Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P41148

- ENPL_CANFA

UniProt

P41148 - ENPL_CANFA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Endoplasmin

Gene

HSP90B1

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).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
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: Ensembl
  3. endoplasmic reticulum membrane Source: Ensembl
  4. extracellular vesicular exosome Source: Ensembl
  5. midbody Source: Ensembl
  6. nucleus Source: Ensembl
  7. perinuclear region of cytoplasm Source: Ensembl
  8. plasma membrane Source: Ensembl
  9. sarcoplasmic reticulum Source: UniProtKB-KW
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 – 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 – 743Combined sources
Helixi80 – 9213Combined sources
Turni93 – 953Combined sources
Helixi99 – 12123Combined sources
Turni123 – 1286Combined sources
Beta strandi134 – 1396Combined sources
Turni140 – 1434Combined sources
Beta strandi144 – 1496Combined sources
Helixi156 – 1649Combined sources
Helixi169 – 18416Combined sources
Helixi189 – 1946Combined sources
Helixi198 – 2047Combined sources
Beta strandi206 – 2149Combined sources
Beta strandi216 – 2183Combined sources
Beta strandi221 – 2288Combined sources
Beta strandi230 – 2345Combined sources
Beta strandi241 – 25111Combined sources
Helixi253 – 2597Combined sources
Helixi261 – 27212Combined sources
Beta strandi279 – 2846Combined sources
Beta strandi331 – 3355Combined sources
Turni342 – 3443Combined sources
Turni347 – 3493Combined sources
Helixi352 – 36110Combined sources
Beta strandi370 – 3778Combined sources
Beta strandi379 – 3813Combined sources
Beta strandi383 – 3897Combined sources
Beta strandi409 – 4135Combined sources
Beta strandi416 – 4205Combined sources
Helixi428 – 4303Combined sources
Beta strandi434 – 4429Combined sources
Beta strandi444 – 4463Combined sources
Helixi448 – 4525Combined sources
Helixi455 – 47420Combined sources
Helixi477 – 4826Combined sources
Helixi484 – 49815Combined sources
Helixi500 – 5023Combined sources
Helixi503 – 5075Combined sources
Beta strandi512 – 5143Combined sources
Beta strandi517 – 5193Combined sources
Helixi524 – 5307Combined sources
Beta strandi537 – 5426Combined sources
Helixi546 – 5505Combined sources
Helixi553 – 5553Combined sources
Helixi556 – 5605Combined sources
Beta strandi566 – 5683Combined sources
Helixi572 – 5787Combined sources
Beta strandi586 – 5905Combined sources
Helixi602 – 61413Combined sources
Helixi616 – 6249Combined sources
Turni625 – 6306Combined sources
Beta strandi631 – 6366Combined sources
Beta strandi644 – 6496Combined sources
Helixi656 – 66813Combined sources
Beta strandi677 – 6804Combined sources
Beta strandi683 – 6875Combined sources
Helixi692 – 70312Combined sources
Helixi708 – 72518Combined sources
Helixi732 – 74413Combined sources
Turni751 – 7577Combined sources
Helixi758 – 7603Combined sources
Helixi762 – 7643Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QY5X-ray1.75A69-337[»]
1QY8X-ray1.85A69-337[»]
1QYEX-ray2.10A69-337[»]
1TBWX-ray2.15A/B69-286[»]
A/B328-337[»]
1TC0X-ray2.20A/B69-286[»]
A/B328-337[»]
1TC6X-ray1.87A/B69-286[»]
A/B328-337[»]
1U0YX-ray2.30A69-337[»]
1U0ZX-ray1.90A/B69-286[»]
A/B328-337[»]
1U2OX-ray2.10A/B69-286[»]
A/B328-337[»]
1YSZX-ray2.65A69-286[»]
A328-337[»]
1YT0X-ray2.40A69-286[»]
A328-337[»]
1YT1X-ray2.20A/B69-286[»]
A/B328-337[»]
1YT2X-ray3.25A69-337[»]
2ESAX-ray1.90A69-286[»]
A328-337[»]
2EXLX-ray2.35A/B69-286[»]
A/B328-337[»]
2FYPX-ray1.95A/B69-286[»]
A/B328-337[»]
2GFDX-ray2.30A/B69-286[»]
A/B328-337[»]
2GQPX-ray1.50A/B69-286[»]
A/B328-337[»]
2H8MX-ray1.80A/B69-286[»]
A/B328-337[»]
2HCHX-ray2.30A/B69-286[»]
A/B328-337[»]
2HG1X-ray2.30A/B69-286[»]
2O1TX-ray3.20A/B/C/D/E/F/G/H/I/J336-765[»]
2O1UX-ray2.40A/B73-286[»]
A/B328-754[»]
2O1VX-ray2.45A/B73-286[»]
A/B328-754[»]
2O1WX-ray3.40A/B/C/D/E73-286[»]
A/B/C/D/E328-594[»]
3O2FX-ray2.00A/B69-286[»]
A/B328-337[»]
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_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. 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

