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P41148

- ENPL_CANFA

UniProt

P41148 - ENPL_CANFA

Protein

Endoplasmin

Gene

HSP90B1

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    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

    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 – 1681ATPBy similarity
    Binding sitei199 – 1991ATP; via amide nitrogen
    Binding sitei448 – 4481ATPBy 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

    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

    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 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 804783EndoplasminPRO_0000013597Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi138 – 138InterchainBy similarity
    Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence Analysis
    Modified residuei288 – 2881Phosphothreonine; by CK2Sequence Analysis
    Modified residuei306 – 3061Phosphoserine; by CK2Sequence Analysis
    Modified residuei404 – 4041N6-succinyllysineBy similarity
    Glycosylationi445 – 4451N-linked (GlcNAc...)Sequence Analysis
    Modified residuei479 – 4791N6-acetyllysineBy similarity
    Glycosylationi481 – 4811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi502 – 5021N-linked (GlcNAc...)Sequence Analysis
    Modified residuei633 – 6331N6-succinyllysineBy similarity
    Modified residuei766 – 7661Phosphothreonine; by CK2Sequence Analysis
    Modified residuei770 – 7701Phosphothreonine; by CK2Sequence Analysis
    Modified residuei774 – 7741Phosphothreonine; by CK2Sequence Analysis
    Modified residuei786 – 7861Phosphothreonine; by CK2Sequence Analysis

    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.By similarity

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP41148.

    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.
    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: October 1, 2014
    This is version 130 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