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P08712 (ENPL_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Protein attributes

Sequence length400 AA.
Sequence statusFragment.
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.

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.

Subcellular location

Endoplasmic reticulum lumen. Melanosome By similarity.

Tissue specificity

Detected in the acrosome of the caput epididymal spermatazoa, not detected in the cauda epididymal spermatazoa (at protein level). Ref.2

Induction

The synthesis of this protein is stimulated when fibroblasts are deprived of glucose.

Post-translational modification

Phosphorylated By similarity.

Sequence similarities

Belongs to the heat shock protein 90 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 400›400Endoplasmin
PRO_0000062926

Regions

Motif397 – 4004Prevents secretion from ER

Sites

Binding site451ATP By similarity

Amino acid modifications

Modified residue11N6-succinyllysine By similarity
Modified residue761N6-acetyllysine By similarity
Modified residue2301N6-succinyllysine By similarity
Glycosylation421N-linked (GlcNAc...) Potential
Glycosylation781N-linked (GlcNAc...) Potential
Glycosylation991N-linked (GlcNAc...) Potential

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P08712 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 3419AD98410EEB80

FASTA40046,794
        10         20         30         40         50         60 
KKSDYIKLYV RRVFITDDFH DMMPKYLNFV KGVVDSDDLP LNVSRETLQQ HKLLKVIRKK 

        70         80         90        100        110        120 
LVRKTLDMIK KIADEKYNDT FWKEFGTNIK LGVIEDHSNR TRLAKLLRFQ SSHHSTDITS 

       130        140        150        160        170        180 
LDQYVERMKE KQDKIYFMAG SSRKEAESSP FVERLLKKGY EVIYLTEPVD EYCIQALPEF 

       190        200        210        220        230        240 
DGKRFQNVAK EGVKFDESEK TKENREATEK EFEPLLNWMK DKALKDKIEK AVVSQRLTES 

       250        260        270        280        290        300 
PCALVASQYG WSGNMERIMK AQAYQTGKDI STNYYASQKK TFEINPRHPL IRDMLRRVKE 

       310        320        330        340        350        360 
DEDDKTVLDL AVVLFETATL RSGYLLPDTK AYADRIERML RLSLNIDPEA QVEEEPEEEP 

       370        380        390        400 
EDTTEDTEQD EEEEVDAGTE EEEEEEQETA KESTAEKDEL 

« Hide

References

[1]"The glucose-regulated protein grp94 is related to heat shock protein hsp90."
Sorger P.K., Pelham H.R.B.
J. Mol. Biol. 194:341-344(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa."
Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.
Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04850 mRNA. Translation: CAA28541.1.
PIRA26258.

3D structure databases

ProteinModelPortalP08712.
SMRP08712. Positions 5-346.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP08712.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG007374.

Family and domain databases

InterProIPR001404. Hsp90_fam.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERPTHR11528. PTHR11528. 1 hit.
PfamPF00183. HSP90. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameENPL_MESAU
AccessionPrimary (citable) accession number: P08712
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: June 11, 2014
This is version 100 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