CF9_SOLPI
ID CF9_SOLPI Reviewed; 863 AA.
AC Q40235;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Receptor-like protein Cf-9 {ECO:0000305};
DE Flags: Precursor;
GN Name=CF-9 {ECO:0000312|EMBL:AAA65235.1, ECO:0000312|EMBL:CAA05274.1};
OS Solanum pimpinellifolium (Currant tomato) (Lycopersicon pimpinellifolium).
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=4084;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Cf9;
RX PubMed=7973631; DOI=10.1126/science.7973631;
RA Jones D.A., Thomas C.M., Hammond-Kosack K.E., Balint-Kurti P.J.,
RA Jones J.D.;
RT "Isolation of the tomato Cf-9 gene for resistance to Cladosporium fulvum by
RT transposon tagging.";
RL Science 266:789-793(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=cv. Cf9;
RX PubMed=9413991; DOI=10.1016/s0092-8674(00)80470-5;
RA Parniske M., Hammond-Kosack K.E., Golstein C., Thomas C.M., Jones D.A.,
RA Harrison K., Wulff B.B., Jones J.D.;
RT "Novel disease resistance specificities result from sequence exchange
RT between tandemly repeated genes at the Cf-4/9 locus of tomato.";
RL Cell 91:821-832(1997).
RN [3]
RP DOMAIN.
RX PubMed=11226184; DOI=10.2307/3871275;
RA Wulff B.B., Thomas C.M., Smoker M., Grant M., Jones J.D.;
RT "Domain swapping and gene shuffling identify sequences required for
RT induction of an Avr-dependent hypersensitive response by the tomato Cf-4
RT and Cf-9 proteins.";
RL Plant Cell 13:255-272(2001).
RN [4]
RP FUNCTION.
RX PubMed=11517316; DOI=10.1073/pnas.181241798;
RA Van Der Hoorn R.A.L., Kruijt M., Roth R., Brandwagt B.F., Joosten M.H.A.J.,
RA De Wit P.J.G.M.;
RT "Intragenic recombination generated two distinct Cf genes that mediate AVR9
RT recognition in the natural population of Lycopersicon pimpinellifolium.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10493-10498(2001).
RN [5]
RP RETRACTED PAPER.
RX PubMed=15131698; DOI=10.1038/sj.emboj.7600224;
RA Rivas S., Rougon-Cardoso A., Smoker M., Schauser L., Yoshioka H.,
RA Jones J.D.;
RT "CITRX thioredoxin interacts with the tomato Cf-9 resistance protein and
RT negatively regulates defence.";
RL EMBO J. 23:2156-2165(2004).
RN [6]
RP RETRACTION NOTICE OF PUBMED:15131698.
RX PubMed=31310343; DOI=10.15252/embj.2019102435;
RA Rivas S., Rougon-Cardoso A., Smoker M., Schauser L., Yoshioka H.,
RA Jones J.D.;
RL EMBO J. 38:e102435-e102435(2019).
RN [7]
RP MUTAGENESIS OF ASP-365; LEU-457; ASP-508; SER-676 AND GLY-825.
RX PubMed=15166169; DOI=10.1534/genetics.167.1.459;
RA Wulff B.B., Thomas C.M., Parniske M., Jones J.D.;
RT "Genetic variation at the tomato Cf-4/Cf-9 locus induced by EMS mutagenesis
RT and intralocus recombination.";
RL Genetics 167:459-470(2004).
RN [8]
RP MUTAGENESIS OF TRP-71; CYS-78; TRP-80; CYS-85; ASN-191; THR-193; ASN-262;
RP ASN-311; THR-313; ASP-365; SER-380; ASN-396; ASP-508; SER-676 AND ASP-722,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND LACK OF GLYCOSYLATION AT ASN-674.
RX PubMed=15722474; DOI=10.1105/tpc.104.028118;
RA van der Hoorn R.A., Wulff B.B., Rivas S., Durrant M.C., van der Ploeg A.,
RA de Wit P.J., Jones J.D.;
RT "Structure-function analysis of cf-9, a receptor-like protein with
RT extracytoplasmic leucine-rich repeats.";
RL Plant Cell 17:1000-1015(2005).
