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Protein

Endoplasmin

Gene

HSP90B1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei107 – 1071ATPBy similarity
Binding sitei149 – 1491ATPBy similarity
Binding sitei162 – 1621ATPBy similarity
Binding sitei168 – 1681ATPBy similarity
Binding sitei199 – 1991ATP; via amide nitrogenBy similarity
Binding sitei448 – 4481ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  2. protein folding Source: InterPro
  3. response to stress Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Calcium, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:HSP90B1
Synonyms:GRP94, TRA1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  2. melanosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 804783EndoplasminPRO_0000013600Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
Modified residuei64 – 641PhosphoserineBy similarity
Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi138 – 138InterchainBy similarity
Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence Analysis
Modified residuei306 – 3061PhosphoserineBy similarity
Modified residuei404 – 4041N6-succinyllysineBy similarity
Glycosylationi445 – 4451N-linked (GlcNAc...)Sequence Analysis
Modified residuei447 – 4471PhosphoserineBy similarity
Modified residuei479 – 4791N6-acetyllysineBy similarity
Glycosylationi481 – 4811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi502 – 5021N-linked (GlcNAc...)Sequence Analysis
Modified residuei633 – 6331N6-succinyllysineBy similarity

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ29092.
PRIDEiQ29092.

Interactioni

Subunit structurei

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).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ29092.
SMRiQ29092. Positions 69-755.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi801 – 8044Prevents secretion from ERSequence Analysis

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0326.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiQ29092.
KOiK09487.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90.
InterProiIPR003594. HATPase_C.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF00183. HSP90. 1 hit.
[Graphical view]
PIRSFiPIRSF002583. Hsp90. 1 hit.
PRINTSiPR00775. HEATSHOCK90.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00298. HSP90. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q29092-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRALWVLGLC CVLLTFGSVR AEDEVDVDGT VEEDLGKSRE GSRTDDEVVQ
60 70 80 90 100
REEEAIQLDG LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF
110 120 130 140 150
LRELISNASD ALDKIRLISL TDENALAGNE ELTVKIKCDK EKNLLHVTDT
160 170 180 190 200
GVGMTREELV KNLGTIAKSG TSEFLNKMAE AQEDGQSTSE LIGQFGVGFY
210 220 230 240 250
SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT LGRGTTITLV
260 270 280 290 300
LKEEASDYLE LDTIKNLVKK YSQFINFPIY VWSSKTETVE EPMEEEEAAK
310 320 330 340 350
EEKEESDDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV
360 370 380 390 400
EDDEYKAFYK SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE
410 420 430 440 450
YGSKKSDYIK LYVRRVFITD DFHDMMPKYL NFVKGVVDSD DLPLNVSRET
460 470 480 490 500
LQQHKLLKVI RKKLVRKTLD MIKKIADEKY NDTFWKEFGT NIKLGVIEDH
510 520 530 540 550
SNRTRLAKLL RFQSSHHPSD ITSLDQYVER MKEKQDKIYF MAGSSRKEAE
560 570 580 590 600
SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE
610 620 630 640 650
SEKSKENREA VEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS
660 670 680 690 700
QYGWSGNMER IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIRDMLRR
710 720 730 740 750
VKEDEDDKTV SDLAVVLFET ATLRSGYLLP DTKAYGDRIE RMLRLSLNID
760 770 780 790 800
PDAKVEEEPE EEPEETTEDT TEDTEQDDDE EMDAGADEEE QETSETSTAE

KDEL
Length:804
Mass (Da):92,471
Last modified:December 13, 2001 - v3
Checksum:iFF823A77406F0190
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481V → I in CAA70347 (Ref. 2) Curated
Sequence conflicti179 – 1791A → T in CAA70347 (Ref. 2) Curated
Sequence conflicti332 – 3343DWE → ELG in CAA62352 (PubMed:9407008).Curated
Sequence conflicti795 – 7951E → EFVFQ in CAA62352 (PubMed:9407008).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76301 mRNA. Translation: CAA53948.1.
Y09136 mRNA. Translation: CAA70347.1.
X90848 Genomic DNA. Translation: CAA62352.1.
PIRiPL0137.
S51358.
RefSeqiNP_999268.1. NM_214103.1.
UniGeneiSsc.94181.
Ssc.9889.

Genome annotation databases

GeneIDi397191.
KEGGissc:397191.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76301 mRNA. Translation: CAA53948.1.
Y09136 mRNA. Translation: CAA70347.1.
X90848 Genomic DNA. Translation: CAA62352.1.
PIRiPL0137.
S51358.
RefSeqiNP_999268.1. NM_214103.1.
UniGeneiSsc.94181.
Ssc.9889.

3D structure databases

ProteinModelPortaliQ29092.
SMRiQ29092. Positions 69-755.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiQ29092.
PRIDEiQ29092.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397191.
KEGGissc:397191.

Organism-specific databases

CTDi7184.

Phylogenomic databases

eggNOGiCOG0326.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiQ29092.
KOiK09487.

Miscellaneous databases

PROiQ29092.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90.
InterProiIPR003594. HATPase_C.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF00183. HSP90. 1 hit.
[Graphical view]
PIRSFiPIRSF002583. Hsp90. 1 hit.
PRINTSiPR00775. HEATSHOCK90.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00298. HSP90. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1993) [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 (SEP-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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Liver.

Entry informationi

Entry nameiENPL_PIG
AccessioniPrimary (citable) accession number: Q29092
Secondary accession number(s): O19070, Q29091
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 13, 2001
Last modified: March 4, 2015
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.