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P41148

- ENPL_CANFA

UniProt

P41148 - ENPL_CANFA

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Protein

Endoplasmin

Gene
HSP90B1, GRP94, TRA1
Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein 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.UniRule annotation

Kineticsi

  1. KM=10 µM for ATP1 Publication

Sites

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. RNA binding Source: Ensembl
  3. virion binding Source: Ensembl

GO - Biological processi

  1. actin rod assembly Source: Ensembl
  2. cellular response to ATP Source: Ensembl
  3. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  4. negative regulation of apoptotic process Source: Ensembl
  5. protein folding Source: InterPro
  6. regulation of phosphoprotein phosphatase activity Source: Ensembl
  7. response to hypoxia Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Calcium, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_203393. ATF6-alpha activates chaperone genes.
REACT_214911. Scavenging by Class A Receptors.
REACT_218639. Trafficking and processing of endosomal TLR.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoplasmin
Alternative name(s):
94 kDa glucose-regulated protein
Short name:
GRP-94
Heat shock protein 90 kDa beta member 1
Gene namesi
Name:HSP90B1
Synonyms:GRP94, TRA1
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  3. endoplasmic reticulum membrane Source: Ensembl
  4. melanosome Source: UniProtKB-SubCell
  5. midbody Source: Ensembl
  6. perinuclear region of cytoplasm Source: Ensembl
  7. plasma membrane Source: Ensembl
  8. sarcoplasmic reticulum Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Sarcoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi103 – 1031E → A: Loss of ATPase activity. 1 Publication
Mutagenesisi448 – 4481R → A: Reduces ATPase activity by 85%. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121 Reviewed predictionAdd
BLAST
Chaini22 – 804783EndoplasminUniRule annotationPRO_0000013597Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi62 – 621N-linked (GlcNAc...) Reviewed prediction
Glycosylationi107 – 1071N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi138 – 138Interchain By similarity
Glycosylationi217 – 2171N-linked (GlcNAc...) Reviewed prediction
Modified residuei288 – 2881Phosphothreonine; by CK2 Reviewed prediction
Modified residuei306 – 3061Phosphoserine; by CK2 Reviewed prediction
Modified residuei404 – 4041N6-succinyllysine By similarity
Glycosylationi445 – 4451N-linked (GlcNAc...) Reviewed prediction
Modified residuei479 – 4791N6-acetyllysine By similarity
Glycosylationi481 – 4811N-linked (GlcNAc...) Reviewed prediction
Glycosylationi502 – 5021N-linked (GlcNAc...) Reviewed prediction
Modified residuei633 – 6331N6-succinyllysine By similarity
Modified residuei766 – 7661Phosphothreonine; by CK2 Reviewed prediction
Modified residuei770 – 7701Phosphothreonine; by CK2 Reviewed prediction
Modified residuei774 – 7741Phosphothreonine; by CK2 Reviewed prediction
Modified residuei786 – 7861Phosphothreonine; by CK2 Reviewed prediction

Post-translational modificationi

Phosphorylated by CK2.1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP41148.
PRIDEiP41148.

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.2 Publications

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000011044.

Structurei

Secondary structure

1
804
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni72 – 743
Helixi80 – 9213
Turni93 – 953
Helixi99 – 12123
Turni123 – 1286
Beta strandi134 – 1396
Turni140 – 1434
Beta strandi144 – 1496
Helixi156 – 1649
Helixi169 – 18416
Helixi189 – 1946
Helixi198 – 2047
Beta strandi206 – 2149
Beta strandi216 – 2183
Beta strandi221 – 2288
Beta strandi230 – 2345
Beta strandi241 – 25111
Helixi253 – 2597
Helixi261 – 27212
Beta strandi279 – 2846
Beta strandi331 – 3355
Turni342 – 3443
Turni347 – 3493
Helixi352 – 36110
Beta strandi370 – 3778
Beta strandi379 – 3813
Beta strandi383 – 3897
Beta strandi409 – 4135
Beta strandi416 – 4205
Helixi428 – 4303
Beta strandi434 – 4429
Beta strandi444 – 4463
Helixi448 – 4525
Helixi455 – 47420
Helixi477 – 4826
Helixi484 – 49815
Helixi500 – 5023
Helixi503 – 5075
Beta strandi512 – 5143
Beta strandi517 – 5193
Helixi524 – 5307
Beta strandi537 – 5426
Helixi546 – 5505
Helixi553 – 5553
Helixi556 – 5605
Beta strandi566 – 5683
Helixi572 – 5787
Beta strandi586 – 5905
Helixi602 – 61413
Helixi616 – 6249
Turni625 – 6306
Beta strandi631 – 6366
Beta strandi644 – 6496
Helixi656 – 66813
Beta strandi677 – 6804
Beta strandi683 – 6875
Helixi692 – 70312
Helixi708 – 72518
Helixi732 – 74413
Turni751 – 7577
Helixi758 – 7603
Helixi762 – 7643

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP41148.
SMRiP41148. Positions 69-755.

Miscellaneous databases

EvolutionaryTraceiP41148.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi801 – 8044Prevents secretion from ER Reviewed prediction

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0326.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiP41148.
KOiK09487.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90.
InterProiIPR003594. HATPase_ATP-bd.
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. 2 hits.
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.