RN [9]
RP INDUCTION BY AVR9, AND REGULATION BY SLY-MIR6022.
RX PubMed=26768363; DOI=10.1016/j.bbrc.2016.01.015;
RA Li W., Xu Y.P., Cai X.Z.;
RT "Transcriptional and posttranscriptional regulation of the tomato leaf
RT mould disease resistance gene Cf-9.";
RL Biochem. Biophys. Res. Commun. 470:163-167(2016).
RN [10]
RP MUTAGENESIS OF THR-835; GLN-836 AND PRO-838, AND INTERACTION WITH CITRX.
RX PubMed=26315781; DOI=10.1111/mpp.12315;
RA Chakrabarti A., Velusamy T., Tee C.Y., Jones D.A.;
RT "A mutational analysis of the cytosolic domain of the tomato Cf-9 disease-
RT resistance protein shows that membrane-proximal residues are important for
RT Avr9-dependent necrosis.";
RL Mol. Plant Pathol. 17:565-576(2016).
CC -!- FUNCTION: Involved in plant defense. Confers resistance to the fungal
CC pathogen C.fulvum through recognition of the AVR9 elicitor protein.
CC {ECO:0000269|PubMed:11517316, ECO:0000269|PubMed:7973631,
CC ECO:0000269|PubMed:9413991}.
CC -!- SUBUNIT: Interacts with thioredoxin-like protein CITRX.
CC {ECO:0000269|PubMed:26315781}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Induced by C.fulvum AVR9 elicitor protein in a temperature-
CC sensitive manner. Repressed by sly-miR6022.
CC {ECO:0000269|PubMed:26768363}.
CC -!- DOMAIN: The extracellular leucine-rich repeats are required for the
CC specificity of the elicitor protein recognition. Important sequence
CC determinants of Cf-9 function are located in LRRs 10 to 18.
CC {ECO:0000269|PubMed:11226184}.
CC -!- SIMILARITY: Belongs to the RLP family. {ECO:0000305}.
CC -!- CAUTION: The article has been retracted, because it has become clear
CC that the thioredoxin that interacts in yeast 2-hybrid with the Cf-9 C-
CC terminus is in fact localized in the chloroplast, rendering a role in
CC Cf-9 signaling unlikely. All the authors agree that this paper should
CC be withdrawn from the scientific literature.
CC {ECO:0000305|PubMed:31310343}.
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DR EMBL; U15936; AAA65235.1; -; mRNA.
DR EMBL; AJ002236; CAA05274.1; -; Genomic_DNA.
DR AlphaFoldDB; Q40235; -.
DR SMR; Q40235; -.
DR IntAct; Q40235; 2.
DR MINT; Q40235; -.
DR KEGG; ag:AAA65235; -.
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 GO; GO:0002238; P:response to molecule of fungal origin; IEP: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; 1.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF08263; LRRNT_2; 1.
DR SMART; SM00369; LRR_TYP; 7.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Leucine-rich repeat; Membrane; Plant defense;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..863
FT /note="Receptor-like protein Cf-9"
FT /id="PRO_5007702783"
FT TOPO_DOM 22..812
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 813..833
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 834..863
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 92..115
FT /note="LRR 1; degenerate"
FT /evidence="ECO:0000305"
FT REPEAT 116..139
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 141..164
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 165..191
FT /note="LRR 4; degenerate"
FT /evidence="ECO:0000305"
FT REPEAT 192..214
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 215..238
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 241..263
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 265..287
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 288..312
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 314..335
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 336..358
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 359..382
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 383..406
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 408..428
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 429..452
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 454..476
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 477..500
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 502..524
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 525..549
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 551..572
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 573..597
