EIX2_SOLLC
ID EIX2_SOLLC Reviewed; 1021 AA.
AC Q6JN46; K4CBY2;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Receptor-like protein EIX2 {ECO:0000305};
DE AltName: Full=EIX receptor 2 {ECO:0000312|EMBL:AAR28378.1};
DE Flags: Precursor;
GN Name=EIX2 {ECO:0000312|EMBL:AAR28378.1};
GN OrderedLocusNames=Solyc07g008630.1.1;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH EIX ELICITOR,
RP AND MUTAGENESIS OF TYR-993.
RC STRAIN=cv. Rio Grande;
RX PubMed=15155877; DOI=10.1105/tpc.022475;
RA Ron M., Avni A.;
RT "The receptor for the fungal elicitor ethylene-inducing xylanase is a
RT member of a resistance-like gene family in tomato.";
RL Plant Cell 16:1604-1615(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
CC -!- FUNCTION: Involved in plant defense. Confers resistance to the fungal
CC pathogen T.viride through recognition of the EIX elicitor protein.
CC {ECO:0000269|PubMed:15155877}.
CC -!- SUBUNIT: Interacts with EIX elicitor protein.
CC {ECO:0000269|PubMed:15155877}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RLP family. {ECO:0000305}.
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DR EMBL; AY359966; AAR28378.1; -; Genomic_DNA.
DR EMBL; CM001070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004243038.3; XM_004242990.3.
DR AlphaFoldDB; Q6JN46; -.
DR SMR; Q6JN46; -.
DR STRING; 4081.Solyc07g008630.1.1; -.
DR PRIDE; Q6JN46; -.
DR EnsemblPlants; Solyc07g008630.1.1; Solyc07g008630.1.1.1; Solyc07g008630.1.
DR GeneID; 101263330; -.
DR Gramene; Solyc07g008630.1.1; Solyc07g008630.1.1.1; Solyc07g008630.1.
DR KEGG; sly:101263330; -.
DR eggNOG; KOG0619; Eukaryota.
DR OMA; SSAEYSW; -.
DR OrthoDB; 826997at2759; -.
DR Proteomes; UP000004994; Chromosome 7.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR SMART; SM00369; LRR_TYP; 10.
DR PROSITE; PS51450; LRR; 19.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Leucine-rich repeat; Membrane; Plant defense;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1021
FT /note="Receptor-like protein EIX2"
FT /id="PRO_5004275128"
FT TOPO_DOM 25..963
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 964..984
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 985..1021
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 113..136
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 138..161
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 162..184
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 186..211
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 214..237
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 239..262
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 265..288
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 290..313
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 314..337
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 342..365
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 366..388
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 389..412
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 413..436
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 437..459
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 461..483
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 484..507
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 509..532
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 533..555
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 557..581
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 583..607
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 608..626
FT /note="LRR 21; degenerate"
FT /evidence="ECO:0000305"
FT REPEAT 627..651
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 652..675
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 677..698
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 699..722
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT REPEAT 723..747
FT /note="LRR 26"
FT /evidence="ECO:0000255"
FT REPEAT 749..773
FT /note="LRR 27"
FT /evidence="ECO:0000255"
FT REPEAT 818..842
FT /note="LRR 28"
FT /evidence="ECO:0000255"
FT REPEAT 843..866
FT /note="LRR 29"
FT /evidence="ECO:0000255"
FT REPEAT 867..890
FT /note="LRR 30"
FT /evidence="ECO:0000255"
FT REPEAT 892..913
FT /note="LRR 31"
FT /evidence="ECO:0000255"
FT REGION 25..109
FT /note="N-cap"
FT /evidence="ECO:0000305|PubMed:15155877"
FT REGION 914..963
FT /note="C-cap/acidic domain"
FT /evidence="ECO:0000305|PubMed:15155877"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 650
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 770
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 778
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 849
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 856
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 889
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 993
FT /note="Y->A: Abolishes hypersensitive response (HR) to EIX
FT elicitor."
FT /evidence="ECO:0000269|PubMed:15155877"
FT CONFLICT 41
FT /note="D -> G (in Ref. 1; AAR28378)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="T -> P (in Ref. 1; AAR28378)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1021 AA; 114821 MW; 72C30C22181C2E95 CRC64;
MGKRTNPRHF LVTWSLLLLE TAFGLTSREV NKTLCIEKER DALLEFKRGL NDDFGRLSTW
GDEEECCNWK GIECDKRTGH VIVLDLHSEV TCPGHACFAP ILTGKVSPSL LELEYLNFLD
LSVNGFENSE IPRFIGSLKR LEYLNLSSSD FSGEIPAQFQ NLTSLRILDL GNNNLIVKDL
VWLSHLSSLE FLRLGGNDFQ ARNWFREITK VPSLKELDLS VCGLSKFVPS PADVANSSLI
SLSVLHLCCN EFSTSSEYSW LFNFSTSLTS IDLSHNQLSR QIDDRFGSLM YLEHLNLANN
FGAEGGVPSS FGNLTRLHYL DMSNTQTYQW LPELFLRLSG SRKSLEVLGL NDNSLFGSIV
NVTRFSSLKK LYLQKNMLNG FFMERVGQVS SLEYLDLSDN QMRGPLPDLA LFPSLRELHL
GSNQFQGRIP QGIGKLSQLR IFDVSSNRLE GLPESMGQLS NLERFDASYN VLKGTITESH
FSNLSSLVDL DLSFNLLSLN TRFDWVPPFQ LQFIRLPSCN MGPSFPKWLQ TQNNYTLLDI
SLANISDMLP SWFSNLPPEL KILNLSNNHI SGRVSEFIVS KQDYMIIDLS SNNFSGHLPL
VPANIQIFYL HKNHFSGSIS SICRNTIGAA TSIDLSRNQF SGEVPDCWMN MSNLAVLNLA
YNNFSGKVPQ SLGSLTNLEA LYIRQNSFRG MLPSFSQCQL LQILDIGGNK LTGRIPAWIG
TDLLQLRILS LRSNKFDGSI PSLICQLQFL QILDLSENGL SGKIPQCLNN FTILRQENGS
GESMDFKVRY DYIPGSYLYI GDLLIQWKNQ ESEYKNALLY LKIIDLSSNK LVGGIPKEIA
EMRGLRSLNL SRNDLNGTVV EGIGQMKLLE SLDLSRNQLS GMIPQGLSNL TFLSVLDLSN
NHLSGRIPSS TQLQSFDRSS YSGNAQLCGP PLEECPGYAP PIDRGSNTNP QEHDDDDEFS
SLEFYVSMVL GFFVTFWGIL GCLIVNRSWR NAYFTFLTDM KSWLHMTSRV CFARLKGKLR
N