P41148-1 [UniParc]FASTAAdd to Basket

« Hide

MRALWVLGLC CVLLTFGSVR ADDEVDVDGT VEEDLGKSRE GSRTDDEVVQ    50
REEEAIQLDG LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF 100
LRELISNASD ALDKIRLISL TDENALAGNE ELTVKIKCDK EKNLLHVTDT 150
GVGMTREELV KNLGTIAKSG TSEFLNKMTE AQEDGQSTSE LIGQFGVGFY 200
SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT LGRGTTITLV 250
LKEEASDYLE LDTIKNLVKK YSQFINFPIY VWSSKTETVE EPMEEEEAAK 300
EEKEDSDDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV 350
EDDEYKAFYK SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE 400
YGSKKSDYIK LYVRRVFITD DFHDMMPKYL NFVKGVVDSD DLPLNVSRET 450
LQQHKLLKVI RKKLVRKTLD MIKKIADEKY NDTFWKEFGT NIKLGVIEDH 500
SNRTRLAKLL RFQSSHHPSD ITSLDQYVER MKEKQDKIYF MAGSSRKEAE 550
SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE 600
SEKTKESREA IEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS 650
QYGWSGNMER IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIKDMLRR 700
VKEDEDDKTV SDLAVVLFET ATLRSGYLLP DTKAYGDRIE RMLRLSLNID 750
PDAKVEEEPE EEPEETTEDT TEDTEQDDEE EMDAGTDDEE QETVKKSTAE 800
KDEL 804
Length:804
Mass (Da):92,514
Last modified:February 1, 1995 - v1
Checksum:i36AA126EDCFFC2D5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U01153 mRNA. Translation: AAA17708.1.
PIRiA53211.
RefSeqiNP_001003327.1. NM_001003327.1.
UniGeneiCfa.3896.

Genome annotation databases

GeneIDi404019.
KEGGicfa:404019.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U01153 mRNA. Translation: AAA17708.1 .
PIRi A53211.
RefSeqi NP_001003327.1. NM_001003327.1.
UniGenei Cfa.3896.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QY5 X-ray 1.75 A 69-337 [» ]
1QY8 X-ray 1.85 A 69-337 [» ]
1QYE X-ray 2.10 A 69-337 [» ]
1TBW X-ray 2.15 A/B 69-337 [» ]
1TC0 X-ray 2.20 A/B 69-337 [» ]
1TC6 X-ray 1.87 A/B 69-337 [» ]
1U0Y X-ray 2.30 A 69-337 [» ]
1U0Z X-ray 1.90 A/B 69-337 [» ]
1U2O X-ray 2.10 A/B 69-337 [» ]
1YSZ X-ray 2.65 A 69-337 [» ]
1YT0 X-ray 2.40 A 69-337 [» ]
1YT1 X-ray 2.20 A/B 69-337 [» ]
1YT2 X-ray 3.25 A 69-337 [» ]
2ESA X-ray 1.90 A 69-337 [» ]
2EXL X-ray 2.35 A/B 69-337 [» ]
2FYP X-ray 1.95 A/B 69-337 [» ]
2GFD X-ray 2.30 A/B 69-337 [» ]
2GQP X-ray 1.50 A/B 69-337 [» ]
2H8M X-ray 1.80 A/B 69-337 [» ]
2HCH X-ray 2.30 A/B 69-337 [» ]
2HG1 X-ray 2.30 A/B 69-286 [» ]
2O1T X-ray 3.20 A/B/C/D/E/F/G/H/I/J 336-765 [» ]
2O1U X-ray 2.40 A/B 73-754 [» ]
2O1V X-ray 2.45 A/B 73-754 [» ]
2O1W X-ray 3.40 A/B/C/D/E 73-594 [» ]
3O2F X-ray 2.00 A/B 69-337 [» ]
ProteinModelPortali P41148.
SMRi P41148. Positions 69-755.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9615.ENSCAFP00000011044.

Chemistry

BindingDBi P41148.
ChEMBLi CHEMBL4748.
DrugBanki DB00131. Adenosine monophosphate.

Proteomic databases

PaxDbi P41148.
PRIDEi P41148.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 404019.
KEGGi cfa:404019.

Organism-specific databases

CTDi 7184.

Phylogenomic databases

eggNOGi COG0326.
HOGENOMi HOG000031988.
HOVERGENi HBG007374.
InParanoidi P41148.
KOi K09487.

Enzyme and pathway databases

Reactomei REACT_203393. ATF6-alpha activates chaperone genes.
REACT_214911. Scavenging by Class A Receptors.
REACT_218639. Trafficking and processing of endosomal TLR.

Miscellaneous databases

EvolutionaryTracei P41148.
NextBioi 20817506.
PROi P41148.

Family and domain databases

Gene3Di 3.30.565.10. 2 hits.
HAMAPi MF_00505. HSP90.
InterProi IPR003594. HATPase_ATP-bd.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view ]
PANTHERi PTHR11528. PTHR11528. 1 hit.
Pfami PF00183. HSP90. 1 hit.
[Graphical view ]
PIRSFi PIRSF002583. Hsp90. 1 hit.
PRINTSi PR00775. HEATSHOCK90.
SMARTi SM00387. HATPase_c. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 2 hits.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00298. HSP90. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiENPL_CANFA
AccessioniPrimary (citable) accession number: P41148
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 3, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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