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 599..623
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 667..690
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 691..714
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 715..739
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT REPEAT 741..759
FT /note="LRR 26"
FT /evidence="ECO:0000255"
FT REGION 24..91
FT /note="N-cap"
FT /evidence="ECO:0000305|PubMed:7973631,
FT ECO:0000305|PubMed:9413991"
FT REGION 760..812
FT /note="C-cap/acidic domain"
FT /evidence="ECO:0000305|PubMed:7973631,
FT ECO:0000305|PubMed:9413991"
FT SITE 674
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:15722474"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 698
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 714
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 767
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 71
FT /note="W->A: Abolishes resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15722474"
FT MUTAGEN 78
FT /note="C->A: Severely reduces resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15722474"
FT MUTAGEN 80
FT /note="W->A,T: Abolishes resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15722474"
FT MUTAGEN 85
FT /note="C->A: Severely reduces resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15722474"
FT MUTAGEN 191
FT /note="N->D: Abolishes resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15722474"
FT MUTAGEN 193
FT /note="T->A: Abolishes resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15722474"
FT MUTAGEN 262
FT /note="N->D: Abolishes resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15722474"
FT MUTAGEN 311
FT /note="N->D: Abolishes resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15722474"
FT MUTAGEN 313
FT /note="T->A: Abolishes resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15722474"
FT MUTAGEN 365
FT /note="D->N: Abolishes resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15166169,
FT ECO:0000269|PubMed:15722474"
FT MUTAGEN 380
FT /note="S->A: Abolishes resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15722474"
FT MUTAGEN 396
FT /note="N->D: Abolishes resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15722474"
FT MUTAGEN 457
FT /note="L->F: Abolishes resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15166169"
FT MUTAGEN 508
FT /note="D->N: Abolishes resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15166169,
FT ECO:0000269|PubMed:15722474"
FT MUTAGEN 676
FT /note="S->L: Abolishes resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15166169,
FT ECO:0000269|PubMed:15722474"
FT MUTAGEN 722
FT /note="D->N: Abolishes resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15722474"
FT MUTAGEN 825
FT /note="G->R: Abolishes resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15166169"
FT MUTAGEN 835
FT /note="T->D: Severely reduces resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15166169"
FT MUTAGEN 836
FT /note="Q->A: Reduces resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15166169"
FT MUTAGEN 838
FT /note="P->A: Reduces resistance to C.fulvum."
FT /evidence="ECO:0000269|PubMed:15166169"
SQ SEQUENCE 863 AA; 96570 MW; B2140DABD63E5FA7 CRC64;
MDCVKLVFLM LYTFLCQLAL SSSLPHLCPE DQALSLLQFK NMFTINPNAS DYCYDIRTYV
DIQSYPRTLS WNKSTSCCSW DGVHCDETTG QVIALDLRCS QLQGKFHSNS SLFQLSNLKR
LDLSFNNFTG SLISPKFGEF SNLTHLDLSH SSFTGLIPSE ICHLSKLHVL RICDQYGLSL
VPYNFELLLK NLTQLRELNL ESVNISSTIP SNFSSHLTTL QLSGTELHGI LPERVFHLSN
LQSLHLSVNP QLTVRFPTTK WNSSASLMTL YVDSVNIADR IPKSFSHLTS LHELYMGRCN
LSGPIPKPLW NLTNIVFLHL GDNHLEGPIS HFTIFEKLKR LSLVNNNFDG GLEFLSFNTQ
LERLDLSSNS LTGPIPSNIS GLQNLECLYL SSNHLNGSIP SWIFSLPSLV ELDLSNNTFS
GKIQEFKSKT LSAVTLKQNK LKGRIPNSLL NQKNLQLLLL SHNNISGHIS SAICNLKTLI
LLDLGSNNLE GTIPQCVVER NEYLSHLDLS KNRLSGTINT TFSVGNILRV ISLHGNKLTG
KVPRSMINCK YLTLLDLGNN MLNDTFPNWL GYLFQLKILS LRSNKLHGPI KSSGNTNLFM
GLQILDLSSN GFSGNLPERI LGNLQTMKEI DESTGFPEYI SDPYDIYYNY LTTISTKGQD
YDSVRILDSN MIINLSKNRF EGHIPSIIGD LVGLRTLNLS HNVLEGHIPA SFQNLSVLES
LDLSSNKISG EIPQQLASLT FLEVLNLSHN HLVGCIPKGK QFDSFGNTSY QGNDGLRGFP
LSKLCGGEDQ VTTPAELDQE EEEEDSPMIS WQGVLVGYGC GLVIGLSVIY IMWSTQYPAW
FSRMDLKLEH IITTKMKKHK KRY
