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Receptor-like protein Cf-9

 CF9_SOLPI               Reviewed;         863 AA.
Q40235;
31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-FEB-2018, entry version 88.
RecName: Full=Receptor-like protein Cf-9 {ECO:0000305};
Flags: Precursor;
Name=CF-9 {ECO:0000312|EMBL:AAA65235.1, ECO:0000312|EMBL:CAA05274.1};
Solanum pimpinellifolium (Currant tomato) (Lycopersicon
pimpinellifolium).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae;
Solaneae; Solanum; Lycopersicon.
NCBI_TaxID=4084;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=cv. Cf9;
PubMed=7973631; DOI=10.1126/science.7973631;
Jones D.A., Thomas C.M., Hammond-Kosack K.E., Balint-Kurti P.J.,
Jones J.D.;
"Isolation of the tomato Cf-9 gene for resistance to Cladosporium
fulvum by transposon tagging.";
Science 266:789-793(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=cv. Cf9;
PubMed=9413991; DOI=10.1016/S0092-8674(00)80470-5;
Parniske M., Hammond-Kosack K.E., Golstein C., Thomas C.M.,
Jones D.A., Harrison K., Wulff B.B., Jones J.D.;
"Novel disease resistance specificities result from sequence exchange
between tandemly repeated genes at the Cf-4/9 locus of tomato.";
Cell 91:821-832(1997).
[3]
DOMAIN.
PubMed=11226184;
Wulff B.B., Thomas C.M., Smoker M., Grant M., Jones J.D.;
"Domain swapping and gene shuffling identify sequences required for
induction of an Avr-dependent hypersensitive response by the tomato
Cf-4 and Cf-9 proteins.";
Plant Cell 13:255-272(2001).
[4]
FUNCTION.
PubMed=11517316; DOI=10.1073/pnas.181241798;
Van Der Hoorn R.A.L., Kruijt M., Roth R., Brandwagt B.F.,
Joosten M.H.A.J., De Wit P.J.G.M.;
"Intragenic recombination generated two distinct Cf genes that mediate
AVR9 recognition in the natural population of Lycopersicon
pimpinellifolium.";
Proc. Natl. Acad. Sci. U.S.A. 98:10493-10498(2001).
[5]
INTERACTS WITH CITRX.
PubMed=15131698; DOI=10.1038/sj.emboj.7600224;
Rivas S., Rougon-Cardoso A., Smoker M., Schauser L., Yoshioka H.,
Jones J.D.;
"CITRX thioredoxin interacts with the tomato Cf-9 resistance protein
and negatively regulates defence.";
EMBO J. 23:2156-2165(2004).
[6]
MUTAGENESIS OF ASP-365; LEU-457; ASP-508; SER-676 AND GLY-825.
PubMed=15166169;
Wulff B.B., Thomas C.M., Parniske M., Jones J.D.;
"Genetic variation at the tomato Cf-4/Cf-9 locus induced by EMS
mutagenesis and intralocus recombination.";
Genetics 167:459-470(2004).
[7]
MUTAGENESIS OF TRP-71; CYS-78; TRP-80; CYS-85; ASN-191; THR-193;
ASN-262; ASN-311; THR-313; ASP-365; SER-380; ASN-396; ASP-508; SER-676
AND ASP-722, IDENTIFICATION BY MASS SPECTROMETRY, AND LACK OF
GLYCOSYLATION AT ASN-674.
PubMed=15722474; DOI=10.1105/tpc.104.028118;
van der Hoorn R.A., Wulff B.B., Rivas S., Durrant M.C.,
van der Ploeg A., de Wit P.J., Jones J.D.;
"Structure-function analysis of cf-9, a receptor-like protein with
extracytoplasmic leucine-rich repeats.";
Plant Cell 17:1000-1015(2005).
[8]
INDUCTION BY AVR9, AND REGULATION BY SLY-MIR6022.
PubMed=26768363; DOI=10.1016/j.bbrc.2016.01.015;
Li W., Xu Y.P., Cai X.Z.;
"Transcriptional and posttranscriptional regulation of the tomato leaf
mould disease resistance gene Cf-9.";
Biochem. Biophys. Res. Commun. 470:163-167(2016).
