Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine/threonine-protein kinase/endoribonuclease IRE1

Gene

IRE1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.3 Publications

Miscellaneous

Present with 259 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

The kinase domain is activated by trans-autophosphorylation. Kinase activity is required for activation of the endoribonuclease domain.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei702ATP1
Active sitei797Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi680 – 688ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • endoribonuclease activity Source: SGD
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW
  • protein homodimerization activity Source: SGD
  • protein serine/threonine kinase activity Source: SGD
  • unfolded protein binding Source: SGD

GO - Biological processi

  • endoplasmic reticulum unfolded protein response Source: SGD
  • fungal-type cell wall organization Source: SGD
  • inositol metabolic process Source: SGD
  • mRNA processing Source: InterPro
  • protein homooligomerization Source: SGD
  • protein localization to Golgi apparatus Source: SGD
  • protein phosphorylation Source: SGD
  • protein trans-autophosphorylation Source: SGD
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • response to endoplasmic reticulum stress Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionHydrolase, Kinase, Multifunctional enzyme, Serine/threonine-protein kinase, Transferase
Biological processTranscription, Transcription regulation, Unfolded protein response
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31126-MONOMER
BRENDAi2.7.11.1 984
ReactomeiR-SCE-381070 IRE1alpha activates chaperones

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase/endoribonuclease IRE1
Alternative name(s):
Endoplasmic reticulum-to-nucleus signaling 1
Including the following 2 domains:
Gene namesi
Name:IRE1
Synonyms:ERN1
Ordered Locus Names:YHR079C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR079C
SGDiS000001121 IRE1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini19 – 526LumenalSequence analysisAdd BLAST508
Transmembranei527 – 555HelicalSequence analysisAdd BLAST29
Topological domaini556 – 1115CytoplasmicSequence analysisAdd BLAST560

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi702K → A: Loss of autophosphorylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000002433819 – 1115Serine/threonine-protein kinase/endoribonuclease IRE1Add BLAST1097

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi111N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi213N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi298N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi397N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei840Phosphoserine; by autocatalysis1 Publication1
Modified residuei841Phosphoserine; by autocatalysis1 Publication1

Post-translational modificationi

Autophosphorylated mainly on serine residues.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP32361
PaxDbiP32361
PRIDEiP32361

PTM databases

iPTMnetiP32361

Interactioni

Subunit structurei

Homodimer; in response to the accumulation of unfolded proteins.

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: SGD
  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi36513, 455 interactors
DIPiDIP-233N
IntActiP32361, 20 interactors
MINTiP32361
STRINGi4932.YHR079C

Structurei

Secondary structure

11115
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi116 – 127Combined sources12
Beta strandi132 – 136Combined sources5
Turni137 – 139Combined sources3
Beta strandi142 – 146Combined sources5
Helixi148 – 150Combined sources3
Beta strandi154 – 156Combined sources3
Turni162 – 164Combined sources3
Beta strandi165 – 171Combined sources7
Turni175 – 177Combined sources3
Beta strandi178 – 183Combined sources6
Turni184 – 186Combined sources3
Beta strandi187 – 194Combined sources8
Helixi195 – 199Combined sources5
Beta strandi203 – 207Combined sources5
Beta strandi222 – 226Combined sources5
Beta strandi228 – 237Combined sources10
Turni238 – 240Combined sources3
Beta strandi243 – 248Combined sources6
Beta strandi277 – 286Combined sources10
Beta strandi300 – 305Combined sources6
Turni308 – 310Combined sources3
Helixi311 – 314Combined sources4
Beta strandi321 – 323Combined sources3
Beta strandi326 – 329Combined sources4
Turni330 – 332Combined sources3
Beta strandi333 – 337Combined sources5
Beta strandi344 – 347Combined sources4
Beta strandi355 – 364Combined sources10
Turni365 – 368Combined sources4
Beta strandi369 – 374Combined sources6
Beta strandi390 – 394Combined sources5
Beta strandi400 – 404Combined sources5
Turni405 – 407Combined sources3
Helixi409 – 413Combined sources5
Helixi419 – 422Combined sources4
Helixi424 – 426Combined sources3
Helixi429 – 433Combined sources5
Helixi435 – 442Combined sources8
Beta strandi444 – 446Combined sources3
Turni666 – 669Combined sources4
Beta strandi674 – 682Combined sources9
Turni684 – 686Combined sources3
Beta strandi688 – 705Combined sources18
Helixi706 – 708Combined sources3
Helixi709 – 722Combined sources14
Beta strandi731 – 736Combined sources6
Beta strandi738 – 745Combined sources8
Beta strandi749 – 751Combined sources3
Helixi752 – 757Combined sources6
Helixi765 – 769Combined sources5
Helixi774 – 790Combined sources17
Helixi800 – 802Combined sources3
Beta strandi803 – 806Combined sources4
Helixi809 – 812Combined sources4
Beta strandi823 – 826Combined sources4
Turni836 – 838Combined sources3
Helixi851 – 855Combined sources5
Helixi858 – 861Combined sources4
Helixi900 – 914Combined sources15
Turni924 – 926Combined sources3
Helixi927 – 933Combined sources7
Helixi947 – 960Combined sources14
Helixi965 – 967Combined sources3
Helixi971 – 975Combined sources5
Helixi978 – 980Combined sources3
Helixi983 – 998Combined sources16
Turni1002 – 1005Combined sources4
Helixi1007 – 1013Combined sources7
Helixi1016 – 1019Combined sources4
Helixi1025 – 1028Combined sources4
Helixi1031 – 1035Combined sources5
Beta strandi1038 – 1041Combined sources4
Helixi1048 – 1060Combined sources13
Helixi1062 – 1064Combined sources3
Helixi1067 – 1072Combined sources6
Helixi1078 – 1087Combined sources10
Helixi1091 – 1102Combined sources12
Turni1107 – 1109Combined sources3
Helixi1110 – 1114Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP32361
SMRiP32361
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32361

