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Q9STX5

- ENPL_ARATH

UniProt

Q9STX5 - ENPL_ARATH

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Protein

Endoplasmin homolog

Gene

SHD

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei110 – 1101ATPBy similarity
Binding sitei154 – 1541ATPBy similarity
Binding sitei167 – 1671ATPBy similarity
Binding sitei173 – 1731ATPBy similarity
Binding sitei199 – 1991ATP; via amide nitrogenBy similarity
Binding sitei455 – 4551ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. protein folding Source: InterPro
  2. protein secretion Source: TAIR
  3. regulation of meristem growth Source: TAIR
  4. regulation of meristem structural organization Source: TAIR
  5. response to cadmium ion Source: TAIR
  6. response to cold Source: TAIR
  7. response to salt stress Source: TAIR
  8. response to water deprivation Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Calcium, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_108190. ATF6-alpha activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoplasmin homolog
Alternative name(s):
Glucose-regulated protein 94 homolog
Short name:
GRP-94 homolog
HSP90-like protein 7
Protein SHEPHERD
Gene namesi
Name:SHD
Synonyms:HSP90-7
Ordered Locus Names:At4g24190
ORF Names:T19F6.1,T22A6.20
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G24190.

Subcellular locationi

GO - Cellular componenti

  1. apoplast Source: TAIR
  2. chloroplast Source: TAIR
  3. endoplasmic reticulum Source: TAIR
  4. membrane Source: TAIR
  5. mitochondrion Source: TAIR
  6. nucleus Source: TAIR
  7. plasma membrane Source: TAIR
  8. plasmodesma Source: TAIR
  9. vacuolar membrane Source: TAIR
  10. 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.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Inductioni

Seems inhibited by heat shock.1 Publication

Gene expression databases

ExpressionAtlasiQ9STX5. baseline and differential.
GenevestigatoriQ9STX5.

Interactioni

Subunit structurei

Interacts with FKBP42.1 Publication

Protein-protein interaction databases

BioGridi13809. 1 interaction.
IntActiQ9STX5. 9 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9STX5.
SMRiQ9STX5. Positions 75-776.
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

eggNOGiCOG0326.
HOGENOMiHOG000031988.
InParanoidiQ9STX5.
KOiK09487.
OMAiQSSHHPS.
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. 1 hit.
PfamiPF00183. 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. Align

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 .
PIRi T09882.
RefSeqi NP_194150.1. NM_118552.3. [Q9STX5-1 ]
UniGenei At.24111.

3D structure databases

ProteinModelPortali Q9STX5.
SMRi Q9STX5. Positions 75-776.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 13809. 1 interaction.
IntActi Q9STX5. 9 interactions.

Proteomic databases

PaxDbi Q9STX5.
PRIDEi Q9STX5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G24190.1 ; AT4G24190.1 ; AT4G24190 . [Q9STX5-1 ]
GeneIDi 828520.
KEGGi ath:AT4G24190.

Organism-specific databases

TAIRi AT4G24190.

Phylogenomic databases

eggNOGi COG0326.
HOGENOMi HOG000031988.
InParanoidi Q9STX5.
KOi K09487.
OMAi QSSHHPS.
PhylomeDBi Q9STX5.

Enzyme and pathway databases

Reactomei REACT_108190. ATF6-alpha activates chaperone genes.

Miscellaneous databases

PROi Q9STX5.

Gene expression databases

ExpressionAtlasi Q9STX5. baseline and differential.
Genevestigatori Q9STX5.

Family and domain databases

Gene3Di 3.30.565.10. 1 hit.
HAMAPi MF_00505. HSP90.
InterProi IPR003594. HATPase_C.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view ]
PANTHERi PTHR11528. PTHR11528. 1 hit.
Pfami PF00183. HSP90. 1 hit.
[Graphical view ]
PIRSFi PIRSF002583. Hsp90. 1 hit.
PRINTSi PR00775. HEATSHOCK90.
SMARTi SM00387. HATPase_c. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00298. HSP90. 1 hit.
[Graphical view ]
ProtoNeti Search...

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.

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: October 29, 2014
This is version 107 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

External Data

Dasty 3