        10         20         30         40         50
MRALWVLGLC CVLLTFGSVR ADDEVDVDGT 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 TSEFLNKMTE 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
EEKEDSDDEA 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
SEKTKESREA IEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS
660 670 680 690 700
QYGWSGNMER IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIKDMLRR
710 720 730 740 750
VKEDEDDKTV SDLAVVLFET ATLRSGYLLP DTKAYGDRIE RMLRLSLNID
760 770 780 790 800
PDAKVEEEPE EEPEETTEDT TEDTEQDDEE EMDAGTDDEE QETVKKSTAE

KDEL
Length:804
Mass (Da):92,514
Last modified:February 1, 1995 - v1
Checksum:i36AA126EDCFFC2D5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 69-286 [» ]
A/B 328-337 [» ]
1TC0 X-ray 2.20 A/B 69-286 [» ]
A/B 328-337 [» ]
1TC6 X-ray 1.87 A/B 69-286 [» ]
A/B 328-337 [» ]
1U0Y X-ray 2.30 A 69-337 [» ]
1U0Z X-ray 1.90 A/B 69-286 [» ]
A/B 328-337 [» ]
1U2O X-ray 2.10 A/B 69-286 [» ]
A/B 328-337 [» ]
1YSZ X-ray 2.65 A 69-286 [» ]
A 328-337 [» ]
1YT0 X-ray 2.40 A 69-286 [» ]
A 328-337 [» ]
1YT1 X-ray 2.20 A/B 69-286 [» ]
A/B 328-337 [» ]
1YT2 X-ray 3.25 A 69-337 [» ]
2ESA X-ray 1.90 A 69-286 [» ]
A 328-337 [» ]
2EXL X-ray 2.35 A/B 69-286 [» ]
A/B 328-337 [» ]
2FYP X-ray 1.95 A/B 69-286 [» ]
A/B 328-337 [» ]
2GFD X-ray 2.30 A/B 69-286 [» ]
A/B 328-337 [» ]
2GQP X-ray 1.50 A/B 69-286 [» ]
A/B 328-337 [» ]
2H8M X-ray 1.80 A/B 69-286 [» ]
A/B 328-337 [» ]
2HCH X-ray 2.30 A/B 69-286 [» ]
A/B 328-337 [» ]
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 73-286 [» ]
A/B 328-754 [» ]
2O1V X-ray 2.45 A/B 73-286 [» ]
A/B 328-754 [» ]
2O1W X-ray 3.40 A/B/C/D/E 73-286 [» ]
A/B/C/D/E 328-594 [» ]
3O2F X-ray 2.00 A/B 69-286 [» ]
A/B 328-337 [» ]
ProteinModelPortali P41148.
SMRi P41148. Positions 69-755.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9615.ENSCAFP00000011044.

Chemistry

BindingDBi P41148.
ChEMBLi CHEMBL4748.

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_C.
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: November 26, 2014
This is version 132 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