartment) and secretion; the translocation
CC process is mediated by the cargo receptor TMED10 (By similarity).
CC {ECO:0000250|UniProtKB:P08113, ECO:0000250|UniProtKB:P14625}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Component of an EIF2 complex at
CC least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1
CC and HSPA5 (By similarity). Part of a large chaperone multiprotein
CC complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6,
CC PPIB, SDF2L1, UGGT1 and very small amounts of ERP29, but not, or at
CC very low levels, CALR nor CANX. Interacts with AIMP1; regulates its
CC retention in the endoplasmic reticulum. Interacts with OS9 (By
CC similarity). Interacts with CNPY3; this interaction is disrupted in the
CC presence of ATP. Interacts with several TLRs, including TLR4 and TLR9,
CC but not with TLR3 (By similarity). Interacts with MZB1 in a calcium-
CC dependent manner (By similarity). Interacts with METTL23 (By
CC similarity). Interacts with IL1B; the interaction facilitates cargo
CC translocation into the ERGIC (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P14625}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:Q66HD0}. Sarcoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:P41148}. Melanosome
CC {ECO:0000250|UniProtKB:P14625}.
CC -!- TISSUE SPECIFICITY: Detected in heart, skeletal muscle, liver and
CC brain. {ECO:0000269|PubMed:9601063}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; AF001631; AAC48853.1; -; mRNA.
DR AlphaFoldDB; O18750; -.
DR SMR; O18750; -.
DR STRING; 9986.ENSOCUP00000014008; -.
DR PRIDE; O18750; -.
DR eggNOG; KOG0020; Eukaryota.
DR InParanoid; O18750; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Calcium; Chaperone; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Hydroxylation; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Sarcoplasmic reticulum.
FT CHAIN <1..716
FT /note="Endoplasmin"
FT /id="PRO_0000062927"
FT REGION 211..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 713..716
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT COMPBIAS 215..235
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..700
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT SITE 368
FT /note="Important for ATP hydrolysis"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT MOD_RES 89
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P14625"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66HD0"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66HD0"
FT MOD_RES 324
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08113"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14625"
FT MOD_RES 399
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08113"
FT MOD_RES 552
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08113"
FT MOD_RES 696
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14625"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 716 AA; 82608 MW; 7098C6442F0EC84B CRC64;
AEVNRMMKLI INSLYKNKEI FLRELISNAS DALDKIRLIS LTDEQALSGN EELTVKIKCD
KEKNLLHVTD TGVGMTREEL VKNLGTIAKS GTSEFLNKMT EAQEDGQSTS ELIGQFGVGF
YSAFLVADKV IVTSKHNNDT QHIWESDSNE FSVIADPRGN TLGRGTTITL VLKEEASDYL
ELDTIKNLVK KYSQFINFPI YVWSSKTETV EEPAGEEEAA KEEKEEAVDE AAVEEEEEEK
KPKTKKVEKQ VWDWELMNDI KPIWQRPSKE VEEDEYKAFY KSFSKESDDP MAYIHFTAEE
STFKSILFVP TSAPRGLFDE YGSKKSDYIK LYVRRVFITD DFHDMMPKYL NFVKGVVDSD
DLPLNVSRET LQQHKLLKVI RKKLVRKTLD MIKKIADEKY NDDTFWKGTN IKLGVIEDHS
NRTRLAKLLR FQSSHHPTDI TSLDQYVERM KEKQDKIYFM AGASRKEAES SPFVERLLKK
GYEVIYLTEP VDEYCIQALP EFDGKRFQNV AKEGVKFDES EKTKESREAT EKEFEPLLNW
MKDKALKDKI EKAVVSQRLT ESPCALVASQ YGWSANMERI MKAQAYQTGK DSTKYYASQK
TFEINPRHPL IRDMLRIKED DKTVMDLAVV LFETAILRSG YLLPDTKAYG DRIERIVRLS
LNIDPDAKVE EEPEEEPEDT TEDTEQDEEE EMDAGTDEQE QEQEPEKKST AEKDEL