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini674 – 980Protein kinasePROSITE-ProRule annotationAdd BLAST307
Domaini983 – 1115KENPROSITE-ProRule annotationAdd BLAST133

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000015684
HOGENOMiHOG000213215
InParanoidiP32361
KOiK08852
OMAiIVEPYGD
OrthoDBiEOG092C0PG1

Family and domain databases

Gene3Di1.20.1440.180, 1 hit
2.130.10.10, 1 hit
InterProiView protein in InterPro
IPR010513 KEN_dom
IPR038357 KEN_sf
IPR011009 Kinase-like_dom_sf
IPR018391 PQQ_beta_propeller_repeat
IPR000719 Prot_kinase_dom
IPR018997 PUB_domain
IPR011047 Quinoprotein_ADH-like_supfam
IPR008271 Ser/Thr_kinase_AS
IPR015943 WD40/YVTN_repeat-like_dom_sf
PfamiView protein in Pfam
PF00069 Pkinase, 2 hits
PF06479 Ribonuc_2-5A, 1 hit
SMARTiView protein in SMART
SM00564 PQQ, 3 hits
SM00580 PUG, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF50998 SSF50998, 1 hit
SSF56112 SSF56112, 2 hits
PROSITEiView protein in PROSITE
PS51392 KEN, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32361-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLRRNMLV LTLLVCVFSS IISCSIPLSS RTSRRQIVED EVASTKKLNF
60 70 80 90 100
NYGVDKNINS PIPAPRTTEG LPNMKLSSYP TPNLLNTADN RRANKKGRRA
110 120 130 140 150
ANSISVPYLE NRSLNELSLS DILIAADVEG GLHAVDRRNG HIIWSIEPEN
160 170 180 190 200
FQPLIEIQEP SRLETYETLI IEPFGDGNIY YFNAHQGLQK LPLSIRQLVS
210 220 230 240 250
TSPLHLKTNI VVNDSGKIVE DEKVYTGSMR TIMYTINMLN GEIISAFGPG
260 270 280 290 300
SKNGYFGSQS VDCSPEEKIK LQECENMIVI GKTIFELGIH SYDGASYNVT
310 320 330 340 350
YSTWQQNVLD VPLALQNTFS KDGMCIAPFR DKSLLASDLD FRIARWVSPT
360 370 380 390 400
FPGIIVGLFD VFNDLRTNEN ILVPHPFNPG DHESISSNKV YLDQTSNLSW
410 420 430 440 450
FALSSQNFPS LVESAPISRY ASSDRWRVSS IFEDETLFKN AIMGVHQIYN
460 470 480 490 500
NEYDHLYENY EKTNSLDTTH KYPPLMIDSS VDTTDLHQNN EMNSLKEYMS
510 520 530 540 550
PEDLEAYRKK IHEQISRELD EKNQNSLLLK FGSLVYRIIE TGVFLLLFLI
560 570 580 590 600
FCAILQRFKI LPPLYVLLSK IGFMPEKEIP IVESKSLNCP SSSENVTKPF
610 620 630 640 650
DMKSGKQVVF EGAVNDGSLK SEKDNDDADE DDEKSLDLTT EKKKRKRGSR
660 670 680 690 700
GGKKGRKSRI ANIPNFEQSL KNLVVSEKIL GYGSSGTVVF QGSFQGRPVA
710 720 730 740 750
VKRMLIDFCD IALMEIKLLT ESDDHPNVIR YYCSETTDRF LYIALELCNL
760 770 780 790 800
NLQDLVESKN VSDENLKLQK EYNPISLLRQ IASGVAHLHS LKIIHRDLKP
810 820 830 840 850
QNILVSTSSR FTADQQTGAE NLRILISDFG LCKKLDSGQS SFRTNLNNPS
860 870 880 890 900
GTSGWRAPEL LEESNNLQCQ VETEHSSSRH TVVSSDSFYD PFTKRRLTRS
910 920 930 940 950
IDIFSMGCVF YYILSKGKHP FGDKYSRESN IIRGIFSLDE MKCLHDRSLI
960 970 980 990 1000
AEATDLISQM IDHDPLKRPT AMKVLRHPLF WPKSKKLEFL LKVSDRLEIE
1010 1020 1030 1040 1050
NRDPPSALLM KFDAGSDFVI PSGDWTVKFD KTFMDNLERY RKYHSSKLMD
1060 1070 1080 1090 1100
LLRALRNKYH HFMDLPEDIA ELMGPVPDGF YDYFTKRFPN LLIGVYMIVK
1110
ENLSDDQILR EFLYS
Length:1,115
Mass (Da):126,976
Last modified:February 1, 1995 - v2
Checksum:iBD65D74E74365945
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti368N → S in CAA77763 (PubMed:1625574).Curated1
Sequence conflicti625 – 626ND → KH in CAA77763 (PubMed:1625574).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
PIRiA47541
RefSeqiNP_011946.1, NM_001179209.1

Genome annotation databases

EnsemblFungiiYHR079C; YHR079C; YHR079C
GeneIDi856478
KEGGisce:YHR079C

Similar proteinsi

Entry informationi

Entry nameiIRE1_YEAST
AccessioniPrimary (citable) accession number: P32361
Secondary accession number(s): D3DL29
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 1, 1995
Last modified: April 25, 2018
This is version 186 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health