ENPL_ARATH
ID ENPL_ARATH Reviewed; 823 AA.
AC Q9STX5; O22972; Q56Y38; Q8VY71;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Endoplasmin homolog {ECO:0000305};
DE AltName: Full=Glucose-regulated protein 94 homolog {ECO:0000303|PubMed:11867518};
DE Short=GRP-94 homolog {ECO:0000303|PubMed:11867518};
DE AltName: Full=Heat shock protein 90-7 {ECO:0000305};
DE Short=AtHSP90.7 {ECO:0000305};
DE Short=AtHsp90-7 {ECO:0000303|PubMed:11599565};
DE AltName: Full=Protein SHEPHERD {ECO:0000303|PubMed:11867518};
DE Flags: Precursor;
GN Name=HSP90-7 {ECO:0000303|PubMed:11599565};
GN Synonyms=SHD {ECO:0000303|PubMed:11867518}; OrderedLocusNames=At4g24190;
GN ORFNames=T19F6.1, T22A6.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11867518; DOI=10.1093/emboj/21.5.898;
RA Ishiguro S., Watanabe Y., Ito N., Nonaka H., Takeda N., Sakai T.,
RA Kanaya H., Okada K.;
RT "SHEPHERD is the Arabidopsis GRP94 responsible for the formation of
RT functional CLAVATA proteins.";
RL EMBO J. 21:898-908(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-238.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11599565; DOI=10.1379/1466-1268(2001)006<0238:thfopi>2.0.co;2;
RA Krishna P., Gloor G.;
RT "The Hsp90 family of proteins in Arabidopsis thaliana.";
RL Cell Stress Chaperones 6:238-246(2001).
RN [7]
RP INTERACTION WITH FKBP42.
RX PubMed=12410806; DOI=10.1046/j.1365-313x.2002.01420.x;
RA Kamphausen T., Fanghaenel J., Neumann D., Schulz B., Rahfeld J.-U.;
RT "Characterization of Arabidopsis thaliana AtFKBP42 that is membrane-bound
RT and interacts with Hsp90.";
RL Plant J. 32:263-276(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [9]
RP INTERACTION WITH P23-1.
RX PubMed=20493581; DOI=10.1016/j.jplph.2010.03.016;
RA Song H., Fan P., Shi W., Zhao R., Li Y.;
RT "Expression of five AtHsp90 genes in Saccharomyces cerevisiae reveals
RT functional differences of AtHsp90s under abiotic stresses.";
RL J. Plant Physiol. 167:1172-1178(2010).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25297550; DOI=10.1093/jxb/eru403;
RA Chong L.P., Wang Y., Gad N., Anderson N., Shah B., Zhao R.;
RT "A highly charged region in the middle domain of plant endoplasmic
RT reticulum (ER)-localized heat-shock protein 90 is required for resistance
RT to tunicamycin or high calcium-induced ER stresses.";
RL J. Exp. Bot. 66:113-124(2015).
CC -!- FUNCTION: May have a molecular chaperone role in the processing of
CC secreted materials. Required for shoot apical meristem (SAM), root
CC apical meristem (RAM) and floral meristem (FM) formation, probably by
CC regulating the folding of CLAVATA proteins (CLVs). Also involved in
CC pollen tube elongation (PubMed:11867518). Involved in resistance to
CC tunicamycin- or high calcium-induced ER stresses. Possesses ATPase
CC activity (PubMed:25297550). {ECO:0000269|PubMed:11867518,
CC ECO:0000269|PubMed:25297550}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.77 mM for ATP {ECO:0000269|PubMed:25297550};
CC -!- SUBUNIT: Interacts with FKBP42 (PubMed:12410806). Interacts with P23-1
CC (PubMed:20493581). {ECO:0000269|PubMed:12410806,
CC ECO:0000269|PubMed:20493581}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9STX5-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11867518}.
CC -!- INDUCTION: Seems inhibited by heat shock.
CC {ECO:0000269|PubMed:11867518}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB63606.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB064528; BAB86369.1; -; mRNA.
DR EMBL; AC002343; AAB63606.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL078637; CAB45054.1; -; Genomic_DNA.
DR EMBL; AL161561; CAB79329.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84861.1; -; Genomic_DNA.
DR EMBL; AY039895; AAK63999.1; -; mRNA.
DR EMBL; AY072394; AAL62386.1; -; mRNA.