[9]
MUTAGENESIS OF THR-835; GLN-836 AND PRO-838, AND INTERACTION WITH
CITRX.
PubMed=26315781; DOI=10.1111/mpp.12315;
Chakrabarti A., Velusamy T., Tee C.Y., Jones D.A.;
"A mutational analysis of the cytosolic domain of the tomato Cf-9
disease-resistance protein shows that membrane-proximal residues are
important for Avr9-dependent necrosis.";
Mol. Plant Pathol. 17:565-576(2016).
-!- FUNCTION: Involved in plant defense. Confers resistance to the
fungal pathogen C.fulvum through recognition of the AVR9 elicitor
protein. {ECO:0000269|PubMed:11517316, ECO:0000269|PubMed:7973631,
ECO:0000269|PubMed:9413991}.
-!- SUBUNIT: Interacts with thioredoxin-like protein CITRX.
{ECO:0000269|PubMed:15131698, ECO:0000269|PubMed:26315781}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
type I membrane protein {ECO:0000305}.
-!- INDUCTION: Induced by C.fulvum AVR9 elicitor protein in a
temperature-sensitive manner. Repressed by sly-miR6022.
{ECO:0000269|PubMed:26768363}.
-!- DOMAIN: The extracellular leucine-rich repeats are required for
the specificity of the elicitor protein recognition. Important
sequence determinants of Cf-9 function are located in LRRs 10 to
18. {ECO:0000269|PubMed:11226184}.
-!- SIMILARITY: Belongs to the RLP family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U15936; AAA65235.1; -; mRNA.
EMBL; AJ002236; CAA05274.1; -; Genomic_DNA.
ProteinModelPortal; Q40235; -.
IntAct; Q40235; 2.
MINT; Q40235; -.
KEGG; ag:AAA65235; -.
KO; K13446; -.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
GO; GO:0002238; P:response to molecule of fungal origin; IEP:UniProtKB.
Gene3D; 3.80.10.10; -; 2.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR013210; LRR_N_plant-typ.
Pfam; PF00560; LRR_1; 1.
Pfam; PF13516; LRR_6; 1.
Pfam; PF13855; LRR_8; 4.
Pfam; PF08263; LRRNT_2; 1.
SMART; SM00369; LRR_TYP; 7.
1: Evidence at protein level;
Cell membrane; Glycoprotein; Leucine-rich repeat; Membrane;
Plant defense; Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 863 Receptor-like protein Cf-9.
/FTId=PRO_5007702783.
TOPO_DOM 22 812 Extracellular. {ECO:0000255}.
TRANSMEM 813 833 Helical. {ECO:0000255}.
TOPO_DOM 834 863 Cytoplasmic. {ECO:0000255}.
REPEAT 92 115 LRR 1; degenerate. {ECO:0000305}.
REPEAT 116 139 LRR 2. {ECO:0000255}.
REPEAT 141 164 LRR 3. {ECO:0000255}.
REPEAT 165 191 LRR 4; degenerate. {ECO:0000305}.
REPEAT 192 214 LRR 5. {ECO:0000255}.
REPEAT 215 238 LRR 6. {ECO:0000255}.
REPEAT 241 263 LRR 7. {ECO:0000255}.
REPEAT 265 287 LRR 8. {ECO:0000255}.
REPEAT 288 312 LRR 9. {ECO:0000255}.
REPEAT 314 335 LRR 10. {ECO:0000255}.
REPEAT 336 358 LRR 11. {ECO:0000255}.
REPEAT 359 382 LRR 12. {ECO:0000255}.
REPEAT 383 406 LRR 13. {ECO:0000255}.
REPEAT 408 428 LRR 14. {ECO:0000255}.
REPEAT 429 452 LRR 15. {ECO:0000255}.
REPEAT 454 476 LRR 16. {ECO:0000255}.
REPEAT 477 500 LRR 17. {ECO:0000255}.
REPEAT 502 524 LRR 18. {ECO:0000255}.
