IRE1_YEAST
ID IRE1_YEAST Reviewed; 1115 AA.
AC P32361; D3DL29;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Serine/threonine-protein kinase/endoribonuclease IRE1;
DE AltName: Full=Endoplasmic reticulum-to-nucleus signaling 1;
DE Includes:
DE RecName: Full=Serine/threonine-protein kinase;
DE EC=2.7.11.1;
DE Includes:
DE RecName: Full=Endoribonuclease;
DE EC=3.1.26.-;
DE Flags: Precursor;
GN Name=IRE1; Synonyms=ERN1; OrderedLocusNames=YHR079C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1625574; DOI=10.1111/j.1365-2958.1992.tb00864.x;
RA Nikawa J., Yamashita S.;
RT "IRE1 encodes a putative protein kinase containing a membrane-spanning
RT domain and is required for inositol phototrophy in Saccharomyces
RT cerevisiae.";
RL Mol. Microbiol. 6:1441-1446(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8358794; DOI=10.1016/0092-8674(93)90521-q;
RA Mori K., Ma W., Gething M.J., Sambrook J.;
RT "A transmembrane protein with a cdc2+/CDC28-related kinase activity is
RT required for signaling from the ER to the nucleus.";
RL Cell 74:743-756(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, ACTIVITY REGULATION, HOMODIMERIZATION, AND MUTAGENESIS OF
RP LYS-702.
RX PubMed=8663458; DOI=10.1074/jbc.271.30.18181;
RA Welihinda A.A., Kaufman R.J.;
RT "The unfolded protein response pathway in Saccharomyces cerevisiae.
RT Oligomerization and trans-phosphorylation of Ire1p (Ern1p) are required for
RT kinase activation.";
RL J. Biol. Chem. 271:18181-18187(1996).
RN [6]
RP FUNCTION, OLIGOMERIZATION, AND PHOSPHORYLATION AT SER-840 AND SER-841.
RX PubMed=8670804; DOI=10.1002/j.1460-2075.1996.tb00666.x;
RA Shamu C.E., Walter P.;
RT "Oligomerization and phosphorylation of the Ire1p kinase during
RT intracellular signaling from the endoplasmic reticulum to the nucleus.";
RL EMBO J. 15:3028-3039(1996).
RN [7]
RP FUNCTION.
RX PubMed=9323131; DOI=10.1016/s0092-8674(00)80369-4;
RA Sidrauski C., Walter P.;
RT "The transmembrane kinase Ire1p is a site-specific endonuclease that
RT initiates mRNA splicing in the unfolded protein response.";
RL Cell 90:1031-1039(1997).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Senses unfolded proteins in the lumen of the endoplasmic
CC reticulum via its N-terminal domain which leads to enzyme auto-
CC activation. The active endoribonuclease domain splices HAC1 precursor
CC mRNA to produce the mature form which then induces transcription of UPR
CC target genes. {ECO:0000269|PubMed:8663458, ECO:0000269|PubMed:8670804,
CC ECO:0000269|PubMed:9323131}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: The kinase domain is activated by trans-
CC autophosphorylation. Kinase activity is required for activation of the
CC endoribonuclease domain. {ECO:0000269|PubMed:8663458}.
CC -!- SUBUNIT: Homodimer; in response to the accumulation of unfolded
CC proteins.
CC -!- INTERACTION:
CC P32361; Q05924: DCR2; NbExp=2; IntAct=EBI-9364, EBI-3669144;
CC P32361; P32361: IRE1; NbExp=5; IntAct=EBI-9364, EBI-9364;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC I membrane protein.
CC -!- PTM: Autophosphorylated mainly on serine residues.
CC {ECO:0000269|PubMed:8670804}.
CC -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB68894.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z11701; CAA77763.1; -; Genomic_DNA.
DR EMBL; L19640; AAA34489.1; -; Genomic_DNA.
DR EMBL; U10556; AAB68894.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006934; DAA06773.1; -; Genomic_DNA.
DR PIR; A47541; A47541.
DR RefSeq; NP_011946.1; NM_001179209.1.
DR PDB; 2BE1; X-ray; 2.98 A; A/B=111-449.
DR PDB; 2RIO; X-ray; 2.40 A; A/B=658-1115.
DR PDB; 3FBV; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=641-1115.
DR PDB; 3LJ0; X-ray; 3.20 A; A/B=658-1115.
DR PDB; 3LJ1; X-ray; 3.33 A; A/B=658-1115.
DR PDB; 3LJ2; X-ray; 3.33 A; A/B=658-1115.
