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P32361 (IRE1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase/endoribonuclease IRE1
Alternative name(s):
Endoplasmic reticulum-to-nucleus signaling 1

Including the following 2 domains:

  1. Serine/threonine-protein kinase
    EC=2.7.11.1
  2. Endoribonuclease
    EC=3.1.26.-
Gene names
Name:IRE1
Synonyms:ERN1
Ordered Locus Names:YHR079C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1115 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto-activation. The active endoribonuclease domain splices HAC1 precursor mRNA to produce the mature form which then induces transcription of UPR target genes. Ref.5 Ref.6 Ref.7

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Enzyme regulation

The kinase domain is activated by trans-autophosphorylation. Kinase activity is required for activation of the endoribonuclease domain. Ref.5

Subunit structure

Homodimer; in response to the accumulation of unfolded proteins. Ref.5 Ref.6

Subcellular location

Endoplasmic reticulum membrane; Single-pass type I membrane protein.

Post-translational modification

Autophosphorylated mainly on serine residues. Ref.6

Miscellaneous

Present with 259 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 1 KEN domain.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAB68894.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Unfolded protein response
   Cellular componentEndoplasmic reticulum
Membrane
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
Kinase
Serine/threonine-protein kinase
Transferase
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processRNA phosphodiester bond hydrolysis, endonucleolytic

Inferred from direct assay Ref.7. Source: GOC

endoplasmic reticulum unfolded protein response

Inferred from mutant phenotype Ref.2PubMed 8513503. Source: SGD

fungal-type cell wall organization

Inferred from mutant phenotype PubMed 18971375PubMed 8898193. Source: SGD

inositol metabolic process

Inferred from mutant phenotype Ref.1. Source: SGD

mRNA processing

Inferred from electronic annotation. Source: InterPro

protein homooligomerization

Inferred from direct assay Ref.5. Source: SGD

protein phosphorylation

Inferred from direct assay Ref.5. Source: SGD

protein trans-autophosphorylation

Inferred from direct assay Ref.5. Source: SGD

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentendoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of endoplasmic reticulum membrane

Inferred from direct assay Ref.2. Source: SGD

nucleus

Inferred from direct assay PubMed 17035634. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

endoribonuclease activity

Inferred from direct assay Ref.7. Source: SGD

identical protein binding

Inferred from physical interaction PubMed 18191223. Source: IntAct

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 16990850. Source: IntAct

protein homodimerization activity

Inferred from direct assay PubMed 15954865. Source: SGD

protein serine/threonine kinase activity

Inferred from direct assay Ref.5. Source: SGD

unfolded protein binding

Inferred from direct assay PubMed 17923530. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-9364,EBI-9364
DCR2Q059242EBI-9364,EBI-3669144

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 11151097Serine/threonine-protein kinase/endoribonuclease IRE1
PRO_0000024338

Regions

Topological domain19 – 526508Lumenal Potential
Transmembrane527 – 55529Helical; Potential
Topological domain556 – 1115560Cytoplasmic Potential
Domain674 – 980307Protein kinase
Domain983 – 1115133KEN
Nucleotide binding680 – 6889ATP By similarity

Sites

Active site7971Proton acceptor By similarity
Binding site7021ATP

Amino acid modifications

Modified residue8401Phosphoserine; by autocatalysis Probable
Modified residue8411Phosphoserine; by autocatalysis Probable
Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation2131N-linked (GlcNAc...) Potential
Glycosylation2981N-linked (GlcNAc...) Potential
Glycosylation3971N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis7021K → A: Loss of autophosphorylation. Ref.5
Sequence conflict3681N → S in CAA77763. Ref.1
Sequence conflict625 – 6262ND → KH in CAA77763. Ref.1

Secondary structure

............................................................................................................................................ 1115
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32361 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: BD65D74E74365945

FASTA1,115126,976
        10         20         30         40         50         60 
MRLLRRNMLV LTLLVCVFSS IISCSIPLSS RTSRRQIVED EVASTKKLNF NYGVDKNINS 

        70         80         90        100        110        120 
PIPAPRTTEG LPNMKLSSYP TPNLLNTADN RRANKKGRRA ANSISVPYLE NRSLNELSLS 

       130        140        150        160        170        180 
DILIAADVEG GLHAVDRRNG HIIWSIEPEN FQPLIEIQEP SRLETYETLI IEPFGDGNIY 

       190        200        210        220        230        240 
YFNAHQGLQK LPLSIRQLVS TSPLHLKTNI VVNDSGKIVE DEKVYTGSMR TIMYTINMLN 

       250        260        270        280        290        300 
GEIISAFGPG SKNGYFGSQS VDCSPEEKIK LQECENMIVI GKTIFELGIH SYDGASYNVT 

       310        320        330        340        350        360 
YSTWQQNVLD VPLALQNTFS KDGMCIAPFR DKSLLASDLD FRIARWVSPT FPGIIVGLFD 

       370        380        390        400        410        420 
VFNDLRTNEN ILVPHPFNPG DHESISSNKV YLDQTSNLSW FALSSQNFPS LVESAPISRY 

       430        440        450        460        470        480 
ASSDRWRVSS IFEDETLFKN AIMGVHQIYN NEYDHLYENY EKTNSLDTTH KYPPLMIDSS 

       490        500        510        520        530        540 
VDTTDLHQNN EMNSLKEYMS PEDLEAYRKK IHEQISRELD EKNQNSLLLK FGSLVYRIIE 

