ENPL_RAT
ID ENPL_RAT Reviewed; 804 AA.
AC Q66HD0; A6IFJ6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Endoplasmin {ECO:0000250|UniProtKB:P08113};
DE AltName: Full=94 kDa glucose-regulated protein {ECO:0000250|UniProtKB:P08113};
DE Short=GRP-94;
DE AltName: Full=Heat shock protein 90 kDa beta member 1 {ECO:0000250|UniProtKB:P08113};
DE Flags: Precursor;
GN Name=Hsp90b1 {ECO:0000250|UniProtKB:P08113};
GN Synonyms=Grp94, Tra1 {ECO:0000312|EMBL:AAH81917.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAH81917.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15489334};
RC TISSUE=Testis {ECO:0000312|EMBL:AAH81917.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=19343716; DOI=10.1002/pmic.200800664;
RA Maurya D.K., Sundaram C.S., Bhargava P.;
RT "Proteome profile of the mature rat olfactory bulb.";
RL Proteomics 9:2593-2599(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172; SER-403 AND SER-447, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 TLR4, TLR9 and TLR11, but not with TLR3
CC (By similarity). Interacts with MZB1 in a calcium-dependent manner (By
CC similarity). Interacts with METTL23 (By similarity). Interacts with
CC IL1B; the interaction facilitates cargo translocation into the ERGIC
CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P14625}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:19343716}. Sarcoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:P41148}. Melanosome
CC {ECO:0000250|UniProtKB:P14625}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q66HD0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q66HD0-2; Sequence=VSP_035206;
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:P41148}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000255}.
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DR EMBL; CH473960; EDM17052.1; -; Genomic_DNA.
DR EMBL; BC081917; AAH81917.1; -; mRNA.
DR RefSeq; NP_001012197.2; NM_001012197.2. [Q66HD0-1]
DR AlphaFoldDB; Q66HD0; -.
DR SMR; Q66HD0; -.
DR BioGRID; 263786; 10.
DR IntAct; Q66HD0; 12.
DR MINT; Q66HD0; -.
DR STRING; 10116.ENSRNOP00000034846; -.
DR GlyGen; Q66HD0; 6 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q66HD0; -.
DR PhosphoSitePlus; Q66HD0; -.
DR World-2DPAGE; 0004:Q66HD0; -.
DR jPOST; Q66HD0; -.
DR PaxDb; Q66HD0; -.
DR PRIDE; Q66HD0; -.
DR Ensembl; ENSRNOT00000079731; ENSRNOP00000073056; ENSRNOG00000026963. [Q66HD0-2]
DR GeneID; 362862; -.
DR KEGG; rno:362862; -.
DR UCSC; RGD:1310482; rat. [Q66HD0-1]
DR CTD; 7184; -.
DR RGD; 1310482; Hsp90b1.
DR eggNOG; KOG0020; Eukaryota.
DR GeneTree; ENSGT01020000230401; -.
DR InParanoid; Q66HD0; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; Q66HD0; -.
DR TreeFam; TF105969; -.
DR Reactome; R-RNO-1679131; Trafficking and processing of endosomal TLR.
DR Reactome; R-RNO-3000480; Scavenging by Class A Receptors.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:Q66HD0; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; ISO:RGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0031247; P:actin rod assembly; ISO:RGD.
DR GO; GO:0071318; P:cellular response to ATP; ISO:RGD.
DR GO; GO:0071287; P:cellular response to manganese ion; IEP:ParkinsonsUK-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Calcium; Chaperone;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydroxylation;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Sarcoplasmic reticulum; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..804
FT /note="Endoplasmin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000349122"
FT REGION 288..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 801..804
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT COMPBIAS 290..314
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..804
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT SITE 448
FT /note="Important for ATP hydrolysis"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14625"
FT MOD_RES 168
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P14625"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 404
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08113"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 479
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08113"
FT MOD_RES 633
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08113"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 138
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P08113"
FT VAR_SEQ 631..804
FT /note="IEKAVVSQRLTESPCALVASQYGWSGNMERIMKAQAYQTGKDISTNYYASQK
FT KTFEINPRHPLIRDMLRRVKEDEDDKTVMDLAVVLFETATLRSGYLLPDTKAYGDRIER
FT MLRLSLNIDPEAQVEEEPEEEPEDTTEDTTDDSEQDEEETDAGAEEEEEEQETEKEPTE
FT KDEL -> VFGPQTVVSPHRN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035206"
SQ SEQUENCE 804 AA; 92771 MW; 5C1A2DC8ED6B1CC8 CRC64;
MRVLWVLGLC CVLLTFGFVR ADDEVDVDGT VEEDLGKSRE GSRTDDEVVQ REEEAIQLDG
LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF LRELISNASD ALDKIRLISL
TDENALAGNE ELTVKIKCDR EKNLLHVTDT GVGMTREELV KNLGTIAKSG TSEFLNKMTE
AQEDGQSTSE LIGQFGVGFY SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT
LGRGTTITLV LKEEASDYLE LDTIKNLVRK YSQFINFPIY VWSSKTETVE EPLEEDETAQ
EEKEEADDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV EEDEYKAFYK
SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE YGSKKSDYIK LYVRRVFITD
DFHDMMPKYL NFVKGVVDSD DLPLNVSRET LQQHKLLKVI RKKLVRKTLD MIKKIADEKY
NDTFWKEFGT NIKLGVIEDH SNRTRLAKLL RFQSSHHSTD ITSLDQYVER MKEKQDKIYF
MAGSSRKEAE SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE
SEKSKESREA TEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS QYGWSGNMER
IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIRDMLRR VKEDEDDKTV MDLAVVLFET
ATLRSGYLLP DTKAYGDRIE RMLRLSLNID PEAQVEEEPE EEPEDTTEDT TDDSEQDEEE
TDAGAEEEEE EQETEKEPTE KDEL
