ENPL_HORVU
ID ENPL_HORVU Reviewed; 809 AA.
AC P36183;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Endoplasmin homolog;
DE AltName: Full=Glucose-regulated protein 94 homolog;
DE Short=GRP-94 homolog;
DE Flags: Precursor;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Pallas / P-01; TISSUE=Leaf;
RX PubMed=8490130; DOI=10.1007/bf00023606;
RA Walther-Larsen H., Brandt J., Collinge D.B., Thordal-Christensen H.;
RT "A pathogen-induced gene of barley encodes a HSP90 homologue showing
RT striking similarity to vertebrate forms resident in the endoplasmic
RT reticulum.";
RL Plant Mol. Biol. 21:1097-1108(1993).
CC -!- FUNCTION: May have a molecular chaperone role in the processing of
CC secreted materials. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC -!- INDUCTION: Accumulates rapidly in leaves upon heat shock treatment and
CC during infection by a pathogen.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; X67960; CAA48143.1; -; mRNA.
DR PIR; S33533; S33533.
DR AlphaFoldDB; P36183; -.
DR SMR; P36183; -.
DR DIP; DIP-737N; -.
DR PRIDE; P36183; -.
DR EnsemblPlants; HORVU.MOREX.r2.7HG0619420.1; HORVU.MOREX.r2.7HG0619420.1; HORVU.MOREX.r2.7HG0619420.
DR EnsemblPlants; HORVU.MOREX.r2.7HG0619420.1.mrna1; HORVU.MOREX.r2.7HG0619420.1.mrna1; HORVU.MOREX.r2.7HG0619420.1.
DR Gramene; HORVU.MOREX.r2.7HG0619420.1; HORVU.MOREX.r2.7HG0619420.1; HORVU.MOREX.r2.7HG0619420.
DR Gramene; HORVU.MOREX.r2.7HG0619420.1.mrna1; HORVU.MOREX.r2.7HG0619420.1.mrna1; HORVU.MOREX.r2.7HG0619420.1.
DR ExpressionAtlas; P36183; baseline and differential.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblPlants.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0009306; P:protein secretion; IEA:EnsemblPlants.
DR GO; GO:0010075; P:regulation of meristem growth; IEA:EnsemblPlants.
DR GO; GO:0009934; P:regulation of meristem structural organization; IEA:EnsemblPlants.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:EnsemblPlants.
DR GO; GO:0009651; P:response to salt stress; IEA:EnsemblPlants.
DR GO; GO:0009414; P:response to water deprivation; IEA:EnsemblPlants.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Calcium; Chaperone; Endoplasmic reticulum; Glycoprotein;
KW Nucleotide-binding; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..809
FT /note="Endoplasmin homolog"
FT /id="PRO_0000013603"
FT REGION 293..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 806..809
FT /note="Prevents secretion from ER"
FT COMPBIAS 293..319
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT SITE 453
FT /note="Important for ATP hydrolysis"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 809 AA; 92917 MW; 79798FDBC15B44D0 CRC64;
MRKWALSCAL LLVLLLTTLP DPAKKLQVNA EESSDEVGDF PKVEEKLGAV PHGLSTDSEV
VQRESESISR KTLRNSAEKF EFQAEVSRLM DIIINSLYSN KDIFLRELIS NASDALDKIR
FLALTDKEVM GEGDTAKLEI QIKLDKENKI LSIRDRGVGM TKEDLIKNLG TIAKSGTSAF
VEKMQTGGDL NLIGQFGVGF YSVYLVADYV EVVSKHNDDK QYVWESKADG SFAISEDTWN
EPLGRGTEIK LHLRDEAKEY LEEGKLKDLV KKYSEFINFP IYLWATKEVD VEVPADEEES
NEEEESTTET TEEEETEDDE EKKPKTKTVK ETTTEWELLN DMKAVWLRSP KEVTEEEYAK
FYHSLAKDFG DDKPMSWSHF SAEGDVEFKA LLFVPPKAPH DLYESYYNAN KSNLKLYVRR
VFISDEFDDL LPKYLSFLMG IVDSDTLPLN VSREMLQQHS SLKTIKKKLI RKALDMIRKL
AEEDPDEYSN KEKTDDEKSA MEEKKGQYAK FWNEFGKSVK LGIIEDATNR NRLAKLLRFE
SSKSDGKLVS LDEYISRMKS GQKDIFYLTG SSKEQLEKSP FLEQLTKKNY EVIYFTDPVD
EYLMQYLMDY EDKKFQNVSK EGLKLGKDSK LKDLKESFKE LTDWWKKALD TEGIDSVKIS
NRLHNTPCVV VTSKYGWSSN MEKIMQAQTL SDASKQAYMR GKRVLEINPR HPIIKELRDK
VAQDSDSEGL KQTARLVYQT ALMESGFNLP DPKDFASSIY RSVQKSLDLS PDAAVEEEEE
VEEPEVEEKE SAKQEAEEPE HEQYDKDEL