REPEAT 525 549 LRR 19. {ECO:0000255}.
REPEAT 551 572 LRR 20. {ECO:0000255}.
REPEAT 573 597 LRR 21. {ECO:0000255}.
REPEAT 599 623 LRR 22. {ECO:0000255}.
REPEAT 667 690 LRR 23. {ECO:0000255}.
REPEAT 691 714 LRR 24. {ECO:0000255}.
REPEAT 715 739 LRR 25. {ECO:0000255}.
REPEAT 741 759 LRR 26. {ECO:0000255}.
REGION 24 91 N-cap. {ECO:0000305|PubMed:7973631,
ECO:0000305|PubMed:9413991}.
REGION 760 812 C-cap/acidic domain.
{ECO:0000305|PubMed:7973631,
ECO:0000305|PubMed:9413991}.
SITE 674 674 Not glycosylated.
{ECO:0000269|PubMed:15722474}.
CARBOHYD 48 48 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 72 72 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 109 109 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 127 127 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 142 142 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 191 191 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 204 204 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 212 212 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 262 262 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 300 300 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 311 311 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 378 378 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 396 396 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 416 416 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 464 464 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 519 519 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 563 563 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 698 698 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 714 714 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 746 746 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 767 767 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
MUTAGEN 71 71 W->A: Abolishes resistance to C.fulvum.
{ECO:0000269|PubMed:15722474}.
MUTAGEN 78 78 C->A: Severely reduces resistance to
C.fulvum. {ECO:0000269|PubMed:15722474}.
MUTAGEN 80 80 W->A,T: Abolishes resistance to C.fulvum.
{ECO:0000269|PubMed:15722474}.
MUTAGEN 85 85 C->A: Severely reduces resistance to
C.fulvum. {ECO:0000269|PubMed:15722474}.
MUTAGEN 191 191 N->D: Abolishes resistance to C.fulvum.
{ECO:0000269|PubMed:15722474}.
MUTAGEN 193 193 T->A: Abolishes resistance to C.fulvum.
{ECO:0000269|PubMed:15722474}.
MUTAGEN 262 262 N->D: Abolishes resistance to C.fulvum.
{ECO:0000269|PubMed:15722474}.
MUTAGEN 311 311 N->D: Abolishes resistance to C.fulvum.
{ECO:0000269|PubMed:15722474}.
MUTAGEN 313 313 T->A: Abolishes resistance to C.fulvum.
{ECO:0000269|PubMed:15722474}.
MUTAGEN 365 365 D->N: Abolishes resistance to C.fulvum.
{ECO:0000269|PubMed:15166169,
ECO:0000269|PubMed:15722474}.
MUTAGEN 380 380 S->A: Abolishes resistance to C.fulvum.
{ECO:0000269|PubMed:15722474}.
MUTAGEN 396 396 N->D: Abolishes resistance to C.fulvum.
{ECO:0000269|PubMed:15722474}.
MUTAGEN 457 457 L->F: Abolishes resistance to C.fulvum.
{ECO:0000269|PubMed:15166169}.
MUTAGEN 508 508 D->N: Abolishes resistance to C.fulvum.
{ECO:0000269|PubMed:15166169,
ECO:0000269|PubMed:15722474}.
MUTAGEN 676 676 S->L: Abolishes resistance to C.fulvum.
{ECO:0000269|PubMed:15166169,
ECO:0000269|PubMed:15722474}.
MUTAGEN 722 722 D->N: Abolishes resistance to C.fulvum.
{ECO:0000269|PubMed:15722474}.
MUTAGEN 825 825 G->R: Abolishes resistance to C.fulvum.
{ECO:0000269|PubMed:15166169}.
MUTAGEN 835 835 T->D: Severely reduces resistance to
C.fulvum. {ECO:0000269|PubMed:15166169}.
MUTAGEN 836 836 Q->A: Reduces resistance to C.fulvum.
{ECO:0000269|PubMed:15166169}.
MUTAGEN 838 838 P->A: Reduces resistance to C.fulvum.
{ECO:0000269|PubMed:15166169}.
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


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