DR EMBL; BT004527; AAO42773.1; -; mRNA.
DR EMBL; AK221485; BAD94659.1; -; mRNA.
DR PIR; T09882; T09882.
DR RefSeq; NP_194150.1; NM_118552.4. [Q9STX5-1]
DR AlphaFoldDB; Q9STX5; -.
DR SMR; Q9STX5; -.
DR BioGRID; 13809; 59.
DR IntAct; Q9STX5; 9.
DR STRING; 3702.AT4G24190.1; -.
DR iPTMnet; Q9STX5; -.
DR MetOSite; Q9STX5; -.
DR PaxDb; Q9STX5; -.
DR PRIDE; Q9STX5; -.
DR ProteomicsDB; 221897; -. [Q9STX5-1]
DR EnsemblPlants; AT4G24190.1; AT4G24190.1; AT4G24190. [Q9STX5-1]
DR GeneID; 828520; -.
DR Gramene; AT4G24190.1; AT4G24190.1; AT4G24190. [Q9STX5-1]
DR KEGG; ath:AT4G24190; -.
DR Araport; AT4G24190; -.
DR TAIR; locus:2135887; AT4G24190.
DR eggNOG; KOG0020; Eukaryota.
DR HOGENOM; CLU_006684_1_1_1; -.
DR InParanoid; Q9STX5; -.
DR OMA; RVMITDE; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; Q9STX5; -.
DR SABIO-RK; Q9STX5; -.
DR PRO; PR:Q9STX5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9STX5; baseline and differential.
DR Genevisible; Q9STX5; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IDA:TAIR.
DR GO; GO:0010075; P:regulation of meristem growth; IMP:TAIR.
DR GO; GO:0009934; P:regulation of meristem structural organization; IMP:TAIR.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Calcium; Chaperone;
KW Endoplasmic reticulum; Glycoprotein; Nucleotide-binding;
KW Reference proteome; Signal; Stress response.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..823
FT /note="Endoplasmin homolog"
FT /id="PRO_0000226071"
FT REGION 29..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 820..823
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000250"
FT COMPBIAS 291..319
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 174..175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 194..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT BINDING 246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT SITE 455
FT /note="Important for ATP hydrolysis"
FT /evidence="ECO:0000250|UniProtKB:P41148"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 823 AA; 94204 MW; 54C88E182A251990 CRC64;
MRKRTLVSVL FLFSLLFLLP DQGRKLHANA EESSDDVTDP PKVEEKIGGH GGLSTDSDVV
HRESESMSKK TLRSNAEKFE FQAEVSRLMD IIINSLYSNK DIFLRELISN ASDALDKIRF
LALTDKDVLG EGDTAKLEIQ IKLDKAKKIL SIRDRGIGMT KEDLIKNLGT IAKSGTSAFV
EKMQSSGDLN LIGQFGVGFY SAYLVADYIE VISKHNDDSQ YVWESKANGK FAVSEDTWNE
PLGRGTEIRL HLRDEAGEYL EESKLKELVK RYSEFINFPI SLWASKEVET EVPVEEDESA
DEETETTSTE EEKEEDAEEE DGEKKQKTKK VKETVYEWEL LNDVKAIWLR SPKEVTEEEY
TKFYHSLSKD FTDEKPMAWS HFNAEGDVEF KAVLYVPPKA PHDLYESYYN SNKANLKLYV
RRVFISDEFD ELLPKYLSFL KGLVDSDTLP LNVSREMLQQ HSSLKTIKKK LIRKALDMIR
KLAEEDPDEI HDDEKKDVEK SGENDEKKGQ YTKFWNEFGK SVKLGIIEDA ANRNRLAKLL
RFETTKSDGK LTSLDQYIKR MKKSQKDIFY ITGSSKEQLE KSPFLERLIK KGYEVIFFTD
PVDEYLMQYL MDYEDKKFQN VSKEGLKVGK DSKDKELKEA FKELTKWWKG NLASENVDDV
KISNRLADTP CVVVTSKFGW SANMERIMQS QTLSDANKQA YMRGKRVLEI NPRHPIIKEL
KDRIASDPED ESVKETAQLM YQTALIESGF ILTDPKDFAA RIYNSVKSGL NISPDAVADE
EIEAAEEPET SEATETKSDD LAGGLNIEAE PVEQQEENTK DEL
