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P41148 (ENPL_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 126. 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

Names and origin

Protein namesRecommended name:
Endoplasmin
Alternative name(s):
94 kDa glucose-regulated protein
Short name=GRP-94
Heat shock protein 90 kDa beta member 1
Gene names
Name:HSP90B1
Synonyms:GRP94, TRA1
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length804 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. HAMAP-Rule MF_00505

Subunit structure

Homodimer; disulfide-linked. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 By similarity. 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 AIMP1; regulates its retention in the endoplasmic reticulum. Interacts with OS9 By similarity. Interacts with CNPY3; this interaction is disrupted in the presence of ATP. Interacts with several TLRs, including TLR4 and TLR9, but not with TLR3 By similarity. Interacts with MZB1 in a calcium-dependent manner By similarity. Interacts with METTL23 By similarity. Ref.3 Ref.5

Subcellular location

Endoplasmic reticulum lumen. Sarcoplasmic reticulum. Melanosome By similarity HAMAP-Rule MF_00505.

Post-translational modification

Phosphorylated by CK2. Ref.1

Sequence similarities

Belongs to the heat shock protein 90 family.

Biophysicochemical properties

Kinetic parameters:

KM=10 µM for ATP Ref.5

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Sarcoplasmic reticulum
   DomainSignal
   LigandATP-binding
Calcium
Nucleotide-binding
   Molecular functionChaperone
   PTMAcetylation
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processER-associated ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

actin rod assembly

Inferred from electronic annotation. Source: Ensembl

cellular response to ATP

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

protein folding

Inferred from electronic annotation. Source: InterPro

regulation of phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: Ensembl

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

sarcoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: Ensembl

virion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 804783Endoplasmin HAMAP-Rule MF_00505
PRO_0000013597

Regions

Motif801 – 8044Prevents secretion from ER Potential

Sites

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

Amino acid modifications

Modified residue2881Phosphothreonine; by CK2 Potential
Modified residue3061Phosphoserine; by CK2 Potential
Modified residue4041N6-succinyllysine By similarity
Modified residue4791N6-acetyllysine By similarity
Modified residue6331N6-succinyllysine By similarity
Modified residue7661Phosphothreonine; by CK2 Potential
Modified residue7701Phosphothreonine; by CK2 Potential
Modified residue7741Phosphothreonine; by CK2 Potential
Modified residue7861Phosphothreonine; by CK2 Potential
Glycosylation621N-linked (GlcNAc...) Potential
Glycosylation1071N-linked (GlcNAc...) Potential
Glycosylation2171N-linked (GlcNAc...) Potential
Glycosylation4451N-linked (GlcNAc...) Potential
Glycosylation4811N-linked (GlcNAc...) Potential
Glycosylation5021N-linked (GlcNAc...) Potential
Disulfide bond138Interchain By similarity

Experimental info

Mutagenesis1031E → A: Loss of ATPase activity. Ref.5
Mutagenesis4481R → A: Reduces ATPase activity by 85%. Ref.5

Secondary structure

..................................................................................................................... 804
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P41148 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 36AA126EDCFFC2D5

FASTA80492,514
        10         20         30         40         50         60 
MRALWVLGLC CVLLTFGSVR 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 LDTIKNLVKK YSQFINFPIY VWSSKTETVE EPMEEEEAAK 

       310        320        330        340        350        360 
EEKEDSDDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV EDDEYKAFYK 

       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 RFQSSHHPSD ITSLDQYVER MKEKQDKIYF 

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

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

       670        680        690        700        710        720 
IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIKDMLRR VKEDEDDKTV SDLAVVLFET 

       730        740        750        760        770        780 
ATLRSGYLLP DTKAYGDRIE RMLRLSLNID PDAKVEEEPE EEPEETTEDT TEDTEQDDEE 

       790        800 
EMDAGTDDEE QETVKKSTAE KDEL 

« Hide

References

[1]"GRP94 resides within cardiac sarcoplasmic reticulum vesicles and is phosphorylated by casein kinase II."
Cala S.E., Jones L.R.
J. Biol. Chem. 269:5926-5931(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION.
Tissue: Heart.
[2]"Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation."
Soldano K.L., Jivan A., Nicchitta C.V., Gewirth D.T.
J. Biol. Chem. 278:48330-48338(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 69-337 IN COMPLEX WITH ADENOSINE ANALOG.
[3]"Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone."
Immormino R.M., Dollins D.E., Shaffer P.L., Soldano K.L., Walker M.A., Gewirth D.T.
J. Biol. Chem. 279:46162-46171(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 69-337 IN COMPLEXES WITH ATP; ADP AND AMP, SUBUNIT.
[4]"Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis for nucleotide-induced conformational change."
Dollins D.E., Immormino R.M., Gewirth D.T.
J. Biol. Chem. 280:30438-30447(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 69-337 OF APOPROTEIN AND IN COMPLEXES WITH ADP AND NECA.
[5]"Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones."
Dollins D.E., Warren J.J., Immormino R.M., Gewirth D.T.
Mol. Cell 28:41-56(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 73-754 IN COMPLEXES WITH AMPPNP AND ADP, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-103 AND ARG-448, CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U01153 mRNA. Translation: AAA17708.1.
PIRA53211.
RefSeqNP_001003327.1. NM_001003327.1.
UniGeneCfa.3896.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QY5X-ray1.75A69-337[»]
1QY8X-ray1.85A69-337[»]
1QYEX-ray2.10A69-337[»]
1TBWX-ray2.15A/B69-337[»]
1TC0X-ray2.20A/B69-337[»]
1TC6X-ray1.87A/B69-337[»]
1U0YX-ray2.30A69-337[»]
1U0ZX-ray1.90A/B69-337[»]
1U2OX-ray2.10A/B69-337[»]
1YSZX-ray2.65A69-337[»]
1YT0X-ray2.40A69-337[»]
1YT1X-ray2.20A/B69-337[»]
1YT2X-ray3.25A69-337[»]
2ESAX-ray1.90A69-337[»]
2EXLX-ray2.35A/B69-337[»]
2FYPX-ray1.95A/B69-337[»]
2GFDX-ray2.30A/B69-337[»]
2GQPX-ray1.50A/B69-337[»]
2H8MX-ray1.80A/B69-337[»]
2HCHX-ray2.30A/B69-337[»]
2HG1X-ray2.30A/B69-286[»]
2O1TX-ray3.20A/B/C/D/E/F/G/H/I/J336-765[»]
2O1UX-ray2.40A/B73-754[»]
2O1VX-ray2.45A/B73-754[»]
2O1WX-ray3.40A/B/C/D/E73-594[»]
3O2FX-ray2.00A/B69-337[»]
ProteinModelPortalP41148.
SMRP41148. Positions 69-755.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000011044.

Chemistry

BindingDBP41148.
ChEMBLCHEMBL4748.
DrugBankDB00131. Adenosine monophosphate.

Proteomic databases

PaxDbP41148.
PRIDEP41148.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID404019.
KEGGcfa:404019.

Organism-specific databases

CTD7184.

Phylogenomic databases

eggNOGCOG0326.
HOGENOMHOG000031988.
HOVERGENHBG007374.
InParanoidP41148.
KOK09487.

Family and domain databases

Gene3D3.30.565.10. 2 hits.
HAMAPMF_00505. HSP90.
InterProIPR015566. Endoplasmin.
IPR003594. HATPase_ATP-bd.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
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]
SUPFAMSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 2 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00298. HSP90. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP41148.
NextBio20817506.
PROP41148.

Entry information

Entry nameENPL_CANFA
AccessionPrimary (citable) accession number: P41148
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: March 19, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references