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P08113 (ENPL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoplasmin
Alternative name(s):
94 kDa glucose-regulated protein
Short name=GRP-94
Endoplasmic reticulum resident protein 99
Short name=ERp99
Heat shock protein 90 kDa beta member 1
Polymorphic tumor rejection antigen 1
Tumor rejection antigen gp96
Gene names
Name:Hsp90b1
Synonyms:Grp94, Tra-1, Tra1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length802 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity By similarity. Ref.10

Subunit structure

Homodimer; disulfide-linked. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Interacts with OS9 By similarity. Interacts with AIMP1; regulates its retention in the endoplasmic reticulum. Interacts with CNPY3; this interaction is disrupted in the presence of ATP. Interacts with TLR4, TLR9 and TLR11, but not with TLR3. Interacts with MZB1 in a calcium-dependent manner. Ref.6 Ref.8 Ref.9 Ref.10 Ref.12

Subcellular location

Endoplasmic reticulum lumen. Melanosome By similarity Ref.10.

Sequence similarities

Belongs to the heat shock protein 90 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainSignal
   LigandATP-binding
Calcium
Nucleotide-binding
   Molecular functionChaperone
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processER-associated protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

actin rod assembly

Inferred from sequence orthology PubMed 19000834. Source: MGI

cellular response to ATP

Inferred from sequence orthology PubMed 19000834. Source: MGI

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Compara

protein folding

Inferred from electronic annotation. Source: InterPro

regulation of phosphoprotein phosphatase activity

Inferred from sequence orthology PubMed 19000834. Source: MGI

response to hypoxia

Inferred from electronic annotation. Source: Compara

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Compara

endoplasmic reticulum

Inferred from direct assay PubMed 10444069PubMed 12135983. Source: MGI

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: Compara

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from electronic annotation. Source: Compara

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Compara

plasma membrane part

Inferred from direct assay PubMed 15252132. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: Compara

low-density lipoprotein particle receptor binding

Inferred from sequence orthology PubMed 15082773. Source: MGI

protein phosphatase binding

Inferred from sequence orthology PubMed 19000834. Source: MGI

virion binding

Inferred from electronic annotation. Source: Compara

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 802781Endoplasmin
PRO_0000013599

Regions

Motif799 – 8024Prevents secretion from ER

Sites

Binding site1071ATP By similarity
Binding site1491ATP By similarity
Binding site1621ATP By similarity
Binding site1681ATP By similarity
Binding site1991ATP; via amide nitrogen By similarity
Binding site4481ATP By similarity

Amino acid modifications

Modified residue3061Phosphoserine Ref.13
Glycosylation621N-linked (GlcNAc...) Potential
Glycosylation1071N-linked (GlcNAc...) Potential
Glycosylation2171N-linked (GlcNAc...) Ref.14
Glycosylation4451N-linked (GlcNAc...) Potential
Glycosylation4811N-linked (GlcNAc...) Potential
Glycosylation5021N-linked (GlcNAc...) Potential
Disulfide bond138Interchain Ref.6

Experimental info

Mutagenesis1031E → A: Loss of CNPY3-binding. Ref.10

Sequences

Sequence LengthMass (Da)Tools
P08113 [UniParc].

Last modified April 1, 1990. Version 2.
Checksum: BDF33B9BD86BFC5F

FASTA80292,476
        10         20         30         40         50         60 
MRVLWVLGLC CVLLTFGFVR ADDEVDVDGT VEEDLGKSRE GSRTDDEVVQ REEEAIQLDG 

        70         80         90        100        110        120 
LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF LRELISNASD ALDKIRLISL 

       130        140        150        160        170        180 
TDENALAGNE ELTVKIKCDK EKNLLHVTDT GVGMTREELV KNLGTIAKSG TSEFLNKMTE 

       190        200        210        220        230        240 
AQEDGQSTSE LIGQFGVGFY SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT 

       250        260        270        280        290        300 
LGRGTTITLV LKEEASDYLE LDTIKNLVRK YSQFINFPIY VWSSKTETVE EPLEEDEAAK 

       310        320        330        340        350        360 
EEKEESDDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV EEDEYKAFYK 

       370        380        390        400        410        420 
SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE YGSKKSDYIK LYVRRVFITD 

       430        440        450        460        470        480 
DFHDMMPKYL NFVKGVVDSD DLPLNVSRET LQQHKLLKVI RKKLVRKTLD MIKKIADEKY 

       490        500        510        520        530        540 
NDTFWKEFGT NIKLGVIEDH SNRTRLAKLL RFQSSHHSTD ITSLDQYVER MKEKQDKIYF 

       550        560        570        580        590        600 
MAGSSRKEAE SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE 

       610        620        630        640        650        660 
SEKTKESREA TEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS QYGWSGNMER 

       670        680        690        700        710        720 
IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIRDMLRR IKEDEDDKTV MDLAVVLFET 

       730        740        750        760        770        780 
ATLRSGYLLP DTKAYGDRIE RMLRLSLNID PEAQVEEEPE EEPEDTSEDA EDSEQDEGEE 

