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Database: UniProt
Entry: P36183
LinkDB: P36183
Original site: P36183 
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   29-OCT-2014, entry version 96.
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; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Pooideae; Triticeae; 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
CC       and during infection by a pathogen.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000305}.
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DR   EMBL; X67960; CAA48143.1; -; mRNA.
DR   PIR; S33533; S33533.
DR   UniGene; Hv.26181; -.
DR   ProteinModelPortal; P36183; -.
DR   SMR; P36183; 77-287.
DR   DIP; DIP-737N; -.
DR   PRIDE; P36183; -.
DR   Gramene; P36183; -.
DR   Genevestigator; P36183; -.
DR   GO; GO:0048046; C:apoplast; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0005739; C:mitochondrion; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0009506; C:plasmodesma; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0006096; P:glycolytic process; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0007030; P:Golgi organization; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0006972; P:hyperosmotic response; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0006499; P:N-terminal protein myristoylation; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0006457; P:protein folding; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0009306; P:protein secretion; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0010075; P:regulation of meristem growth; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0009934; P:regulation of meristem structural organization; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0009408; P:response to heat; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0009644; P:response to high light intensity; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0009651; P:response to salt stress; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0009414; P:response to water deprivation; IEA:EnsemblPlants/Gramene.
DR   GO; GO:0006833; P:water transport; IEA:EnsemblPlants/Gramene.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
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; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 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       {ECO:0000255}.
FT   CHAIN        19    809       Endoplasmin homolog.
FT                                /FTId=PRO_0000013603.
FT   MOTIF       806    809       Prevents secretion from ER.
FT   BINDING     111    111       ATP. {ECO:0000250}.
FT   BINDING     155    155       ATP. {ECO:0000250}.
FT   BINDING     168    168       ATP. {ECO:0000250}.
FT   BINDING     174    174       ATP. {ECO:0000250}.
FT   BINDING     200    200       ATP; via amide nitrogen. {ECO:0000250}.
FT   BINDING     453    453       ATP. {ECO:0000250}.
FT   CARBOHYD    111    111       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    410    410       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    450    450       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    617    617       N-linked (GlcNAc...). {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
//
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