Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q29092 (ENPL_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 120. 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
98 kDa protein kinase
Short name=PPK 98
Short name=ppk98
Heat shock protein 90 kDa beta member 1
gp96 homolog
Gene names
Name:HSP90B1
Synonyms:GRP94, TRA1
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length804 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Subcellular location

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

Post-translational modification

Phosphorylated By similarity. HAMAP-Rule MF_00505

Sequence similarities

Belongs to the heat shock protein 90 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 804783Endoplasmin HAMAP-Rule MF_00505
PRO_0000013600

Regions

Motif801 – 8044Prevents secretion from ER Potential

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 By similarity
Modified residue4041N6-succinyllysine By similarity
Modified residue4791N6-acetyllysine By similarity
Modified residue6331N6-succinyllysine By similarity
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

Sequence conflict481V → I in CAA70347. Ref.2
Sequence conflict1791A → T in CAA70347. Ref.2
Sequence conflict332 – 3343DWE → ELG in CAA62352. Ref.3
Sequence conflict7951E → EFVFQ in CAA62352. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q29092 [UniParc].

Last modified December 13, 2001. Version 3.
Checksum: FF823A77406F0190

FASTA80492,471
        10         20         30         40         50         60 
MRALWVLGLC CVLLTFGSVR AEDEVDVDGT 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 TSEFLNKMAE 

       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 
EEKEESDDEA 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 
SEKSKENREA VEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS QYGWSGNMER 

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

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

       790        800 
EMDAGADEEE QETSETSTAE KDEL 

« Hide

References

[1]"A protein kinase isolated from porcine brain microvessels is similar to a class of heat-shock proteins."
Dechert U., Weber P., Koenig B., Ortwein C., Nilson I., Linxweiler W., Wollny E., Gassen H.G.
Eur. J. Biochem. 225:805-809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Structurally related high density lipoprotein-binding proteins in liver I: identification as gp96/GRP94."
de Crom R.P.G., van Haperen R., Janssens R., Visser P., van der Kamp A.W.M.
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"Cloning and characterization of a porcine protein kinase gene and relationship to a class of heat shock proteins."
Koenig B., Seehaus B., Bangsow T., Bangsow T., Henninger J., Weber P., Schepelmann S., Wollny E., Gassen H.G.
DNA Cell Biol. 16:1365-1372(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X76301 mRNA. Translation: CAA53948.1.
Y09136 mRNA. Translation: CAA70347.1.
X90848 Genomic DNA. Translation: CAA62352.1.
PIRPL0137.
S51358.
RefSeqNP_999268.1. NM_214103.1.
UniGeneSsc.94181.
Ssc.9889.

3D structure databases

ProteinModelPortalQ29092.
SMRQ29092. Positions 69-755.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ29092.
PRIDEQ29092.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397191.
KEGGssc:397191.

Organism-specific databases

CTD7184.

Phylogenomic databases

eggNOGCOG0326.
HOGENOMHOG000031988.
HOVERGENHBG007374.
KOK09487.

Family and domain databases

Gene3D3.30.565.10. 2 hits.
HAMAPMF_00505. HSP90.
InterProIPR003594. 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.
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. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00298. HSP90. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ29092.

Entry information

Entry nameENPL_PIG
AccessionPrimary (citable) accession number: Q29092
Secondary accession number(s): O19070, Q29091
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 13, 2001
Last modified: June 11, 2014
This is version 120 of the entry and version 3 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