       790        800 
MDAGTEEEEE ETEKESTEKD EL

« Hide

References

« Hide 'large scale' references
[1]"ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94)."
Mazzarella R.A., Green M.
J. Biol. Chem. 262:8875-8883(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 76-84; 88-95; 117-135; 143-156; 244-265; 270-285; 385-404; 416-428; 435-448; 512-530; 609-623 AND 640-660, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[3]"Isolation and identification of partial cDNA clones for endoplasmin, the major glycoprotein of mammalian endoplasmic reticulum."
Smith M.J., Koch G.L.E.
J. Mol. Biol. 194:345-347(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 378-507.
[4]"5'-structural analysis of genes encoding polymorphic antigens of chemically induced tumors."
Srivastava P.K., Chen Y.-T., Old L.J.
Proc. Natl. Acad. Sci. U.S.A. 84:3807-3811(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-88.
[5]"HSP100, a 100-kDa heat shock protein, is a Ca2+-calmodulin-regulated actin-binding protein."
Koyasu S., Nishida E., Miyata Y., Sakai H., Yahara I.
J. Biol. Chem. 264:15083-15087(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 271-284; 328-339 AND 633-659.
[6]"Analysis of the structure and synthesis of GRP94, an abundant stress protein of the endoplasmic reticulum."
Qu D., Mazzarella R.A., Green M.
DNA Cell Biol. 13:117-124(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERCHAIN DISULFIDE BOND.
[7]"A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins."
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.
Mol. Biol. Cell 13:4456-4469(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPONENT OF A CHAPERONE COMPLEX.
[8]"Age-specific CUGBP1-eIF2 complex increases translation of CCAAT/enhancer-binding protein beta in old liver."
Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H., Hershey J.W., Timchenko N.A.
J. Biol. Chem. 281:32806-32819(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN AN EIF2 COMPLEX WITH EIF2S1; EIF2S2; CELF1; CALR3; HSPA5 AND CALR.
[9]"Mzb1 protein regulates calcium homeostasis, antibody secretion, and integrin activation in innate-like B cells."
Flach H., Rosenbaum M., Duchniewicz M., Kim S., Zhang S.L., Cahalan M.D., Mittler G., Grosschedl R.
Immunity 33:723-735(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MZB1.
[10]"Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone."
Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B., Bona R., Han D., Li Z.
Nat. Commun. 1:79-79(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CNPY3; TLR4; TLR9 AND TLR11, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-103.
[11]Erratum
Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B., Bona R., Han D., Li Z.
Nat. Commun. 3:653-653(2012)
[12]"Aminoacyl-tRNA synthetase-interacting multifunctional protein 1/p43 controls endoplasmic reticulum retention of heat shock protein gp96: its pathological implications in lupus-like autoimmune diseases."
Han J.M., Park S.G., Liu B., Park B.-J., Kim J.Y., Jin C.H., Song Y.W., Li Z., Kim S.
Am. J. Pathol. 170:2042-2054(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AIMP1.
[13]"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry."
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.
J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, MASS SPECTROMETRY.
Tissue: Liver.
[14]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-217, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J03297 mRNA. Translation: AAA37573.1.
M29652 mRNA. Translation: AAA37743.1.
M16370 mRNA. Translation: AAA40023.1.
IPIIPI00129526.
PIRA29317.
RefSeqNP_035761.1. NM_011631.1.
UniGeneMm.87773.

3D structure databases

ProteinModelPortalP08113.
SMRP08113. Positions 72-755.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-32352N.
IntActP08113. 3 interactions.

PTM databases

PhosphoSiteP08113.

2D gel databases

REPRODUCTION-2DPAGEP08113.
SWISS-2DPAGEP08113.

Proteomic databases

PaxDbP08113.
PRIDEP08113.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020238; ENSMUSP00000020238; ENSMUSG00000020048.
GeneID22027.
KEGGmmu:22027.

Organism-specific databases

CTD7184.
MGIMGI:98817. Hsp90b1.

Phylogenomic databases

eggNOGCOG0326.
HOGENOMHOG000031988.
HOVERGENHBG007374.
InParanoidP08113.
KOK09487.
OMAHITDTGI.
OrthoDBEOG4Z62N4.

Gene expression databases

ArrayExpressP08113.
BgeeP08113.
CleanExMM_HSP90B1.
GenevestigatorP08113.
GermOnlineENSMUSG00000020048. Mus musculus.

Family and domain databases

Gene3D3.30.565.10. 2 hits.
InterProIPR015566. Endoplasmin.
IPR003594. HATPase_ATP-bd.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERPTHR11528. PTHR11528. 1 hit.
PTHR11528:SF21. PTHR11528:SF21. 1 hit.
PfamPF00183. HSP90. 1 hit.
[Graphical view]
PIRSFPIRSF002583. Hsp90. 1 hit.
PRINTSPR00775. HEATSHOCK90.
SMARTSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMSSF55874. ATP_bd_ATPase. 1 hit.
SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00298. HSP90. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHSP90B1. mouse.
NextBio301772.
PMAP-CutDBP08113.
SOURCESearch...

Entry information

Entry nameENPL_MOUSE
AccessionPrimary (citable) accession number: P08113
Secondary accession number(s): P11427
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: April 1, 1990
Last modified: May 1, 2013
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents