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Protein

Endoplasmin homolog

Gene

HSP90-7

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).2 Publications

Kineticsi

  1. KM=0.77 mM for ATP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei106 – 1061ATPBy similarity
    Binding sitei110 – 1101ATPBy similarity
    Binding sitei154 – 1541ATPBy similarity
    Binding sitei159 – 1591ATPBy similarity
    Binding sitei167 – 1671ATPBy similarity
    Binding sitei173 – 1731ATPBy similarity
    Binding sitei246 – 2461ATPBy similarity
    Binding sitei455 – 4551ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi174 – 1752ATPBy similarity
    Nucleotide bindingi194 – 1996ATPBy similarity

    GO - Molecular functioni

    GO - Biological processi

    • protein folding Source: InterPro
    • protein secretion Source: TAIR
    • regulation of meristem growth Source: TAIR
    • regulation of meristem structural organization Source: TAIR
    • response to cadmium ion Source: TAIR
    • response to cold Source: TAIR
    • response to salt stress Source: TAIR
    • response to water deprivation Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    ATP-binding, Calcium, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoplasmin homologCurated
    Alternative name(s):
    Glucose-regulated protein 94 homolog1 Publication
    Short name:
    GRP-94 homolog1 Publication
    Heat shock protein 90-7Curated
    Short name:
    AtHSP90.7Curated
    Short name:
    AtHsp90-71 Publication
    Protein SHEPHERD1 Publication
    Gene namesi
    Name:HSP90-71 Publication
    Synonyms:SHD1 Publication
    Ordered Locus Names:At4g24190
    ORF Names:T19F6.1, T22A6.20
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G24190.

    Subcellular locationi

    GO - Cellular componenti

    • apoplast Source: TAIR
    • chloroplast Source: TAIR
    • endoplasmic reticulum Source: TAIR
    • endoplasmic reticulum lumen Source: UniProtKB-SubCell
    • membrane Source: TAIR
    • mitochondrion Source: TAIR
    • nucleus Source: TAIR
    • plasma membrane Source: TAIR
    • plasmodesma Source: TAIR
    • vacuolar membrane Source: TAIR
    • vacuole Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence analysisAdd
    BLAST
    Chaini24 – 823800Endoplasmin homologPRO_0000226071Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi110 – 1101N-linked (GlcNAc...)Sequence analysis
    Glycosylationi452 – 4521N-linked (GlcNAc...)Sequence analysis
    Glycosylationi620 – 6201N-linked (GlcNAc...)Sequence analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ9STX5.
    PRIDEiQ9STX5.

    PTM databases

    iPTMnetiQ9STX5.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Inductioni

    Seems inhibited by heat shock.1 Publication

    Gene expression databases

    ExpressionAtlasiQ9STX5. baseline and differential.
    GenevisibleiQ9STX5. AT.

    Interactioni

    Subunit structurei

    Interacts with FKBP42.1 Publication

    Protein-protein interaction databases

    BioGridi13809. 16 interactions.
    IntActiQ9STX5. 9 interactions.
    STRINGi3702.AT4G24190.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9STX5.
    SMRiQ9STX5. Positions 74-776.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi820 – 8234Prevents secretion from ERBy similarity

    Sequence similaritiesi

    Belongs to the heat shock protein 90 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiKOG0020. Eukaryota.
    COG0326. LUCA.
    HOGENOMiHOG000031988.
    InParanoidiQ9STX5.
    KOiK09487.
    OMAiRKPADVT.
    PhylomeDBiQ9STX5.

    Family and domain databases

    Gene3Di3.30.565.10. 1 hit.
    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. 2 hits.
    PfamiPF02518. HATPase_c. 1 hit.
    PF00183. HSP90. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002583. Hsp90. 1 hit.
    PRINTSiPR00775. HEATSHOCK90.
    SMARTiSM00387. HATPase_c. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 1 hit.
    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.

    This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

    Note: A number of isoforms are produced. According to EST sequences.

    Isoform 1 (identifier: Q9STX5-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MRKRTLVSVL FLFSLLFLLP DQGRKLHANA EESSDDVTDP PKVEEKIGGH
    60 70 80 90 100
    GGLSTDSDVV HRESESMSKK TLRSNAEKFE FQAEVSRLMD IIINSLYSNK
    110 120 130 140 150
    DIFLRELISN ASDALDKIRF LALTDKDVLG EGDTAKLEIQ IKLDKAKKIL
    160 170 180 190 200
    SIRDRGIGMT KEDLIKNLGT IAKSGTSAFV EKMQSSGDLN LIGQFGVGFY
    210 220 230 240 250
    SAYLVADYIE VISKHNDDSQ YVWESKANGK FAVSEDTWNE PLGRGTEIRL
    260 270 280 290 300
    HLRDEAGEYL EESKLKELVK RYSEFINFPI SLWASKEVET EVPVEEDESA
    310 320 330 340 350
    DEETETTSTE EEKEEDAEEE DGEKKQKTKK VKETVYEWEL LNDVKAIWLR
    360 370 380 390 400
    SPKEVTEEEY TKFYHSLSKD FTDEKPMAWS HFNAEGDVEF KAVLYVPPKA
    410 420 430 440 450
    PHDLYESYYN SNKANLKLYV RRVFISDEFD ELLPKYLSFL KGLVDSDTLP
    460 470 480 490 500
    LNVSREMLQQ HSSLKTIKKK LIRKALDMIR KLAEEDPDEI HDDEKKDVEK
    510 520 530 540 550
    SGENDEKKGQ YTKFWNEFGK SVKLGIIEDA ANRNRLAKLL RFETTKSDGK
    560 570 580 590 600
    LTSLDQYIKR MKKSQKDIFY ITGSSKEQLE KSPFLERLIK KGYEVIFFTD
    610 620 630 640 650
    PVDEYLMQYL MDYEDKKFQN VSKEGLKVGK DSKDKELKEA FKELTKWWKG
    660 670 680 690 700
    NLASENVDDV KISNRLADTP CVVVTSKFGW SANMERIMQS QTLSDANKQA
    710 720 730 740 750
    YMRGKRVLEI NPRHPIIKEL KDRIASDPED ESVKETAQLM YQTALIESGF
    760 770 780 790 800
    ILTDPKDFAA RIYNSVKSGL NISPDAVADE EIEAAEEPET SEATETKSDD
    810 820
    LAGGLNIEAE PVEQQEENTK DEL
    Length:823
    Mass (Da):94,204
    Last modified:May 1, 2000 - v1
    Checksum:i54C88E182A251990
    GO

    Sequence cautioni

    The sequence AAB63606.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB064528 mRNA. Translation: BAB86369.1.
    AC002343 Genomic DNA. Translation: AAB63606.1. Sequence problems.
    AL078637 Genomic DNA. Translation: CAB45054.1.
    AL161561 Genomic DNA. Translation: CAB79329.1.
    CP002687 Genomic DNA. Translation: AEE84861.1.
    AY039895 mRNA. Translation: AAK63999.1.
    AY072394 mRNA. Translation: AAL62386.1.
    BT004527 mRNA. Translation: AAO42773.1.
    AK221485 mRNA. Translation: BAD94659.1.
    PIRiT09882.
    RefSeqiNP_194150.1. NM_118552.3. [Q9STX5-1]
    UniGeneiAt.24111.

    Genome annotation databases

    EnsemblPlantsiAT4G24190.1; AT4G24190.1; AT4G24190. [Q9STX5-1]
    GeneIDi828520.
    KEGGiath:AT4G24190.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB064528 mRNA. Translation: BAB86369.1.
    AC002343 Genomic DNA. Translation: AAB63606.1. Sequence problems.
    AL078637 Genomic DNA. Translation: CAB45054.1.
    AL161561 Genomic DNA. Translation: CAB79329.1.
    CP002687 Genomic DNA. Translation: AEE84861.1.
    AY039895 mRNA. Translation: AAK63999.1.
    AY072394 mRNA. Translation: AAL62386.1.
    BT004527 mRNA. Translation: AAO42773.1.
    AK221485 mRNA. Translation: BAD94659.1.
    PIRiT09882.
    RefSeqiNP_194150.1. NM_118552.3. [Q9STX5-1]
    UniGeneiAt.24111.

    3D structure databases

    ProteinModelPortaliQ9STX5.
    SMRiQ9STX5. Positions 74-776.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi13809. 16 interactions.
    IntActiQ9STX5. 9 interactions.
    STRINGi3702.AT4G24190.1.

    PTM databases

    iPTMnetiQ9STX5.

    Proteomic databases

    PaxDbiQ9STX5.
    PRIDEiQ9STX5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G24190.1; AT4G24190.1; AT4G24190. [Q9STX5-1]
    GeneIDi828520.
    KEGGiath:AT4G24190.

    Organism-specific databases

    TAIRiAT4G24190.

    Phylogenomic databases

    eggNOGiKOG0020. Eukaryota.
    COG0326. LUCA.
    HOGENOMiHOG000031988.
    InParanoidiQ9STX5.
    KOiK09487.
    OMAiRKPADVT.
    PhylomeDBiQ9STX5.

    Miscellaneous databases

    PROiQ9STX5.

    Gene expression databases

    ExpressionAtlasiQ9STX5. baseline and differential.
    GenevisibleiQ9STX5. AT.

    Family and domain databases

    Gene3Di3.30.565.10. 1 hit.
    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. 2 hits.
    PfamiPF02518. HATPase_c. 1 hit.
    PF00183. HSP90. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002583. Hsp90. 1 hit.
    PRINTSiPR00775. HEATSHOCK90.
    SMARTiSM00387. HATPase_c. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    SSF55874. SSF55874. 1 hit.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    PS00298. HSP90. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "SHEPHERD is the Arabidopsis GRP94 responsible for the formation of functional CLAVATA proteins."
      Ishiguro S., Watanabe Y., Ito N., Nonaka H., Takeda N., Sakai T., Kanaya H., Okada K.
      EMBO J. 21:898-908(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION.
      Strain: cv. Columbia.
    2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      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.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      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.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      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.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-238.
      Strain: cv. Columbia.
    6. "The Hsp90 family of proteins in Arabidopsis thaliana."
      Krishna P., Gloor G.
      Cell Stress Chaperones 6:238-246(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE.
    7. "Characterization of Arabidopsis thaliana AtFKBP42 that is membrane-bound and interacts with Hsp90."
      Kamphausen T., Fanghaenel J., Neumann D., Schulz B., Rahfeld J.-U.
      Plant J. 32:263-276(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FKBP42.
    8. "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."
      Chong L.P., Wang Y., Gad N., Anderson N., Shah B., Zhao R.
      J. Exp. Bot. 66:113-124(2015) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiENPL_ARATH
    AccessioniPrimary (citable) accession number: Q9STX5
    Secondary accession number(s): O22972, Q56Y38, Q8VY71
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 7, 2006
    Last sequence update: May 1, 2000
    Last modified: January 20, 2016
    This is version 118 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.