EIX1_SOLLC
ID EIX1_SOLLC Reviewed; 1031 AA.
AC Q6JN47; K4CBY1;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Receptor-like protein EIX1 {ECO:0000305};
DE AltName: Full=EIX receptor 1 {ECO:0000312|EMBL:AAR28377.1};
DE Flags: Precursor;
GN Name=EIX1 {ECO:0000312|EMBL:AAR28377.1};
GN OrderedLocusNames=Solyc07g008620.1.1;
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 [MRNA], AND FUNCTION.
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:0000250|UniProtKB:Q6JN46}.
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; AY359965; AAR28377.1; -; mRNA.
DR EMBL; CM001070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001234427.1; NM_001247498.2.
DR AlphaFoldDB; Q6JN47; -.
DR SMR; Q6JN47; -.
DR STRING; 4081.Solyc07g008620.1.1; -.
DR PRIDE; Q6JN47; -.
DR EnsemblPlants; Solyc07g008620.1.1; Solyc07g008620.1.1.1; Solyc07g008620.1.
DR GeneID; 543900; -.
DR Gramene; Solyc07g008620.1.1; Solyc07g008620.1.1.1; Solyc07g008620.1.
DR KEGG; sly:543900; -.
DR eggNOG; KOG0619; Eukaryota.
DR OMA; EIPRFIC; -.
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; -; 6.
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; PF13855; LRR_8; 5.
DR Pfam; PF08263; LRRNT_2; 1.
DR SMART; SM00369; LRR_TYP; 11.
DR PROSITE; PS51450; LRR; 19.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Leucine-rich repeat; Membrane; Plant defense;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000305|PubMed:15155877"
FT CHAIN 30..1031
FT /note="Receptor-like protein EIX1"
FT /id="PRO_5004276343"
FT TOPO_DOM 30..971
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 972..992
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 993..1031
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 117..140
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 142..165
FT /note="LRR 2; degenerate"
FT /evidence="ECO:0000305"
FT REPEAT 166..189
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 191..215
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 216..240
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 243..266
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 269..292
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 293..317
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 318..341
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 346..369
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 370..393
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 394..416
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 417..440
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 441..463
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 465..487
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 488..509
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 512..536
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 538..559
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 561..584
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 586..611
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 612..629
FT /note="LRR 21; degenerate"
FT /evidence="ECO:0000305"
FT REPEAT 630..654
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 655..678
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 679..703
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 705..725
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT REPEAT 726..750
FT /note="LRR 26"
FT /evidence="ECO:0000255"
FT REPEAT 752..773
FT /note="LRR 27"
FT /evidence="ECO:0000255"
FT REPEAT 823..847
FT /note="LRR 28"
FT /evidence="ECO:0000255"
FT REPEAT 848..871
FT /note="LRR 29"
FT /evidence="ECO:0000255"
FT REPEAT 872..895
FT /note="LRR 30"
FT /evidence="ECO:0000255"
FT REPEAT 896..918
FT /note="LRR 31"
FT /evidence="ECO:0000255"
FT REGION 30..113
FT /note="N-cap"
FT /evidence="ECO:0000305|PubMed:15155877"
FT REGION 919..971
FT /note="C-cap/acidic domain"
FT /evidence="ECO:0000305|PubMed:15155877"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 773
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 781
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 854
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 861
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 894
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 232
FT /note="V -> A (in Ref. 1; AAR28377)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="L -> F (in Ref. 1; AAR28377)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1031 AA; 115747 MW; C787B9BE6F27F7B0 CRC64;
MDKWKYARLA QFLFTLSLLF LETSFGLGGN KTLCLDKERD ALLEFKRGLT DSFDHLSTWG
DEEDKQECCK WKGIECDRRT GHVTVIDLHN KFTCSAGASA CFAPRLTGKL SPSLLELEYL
NYLDLSVNEF ERSEIPRFIG SLKRLEYLNL SASFFSGVIP IQFQNLTSLR TLDLGENNLI
VKDLRWLSHL SSLEFLSLSS SNFQVNNWFQ EITKVPSLKE LDLSGCGLSK LVPSQADLAN
SSLISLSVLH LCCNEFSSSS EYSWVFNLTT SLTSIDLLYN QLSGQIDDRF GTLMYLEHLD
LANNLKIEGG VPSSFGNLTR LRHLDMSNTQ TVQWLPELFL RLSGSRKSLE VLGLNENSLF
GSIVNATRFS SLKKLYLQKN MLNGSFMESA GQVSTLEYLD LSENQMRGAL PDLALFPSLR
ELHLGSNQFR GRIPQGIGKL SQLRILDVSS NRLEGLPESM GQLSNLESFD ASYNVLKGTI
TESHLSNLSS LVDLDLSFNS LALKTSFNWL PPFQLQVISL PSCNLGPSFP KWLQNQNNYT
VLDISLASIS DTLPSWFSSF PPDLKILNLS NNQISGRVSD LIENTYGYRV IDLSYNNFSG
ALPLVPTNVQ IFYLHKNQFF GSISSICRSR TSPTSLDLSH NQFSGELPDC WMNMTSLAVL
NLAYNNFSGE IPHSLGSLTN LKALYIRQNS LSGMLPSFSQ CQGLQILDLG GNKLTGSIPG
WIGTDLLNLR ILSLRFNRLH GSIPSIICQL QFLQILDLSA NGLSGKIPHC FNNFTLLYQD
NNSGEPMEFI VQGFYGKFPR RYLYIGDLLV QWKNQESEYK NPLLYLKTID LSSNELIGGV
PKEIADMRGL KSLNLSRNEL NGTVIEGIGQ MRMLESLDMS RNQLSGVIPQ DLANLTFLSV
LDLSNNQLSG RIPSSTQLQS FDRSSYSDNA QLCGPPLQEC PGYAPPSPLI DHGSNNNPQE
HDEEEEFPSL EFYISMVLSF FVAFWGILGC LIVNSSWRNA YFKFLTDTTS WLDMISRVWF
ARLKKKLRRA R