       550        560        570        580        590        600 
TGVFLLLFLI FCAILQRFKI LPPLYVLLSK IGFMPEKEIP IVESKSLNCP SSSENVTKPF 

       610        620        630        640        650        660 
DMKSGKQVVF EGAVNDGSLK SEKDNDDADE DDEKSLDLTT EKKKRKRGSR GGKKGRKSRI 

       670        680        690        700        710        720 
ANIPNFEQSL KNLVVSEKIL GYGSSGTVVF QGSFQGRPVA VKRMLIDFCD IALMEIKLLT 

       730        740        750        760        770        780 
ESDDHPNVIR YYCSETTDRF LYIALELCNL NLQDLVESKN VSDENLKLQK EYNPISLLRQ 

       790        800        810        820        830        840 
IASGVAHLHS LKIIHRDLKP QNILVSTSSR FTADQQTGAE NLRILISDFG LCKKLDSGQS 

       850        860        870        880        890        900 
SFRTNLNNPS GTSGWRAPEL LEESNNLQCQ VETEHSSSRH TVVSSDSFYD PFTKRRLTRS 

       910        920        930        940        950        960 
IDIFSMGCVF YYILSKGKHP FGDKYSRESN IIRGIFSLDE MKCLHDRSLI AEATDLISQM 

       970        980        990       1000       1010       1020 
IDHDPLKRPT AMKVLRHPLF WPKSKKLEFL LKVSDRLEIE NRDPPSALLM KFDAGSDFVI 

      1030       1040       1050       1060       1070       1080 
PSGDWTVKFD KTFMDNLERY RKYHSSKLMD LLRALRNKYH HFMDLPEDIA ELMGPVPDGF 

      1090       1100       1110 
YDYFTKRFPN LLIGVYMIVK ENLSDDQILR EFLYS 

« Hide

References

« Hide 'large scale' references
[1]"IRE1 encodes a putative protein kinase containing a membrane-spanning domain and is required for inositol phototrophy in Saccharomyces cerevisiae."
Nikawa J., Yamashita S.
Mol. Microbiol. 6:1441-1446(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus."
Mori K., Ma W., Gething M.J., Sambrook J.
Cell 74:743-756(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"The unfolded protein response pathway in Saccharomyces cerevisiae. Oligomerization and trans-phosphorylation of Ire1p (Ern1p) are required for kinase activation."
Welihinda A.A., Kaufman R.J.
J. Biol. Chem. 271:18181-18187(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, HOMODIMERIZATION, MUTAGENESIS OF LYS-702.
[6]"Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus."
Shamu C.E., Walter P.
EMBO J. 15:3028-3039(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, OLIGOMERIZATION, PHOSPHORYLATION.
[7]"The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response."
Sidrauski C., Walter P.
Cell 90:1031-1039(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z11701 Genomic DNA. Translation: CAA77763.1.
L19640 Genomic DNA. Translation: AAA34489.1.
U10556 Genomic DNA. Translation: AAB68894.1. Different initiation.
BK006934 Genomic DNA. Translation: DAA06773.1.
PIRA47541.
RefSeqNP_011946.1. NM_001179209.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BE1X-ray2.98A/B111-449[»]
2RIOX-ray2.40A/B658-1115[»]
3FBVX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L/M/N641-1115[»]
3LJ0X-ray3.20A/B658-1115[»]
3LJ1X-ray3.33A/B658-1115[»]
3LJ2X-ray3.33A/B658-1115[»]
3SDJX-ray3.65A/B/C/D/E/F/G/H/I/J/K/L/M/N641-1115[»]
3SDMX-ray6.60A/B/C/D/E/F/G641-1115[»]
ProteinModelPortalP32361.
SMRP32361. Positions 111-449, 663-1115.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36513. 334 interactions.
DIPDIP-233N.
IntActP32361. 4 interactions.
MINTMINT-408165.
STRING4932.YHR079C.

Proteomic databases

MaxQBP32361.
PRIDEP32361.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR079C; YHR079C; YHR079C.
GeneID856478.
KEGGsce:YHR079C.

Organism-specific databases

CYGDYHR079c.
SGDS000001121. IRE1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00390000015684.
HOGENOMHOG000213215.
KOK08852.
OMANILWFVE.
OrthoDBEOG7X3R27.

Enzyme and pathway databases

BioCycYEAST:G3O-31126-MONOMER.
BRENDA2.7.11.1. 984.

Gene expression databases

GenevestigatorP32361.

Family and domain databases

Gene3D2.140.10.10. 1 hit.
InterProIPR010513. KEN_dom.
IPR011009. Kinase-like_dom.
IPR018391. PQQ_beta_propeller_repeat.
IPR000719. Prot_kinase_dom.
IPR006567. PUG-dom.
IPR027295. Quinonprotein_ADH-like_fam.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF06479. Ribonuc_2-5A. 1 hit.
[Graphical view]
SMARTSM00564. PQQ. 3 hits.
SM00580. PUG. 1 hit.
[Graphical view]
SUPFAMSSF50998. SSF50998. 1 hit.
SSF56112. SSF56112. 2 hits.
PROSITEPS51392. KEN. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32361.
NextBio982158.
PROP32361.

Entry information

Entry nameIRE1_YEAST
AccessionPrimary (citable) accession number: P32361
Secondary accession number(s): D3DL29
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references