IREA_DICDI
ID IREA_DICDI Reviewed; 984 AA.
AC Q55GJ2;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable serine/threonine-protein kinase ireA;
DE EC=2.7.11.1;
DE AltName: Full=Inositol-requiring protein A;
DE Flags: Precursor;
GN Name=ireA; ORFNames=DDB_G0267650;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AAFI02000003; EAL73278.1; -; Genomic_DNA.
DR RefSeq; XP_647192.1; XM_642100.1.
DR AlphaFoldDB; Q55GJ2; -.
DR SMR; Q55GJ2; -.
DR STRING; 44689.DDB0231217; -.
DR PaxDb; Q55GJ2; -.
DR EnsemblProtists; EAL73278; EAL73278; DDB_G0267650.
DR GeneID; 8615996; -.
DR KEGG; ddi:DDB_G0267650; -.
DR dictyBase; DDB_G0267650; ireA.
DR eggNOG; KOG1027; Eukaryota.
DR HOGENOM; CLU_004875_2_1_1; -.
DR InParanoid; Q55GJ2; -.
DR OMA; IDNIGRY; -.
DR Reactome; R-DDI-381070; IRE1alpha activates chaperones.
DR PRO; PR:Q55GJ2; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:dictyBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1990604; C:IRE1-TRAF2-ASK1 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004521; F:endoribonuclease activity; ISS:dictyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:dictyBase.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:dictyBase.
DR GO; GO:0006020; P:inositol metabolic process; ISS:dictyBase.
DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; ISS:dictyBase.
DR GO; GO:1903894; P:regulation of IRE1-mediated unfolded protein response; IMP:dictyBase.
DR Gene3D; 1.20.1440.180; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045133; IRE1/2-like.
DR InterPro; IPR010513; KEN_dom.
DR InterPro; IPR038357; KEN_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR13954; PTHR13954; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF06479; Ribonuc_2-5A; 1.
DR SMART; SM00564; PQQ; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51392; KEN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..984
FT /note="Probable serine/threonine-protein kinase ireA"
FT /id="PRO_0000362015"
FT TOPO_DOM 27..436
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..984
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 575..851
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 854..984
FT /note="KEN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00725"
FT REGION 70..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 467..533
FT /evidence="ECO:0000255"
FT COMPBIAS 472..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 722
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 581..589
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 603
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 984 AA; 112801 MW; 2D8B3444AD001E87 CRC64;
MTFSKTRNKI IFLLFLIIIN IFNINAYIKD ENEDDLSLLI STLDGNIYSF NYESGELNWD
LKPNGGDSLY STSQFDRKQQ QSTSTSTEIT KSSPSILIPT LDGSGLLFQY SNDRLHQVPF
SLQELVNTSP LFLKELEDKS STSSTSTTSE SSKDENKVTM FIGNKKTSIT VVDSQTGEII
KSMSKDGLWL TDEDDCPVNI IPDEALMFTR SDYQIIALDP KSGVEKWNLS VGEYIPHSTK
SFYNSEISLN FEGLIEVASL SQRMYKIYIK KPEKTVVGIS HNYWEHILTS SPVSIYAYSS
KKHILKKLDF HRKVSPYSNS LIPVASTDLM IPSNFDRTFM FDDYYGQLFI VSPPSNNNNN
NNNNNNNNNN NNNNNNNNNN NNNNNNNNNK NNNNNNKNES DKSNLTPLTP YDPSKPNGAN
NNNNNNNDLL DSNKLKNYDI YLYSSIVILI TSIIVFIRSK KNFNLINVNN NNNQNNNQNS
NQNNNINNKK TPKKKKKKQK NKNNKNNNDE DDENEIENYN DNQNDLIDEF ISTNSVIQQQ
QQQQQQLINS SNKINNGSGK IILDNGNVKI GKLEIITNKI LGTGSCGTIV YEGKMEGRKV
AVKRMLSQFV KFADREVSIL IHSDEHTNVV RYYAKEEDDE FIYLAISFCQ KSLDMYVQQT
LSLQISPTDS PSIQSSNNNG NGNNGNNNNN NQIIIDNKTK QMILELFKGL EHLHSLNIVH
RDIKPHNVLI DPNNRVKISD MGLGKLLDND DQSLTFTSDS HGWQPAEYLN GTNRNTKKVD
IFSLGCVVYY LLTGAHPFGH RYNREKNVLK GKFDIDQIKH LPDIHQLVHS MIQFEPEKRP
DIGECINHPF FWEVHKKLSF LVAASDYLEF EKPTSPLNLE IDSHVDLVTD GSGDWWLKID
QVLIDNIGRY RKYNGKSIRD LLRVIRNKFN HYRDLSPEEQ TCLGILPDGF FNYFDLKFPQ
LFIVTYLFIL KNLKNDQYFV QYYY