DR PDB; 3SDJ; X-ray; 3.65 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=641-1115.
DR PDB; 3SDM; X-ray; 6.60 A; A/B/C/D/E/F/G=641-1115.
DR PDBsum; 2BE1; -.
DR PDBsum; 2RIO; -.
DR PDBsum; 3FBV; -.
DR PDBsum; 3LJ0; -.
DR PDBsum; 3LJ1; -.
DR PDBsum; 3LJ2; -.
DR PDBsum; 3SDJ; -.
DR PDBsum; 3SDM; -.
DR AlphaFoldDB; P32361; -.
DR SMR; P32361; -.
DR BioGRID; 36513; 489.
DR ComplexPortal; CPX-2147; Ire1 serine/threonine-protein kinase/endoribonuclease complex.
DR DIP; DIP-233N; -.
DR IntAct; P32361; 5.
DR MINT; P32361; -.
DR STRING; 4932.YHR079C; -.
DR iPTMnet; P32361; -.
DR MaxQB; P32361; -.
DR PaxDb; P32361; -.
DR PRIDE; P32361; -.
DR EnsemblFungi; YHR079C_mRNA; YHR079C; YHR079C.
DR GeneID; 856478; -.
DR KEGG; sce:YHR079C; -.
DR SGD; S000001121; IRE1.
DR VEuPathDB; FungiDB:YHR079C; -.
DR eggNOG; KOG1027; Eukaryota.
DR GeneTree; ENSGT00940000167966; -.
DR HOGENOM; CLU_004875_2_1_1; -.
DR InParanoid; P32361; -.
DR OMA; VRYYCSE; -.
DR BioCyc; YEAST:G3O-31126-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR Reactome; R-SCE-381070; IRE1alpha activates chaperones.
DR EvolutionaryTrace; P32361; -.
DR PRO; PR:P32361; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P32361; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ComplexPortal.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:1990332; C:Ire1 complex; IPI:ComplexPortal.
DR GO; GO:1990604; C:IRE1-TRAF2-ASK1 complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0006020; P:inositol metabolic process; IMP:SGD.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IBA:GO_Central.
DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; IDA:ComplexPortal.
DR GO; GO:0098787; P:mRNA cleavage involved in mRNA processing; IDA:ComplexPortal.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:SGD.
DR GO; GO:0036290; P:protein trans-autophosphorylation; IDA:ComplexPortal.
DR GO; GO:0043620; P:regulation of DNA-templated transcription in response to stress; IDA:ComplexPortal.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:SGD.
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; 2.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Kinase; Magnesium; Membrane; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transcription;
KW Transcription regulation; Transferase; Transmembrane; Transmembrane helix;
KW Unfolded protein response.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1115
FT /note="Serine/threonine-protein kinase/endoribonuclease
FT IRE1"
FT /id="PRO_0000024338"
FT TOPO_DOM 19..526
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..555
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 556..1115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 674..980
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 983..1115
FT /note="KEN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00725"
FT REGION 617..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 797
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 680..688
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 702
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 840
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:8670804"
FT MOD_RES 841
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:8670804"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 702
FT /note="K->A: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:8663458"
FT CONFLICT 368
FT /note="N -> S (in Ref. 1; CAA77763)"
FT /evidence="ECO:0000305"
FT CONFLICT 625..626
FT /note="ND -> KH (in Ref. 1; CAA77763)"
FT /evidence="ECO:0000305"
FT STRAND 116..127
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:2BE1"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:2BE1"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:2BE1"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:2BE1"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:2BE1"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:2BE1"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 228..237
FT /evidence="ECO:0007829|PDB:2BE1"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 277..286
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:2BE1"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:2BE1"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:2BE1"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 355..364
