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Q9STX5 (ENPL_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoplasmin homolog
Alternative name(s):
Glucose-regulated protein 94 homolog
Short name=GRP-94 homolog
HSP90-like protein 7
Protein SHEPHERD
Gene names
Name:SHD
Synonyms:HSP90-7
Ordered Locus Names:At4g24190
ORF Names:T19F6.1,T22A6.20
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length823 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1

Subunit structure

Interacts with FKBP42. Ref.7

Subcellular location

Endoplasmic reticulum lumen By similarity HAMAP-Rule MF_00505.

Tissue specificity

Ubiquitous. Ref.1

Induction

Seems inhibited by heat shock. Ref.1

Sequence similarities

Belongs to the heat shock protein 90 family.

Sequence caution

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

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   Coding sequence diversityAlternative splicing
   DomainSignal
   LigandATP-binding
Calcium
Nucleotide-binding
   Molecular functionChaperone
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: InterPro

protein secretion

Inferred from direct assay PubMed 17059403. Source: TAIR

regulation of meristem growth

Inferred from mutant phenotype Ref.1. Source: TAIR

regulation of meristem structural organization

Inferred from mutant phenotype Ref.1. Source: TAIR

response to cadmium ion

Inferred from expression pattern PubMed 16502469. Source: TAIR

response to cold

Inferred from expression pattern PubMed 14617066. Source: TAIR

response to salt stress

Inferred from mutant phenotype PubMed 19148673. Source: TAIR

response to water deprivation

Inferred from mutant phenotype PubMed 19148673. Source: TAIR

   Cellular_componentapoplast

Inferred from direct assay PubMed 21798377. Source: TAIR

chloroplast

Inferred from direct assay PubMed 15028209PubMed 18431481. Source: TAIR

endoplasmic reticulum

Inferred from direct assay PubMed 16618929PubMed 17059403PubMed 22923678. Source: TAIR

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from direct assay PubMed 17432890. Source: TAIR

mitochondrion

Inferred from direct assay PubMed 14671022. Source: TAIR

nucleus

Inferred from direct assay PubMed 14617066. Source: TAIR

plasma membrane

Inferred from direct assay PubMed 17644812. Source: TAIR

plasmodesma

Inferred from direct assay PubMed 21533090. Source: TAIR

vacuolar membrane

Inferred from direct assay PubMed 17151019. Source: TAIR

vacuole

Inferred from direct assay PubMed 15539469. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9STX5-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 823800Endoplasmin homolog HAMAP-Rule MF_00505
PRO_0000226071

Regions

Motif820 – 8234Prevents secretion from ER By similarity

Sites

Binding site1101ATP By similarity
Binding site1541ATP By similarity
Binding site1671ATP By similarity
Binding site1731ATP By similarity
Binding site1991ATP; via amide nitrogen By similarity
Binding site4551ATP By similarity

Amino acid modifications

Glycosylation1101N-linked (GlcNAc...) Potential
Glycosylation4521N-linked (GlcNAc...) Potential
Glycosylation6201N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 54C88E182A251990

FASTA82394,204
        10         20         30         40         50         60 
MRKRTLVSVL FLFSLLFLLP DQGRKLHANA EESSDDVTDP PKVEEKIGGH GGLSTDSDVV 

        70         80         90        100        110        120 
HRESESMSKK TLRSNAEKFE FQAEVSRLMD IIINSLYSNK DIFLRELISN ASDALDKIRF 

       130        140        150        160        170        180 
LALTDKDVLG EGDTAKLEIQ IKLDKAKKIL SIRDRGIGMT KEDLIKNLGT IAKSGTSAFV 

       190        200        210        220        230        240 
EKMQSSGDLN LIGQFGVGFY SAYLVADYIE VISKHNDDSQ YVWESKANGK FAVSEDTWNE 

       250        260        270        280        290        300 
PLGRGTEIRL HLRDEAGEYL EESKLKELVK RYSEFINFPI SLWASKEVET EVPVEEDESA 

       310        320        330        340        350        360 
DEETETTSTE EEKEEDAEEE DGEKKQKTKK VKETVYEWEL LNDVKAIWLR SPKEVTEEEY 

       370        380        390        400        410        420 
TKFYHSLSKD FTDEKPMAWS HFNAEGDVEF KAVLYVPPKA PHDLYESYYN SNKANLKLYV 

       430        440        450        460        470        480 
RRVFISDEFD ELLPKYLSFL KGLVDSDTLP LNVSREMLQQ HSSLKTIKKK LIRKALDMIR 

       490        500        510        520        530        540 
KLAEEDPDEI HDDEKKDVEK SGENDEKKGQ YTKFWNEFGK SVKLGIIEDA ANRNRLAKLL 

       550        560        570        580        590        600 
RFETTKSDGK LTSLDQYIKR MKKSQKDIFY ITGSSKEQLE KSPFLERLIK KGYEVIFFTD 

       610        620        630        640        650        660 
PVDEYLMQYL MDYEDKKFQN VSKEGLKVGK DSKDKELKEA FKELTKWWKG NLASENVDDV 

       670        680        690        700        710        720 
KISNRLADTP CVVVTSKFGW SANMERIMQS QTLSDANKQA YMRGKRVLEI NPRHPIIKEL 

       730        740        750        760        770        780 
KDRIASDPED ESVKETAQLM YQTALIESGF ILTDPKDFAA RIYNSVKSGL NISPDAVADE 

       790        800        810        820 
EIEAAEEPET SEATETKSDD LAGGLNIEAE PVEQQEENTK DEL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT09882.
RefSeqNP_194150.1. NM_118552.3. [Q9STX5-1]
UniGeneAt.24111.

3D structure databases

ProteinModelPortalQ9STX5.
SMRQ9STX5. Positions 75-776.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid13809. 1 interaction.
IntActQ9STX5. 9 interactions.

Proteomic databases

PaxDbQ9STX5.
PRIDEQ9STX5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G24190.1; AT4G24190.1; AT4G24190. [Q9STX5-1]
GeneID828520.
KEGGath:AT4G24190.

Organism-specific databases

TAIRAT4G24190.

Phylogenomic databases

eggNOGCOG0326.
HOGENOMHOG000031988.
InParanoidQ9STX5.
KOK09487.
OMAQSSHHPS.
PhylomeDBQ9STX5.

Gene expression databases

ArrayExpressQ9STX5.
GenevestigatorQ9STX5.

Family and domain databases

Gene3D3.30.565.10. 1 hit.
HAMAPMF_00505. HSP90.
InterProIPR003594. HATPase_ATP-bd.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERPTHR11528. PTHR11528. 1 hit.
PfamPF00183. HSP90. 1 hit.
[Graphical view]
PIRSFPIRSF002583. Hsp90. 1 hit.
PRINTSPR00775. HEATSHOCK90.
SMARTSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00298. HSP90. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9STX5.

Entry information

Entry nameENPL_ARATH
AccessionPrimary (citable) accession number: Q9STX5
Secondary accession number(s): O22972, Q56Y38, Q8VY71
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names