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Endoplasmin homolog (Glucose-regulated protein 94 homolog) (GRP-94 homolog) (Heat shock protein 90-7) (AtHSP90.7) (AtHsp90-7) (Protein SHEPHERD)

 ENPL_ARATH              Reviewed;         823 AA.
Q9STX5; O22972; Q56Y38; Q8VY71;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
20-DEC-2017, entry version 130.
RecName: Full=Endoplasmin homolog {ECO:0000305};
AltName: Full=Glucose-regulated protein 94 homolog {ECO:0000303|PubMed:11867518};
Short=GRP-94 homolog {ECO:0000303|PubMed:11867518};
AltName: Full=Heat shock protein 90-7 {ECO:0000305};
Short=AtHSP90.7 {ECO:0000305};
Short=AtHsp90-7 {ECO:0000303|PubMed:11599565};
AltName: Full=Protein SHEPHERD {ECO:0000303|PubMed:11867518};
Flags: Precursor;
Name=HSP90-7 {ECO:0000303|PubMed:11599565};
Synonyms=SHD {ECO:0000303|PubMed:11867518};
OrderedLocusNames=At4g24190; ORFNames=T19F6.1, T22A6.20;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
INDUCTION.
STRAIN=cv. Columbia;
PubMed=11867518; DOI=10.1093/emboj/21.5.898;
Ishiguro S., Watanabe Y., Ito N., Nonaka H., Takeda N., Sakai T.,
Kanaya H., Okada K.;
"SHEPHERD is the Arabidopsis GRP94 responsible for the formation of
functional CLAVATA proteins.";
EMBO J. 21:898-908(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-238.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11599565; DOI=10.1379/1466-1268(2001)006<0238:THFOPI>2.0.CO;2;
Krishna P., Gloor G.;
"The Hsp90 family of proteins in Arabidopsis thaliana.";
Cell Stress Chaperones 6:238-246(2001).
[7]
INTERACTION WITH FKBP42.
PubMed=12410806; DOI=10.1046/j.1365-313X.2002.01420.x;
Kamphausen T., Fanghaenel J., Neumann D., Schulz B., Rahfeld J.-U.;
"Characterization of Arabidopsis thaliana AtFKBP42 that is membrane-
bound and interacts with Hsp90.";
Plant J. 32:263-276(2002).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
[9]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=25297550; DOI=10.1093/jxb/eru403;
Chong L.P., Wang Y., Gad N., Anderson N., Shah B., Zhao R.;
"A highly charged region in the middle domain of plant endoplasmic
reticulum (ER)-localized heat-shock protein 90 is required for
resistance to tunicamycin or high calcium-induced ER stresses.";
J. Exp. Bot. 66:113-124(2015).
-!- FUNCTION: May have a molecular chaperone role in the processing of
secreted materials. Required for shoot apical meristem (SAM), root
apical meristem (RAM) and floral meristem (FM) formation, probably
by regulating the folding of CLAVATA proteins (CLVs). Also
involved in pollen tube elongation (PubMed:11867518). Involved in
resistance to tunicamycin- or high calcium-induced ER stresses.
Possesses ATPase activity (PubMed:25297550).
{ECO:0000269|PubMed:11867518, ECO:0000269|PubMed:25297550}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.77 mM for ATP {ECO:0000269|PubMed:25297550};
-!- SUBUNIT: Interacts with FKBP42. {ECO:0000269|PubMed:12410806}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=Q9STX5-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11867518}.
-!- INDUCTION: Seems inhibited by heat shock.
{ECO:0000269|PubMed:11867518}.
-!- SIMILARITY: Belongs to the heat shock protein 90 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB63606.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB064528; BAB86369.1; -; mRNA.
EMBL; AC002343; AAB63606.1; ALT_SEQ; Genomic_DNA.
EMBL; AL078637; CAB45054.1; -; Genomic_DNA.
EMBL; AL161561; CAB79329.1; -; Genomic_DNA.
EMBL; CP002687; AEE84861.1; -; Genomic_DNA.
EMBL; AY039895; AAK63999.1; -; mRNA.
EMBL; AY072394; AAL62386.1; -; mRNA.
EMBL; BT004527; AAO42773.1; -; mRNA.
EMBL; AK221485; BAD94659.1; -; mRNA.
PIR; T09882; T09882.
RefSeq; NP_194150.1; NM_118552.4. [Q9STX5-1]
UniGene; At.24111; -.
ProteinModelPortal; Q9STX5; -.
SMR; Q9STX5; -.
BioGrid; 13809; 16.
IntAct; Q9STX5; 9.
STRING; 3702.AT4G24190.1; -.
iPTMnet; Q9STX5; -.
PaxDb; Q9STX5; -.
PRIDE; Q9STX5; -.
EnsemblPlants; AT4G24190.1; AT4G24190.1; AT4G24190. [Q9STX5-1]
GeneID; 828520; -.
Gramene; AT4G24190.1; AT4G24190.1; AT4G24190. [Q9STX5-1]
KEGG; ath:AT4G24190; -.
Araport; AT4G24190; -.
TAIR; locus:2135887; AT4G24190.
eggNOG; KOG0020; Eukaryota.
eggNOG; COG0326; LUCA.
HOGENOM; HOG000031988; -.
InParanoid; Q9STX5; -.
KO; K09487; -.
OMA; SDHEIFL; -.
PhylomeDB; Q9STX5; -.
PRO; PR:Q9STX5; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9STX5; baseline and differential.
Genevisible; Q9STX5; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0009306; P:protein secretion; IDA:TAIR.
GO; GO:0010075; P:regulation of meristem growth; IMP:TAIR.
GO; GO:0009934; P:regulation of meristem structural organization; IMP:TAIR.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009409; P:response to cold; IEP:TAIR.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:UniProtKB.
GO; GO:0009651; P:response to salt stress; IMP:TAIR.
GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
CDD; cd00075; HATPase_c; 1.
Gene3D; 3.30.565.10; -; 2.
HAMAP; MF_00505; HSP90; 1.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR019805; Heat_shock_protein_90_CS.
InterPro; IPR037196; HSP90_C.
InterPro; IPR001404; Hsp90_fam.
InterPro; IPR020575; Hsp90_N.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
PANTHER; PTHR11528; PTHR11528; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00183; HSP90; 1.
PIRSF; PIRSF002583; Hsp90; 1.
PRINTS; PR00775; HEATSHOCK90.
SMART; SM00387; HATPase_c; 1.
SUPFAM; SSF110942; SSF110942; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55874; SSF55874; 1.
PROSITE; PS00014; ER_TARGET; 1.
PROSITE; PS00298; HSP90; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Calcium; Chaperone;
Complete proteome; Endoplasmic reticulum; Glycoprotein;
Nucleotide-binding; Reference proteome; Signal; Stress response.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 823 Endoplasmin homolog.
/FTId=PRO_0000226071.
NP_BIND 174 175 ATP. {ECO:0000250|UniProtKB:P02829}.
NP_BIND 194 199 ATP. {ECO:0000250|UniProtKB:P02829}.
MOTIF 820 823 Prevents secretion from ER.
{ECO:0000250}.
BINDING 106 106 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 110 110 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 154 154 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 159 159 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 167 167 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 173 173 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 246 246 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 455 455 ATP. {ECO:0000250|UniProtKB:P02829}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 452 452 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 620 620 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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


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