FT /evidence="ECO:0007829|PDB:2BE1"
FT TURN 365..368
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 390..394
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:2BE1"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:2BE1"
FT HELIX 409..413
FT /evidence="ECO:0007829|PDB:2BE1"
FT HELIX 419..422
FT /evidence="ECO:0007829|PDB:2BE1"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:2BE1"
FT HELIX 429..433
FT /evidence="ECO:0007829|PDB:2BE1"
FT HELIX 435..442
FT /evidence="ECO:0007829|PDB:2BE1"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:2BE1"
FT TURN 666..669
FT /evidence="ECO:0007829|PDB:3LJ2"
FT STRAND 674..682
FT /evidence="ECO:0007829|PDB:2RIO"
FT TURN 684..686
FT /evidence="ECO:0007829|PDB:3FBV"
FT STRAND 688..705
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 706..708
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 709..722
FT /evidence="ECO:0007829|PDB:2RIO"
FT STRAND 731..736
FT /evidence="ECO:0007829|PDB:2RIO"
FT STRAND 738..745
FT /evidence="ECO:0007829|PDB:2RIO"
FT STRAND 749..751
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 752..757
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 765..769
FT /evidence="ECO:0007829|PDB:3FBV"
FT HELIX 774..790
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 800..802
FT /evidence="ECO:0007829|PDB:2RIO"
FT STRAND 803..806
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 809..812
FT /evidence="ECO:0007829|PDB:2RIO"
FT STRAND 823..826
FT /evidence="ECO:0007829|PDB:2RIO"
FT TURN 836..838
FT /evidence="ECO:0007829|PDB:3FBV"
FT HELIX 851..855
FT /evidence="ECO:0007829|PDB:3FBV"
FT HELIX 858..861
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 900..914
FT /evidence="ECO:0007829|PDB:2RIO"
FT TURN 924..926
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 927..933
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 947..960
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 965..967
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 971..975
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 978..980
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 983..998
FT /evidence="ECO:0007829|PDB:2RIO"
FT TURN 1002..1005
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 1007..1013
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 1016..1019
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 1025..1028
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 1031..1035
FT /evidence="ECO:0007829|PDB:3FBV"
FT STRAND 1038..1041
FT /evidence="ECO:0007829|PDB:3FBV"
FT HELIX 1048..1060
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 1062..1064
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 1067..1072
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 1078..1087
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 1091..1102
FT /evidence="ECO:0007829|PDB:2RIO"
FT TURN 1107..1109
FT /evidence="ECO:0007829|PDB:2RIO"
FT HELIX 1110..1114
FT /evidence="ECO:0007829|PDB:2RIO"
SQ SEQUENCE 1115 AA; 126976 MW; BD65D74E74365945 CRC64;
MRLLRRNMLV LTLLVCVFSS IISCSIPLSS RTSRRQIVED EVASTKKLNF NYGVDKNINS
PIPAPRTTEG LPNMKLSSYP TPNLLNTADN RRANKKGRRA ANSISVPYLE NRSLNELSLS
DILIAADVEG GLHAVDRRNG HIIWSIEPEN FQPLIEIQEP SRLETYETLI IEPFGDGNIY
YFNAHQGLQK LPLSIRQLVS TSPLHLKTNI VVNDSGKIVE DEKVYTGSMR TIMYTINMLN
GEIISAFGPG SKNGYFGSQS VDCSPEEKIK LQECENMIVI GKTIFELGIH SYDGASYNVT
YSTWQQNVLD VPLALQNTFS KDGMCIAPFR DKSLLASDLD FRIARWVSPT FPGIIVGLFD
VFNDLRTNEN ILVPHPFNPG DHESISSNKV YLDQTSNLSW FALSSQNFPS LVESAPISRY
ASSDRWRVSS IFEDETLFKN AIMGVHQIYN NEYDHLYENY EKTNSLDTTH KYPPLMIDSS
VDTTDLHQNN EMNSLKEYMS PEDLEAYRKK IHEQISRELD EKNQNSLLLK FGSLVYRIIE
TGVFLLLFLI FCAILQRFKI LPPLYVLLSK IGFMPEKEIP IVESKSLNCP SSSENVTKPF
DMKSGKQVVF EGAVNDGSLK SEKDNDDADE DDEKSLDLTT EKKKRKRGSR GGKKGRKSRI
ANIPNFEQSL KNLVVSEKIL GYGSSGTVVF QGSFQGRPVA VKRMLIDFCD IALMEIKLLT
ESDDHPNVIR YYCSETTDRF LYIALELCNL NLQDLVESKN VSDENLKLQK EYNPISLLRQ
IASGVAHLHS LKIIHRDLKP QNILVSTSSR FTADQQTGAE NLRILISDFG LCKKLDSGQS
SFRTNLNNPS GTSGWRAPEL LEESNNLQCQ VETEHSSSRH TVVSSDSFYD PFTKRRLTRS
IDIFSMGCVF YYILSKGKHP FGDKYSRESN IIRGIFSLDE MKCLHDRSLI AEATDLISQM
IDHDPLKRPT AMKVLRHPLF WPKSKKLEFL LKVSDRLEIE NRDPPSALLM KFDAGSDFVI
PSGDWTVKFD KTFMDNLERY RKYHSSKLMD LLRALRNKYH HFMDLPEDIA ELMGPVPDGF
YDYFTKRFPN LLIGVYMIVK ENLSDDQILR EFLYS
