CHS1_ARATH
ID CHS1_ARATH Reviewed; 420 AA.
AC F4I902; Q9LNP4;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Disease resistance protein CHS1 {ECO:0000303|PubMed:16667557};
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=Protein CHILLING SENSITIVE 1 {ECO:0000303|PubMed:16667557};
GN Name=CHS1 {ECO:0000303|PubMed:16667557};
GN OrderedLocusNames=At1g17610 {ECO:0000312|Araport:AT1G17610};
GN ORFNames=F1L3.31 {ECO:0000312|EMBL:AAF79471.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF ALA-10.
RC STRAIN=cv. Columbia;
RX PubMed=16667557; DOI=10.1104/pp.93.3.1053;
RA Hugly S., McCourt P., Browse J., Patterson G.W., Somerville C.;
RT "A chilling sensitive mutant of Arabidopsis with altered steryl-ester
RT metabolism.";
RL Plant Physiol. 93:1053-1062(1990).
RN [4]
RP GENE FAMILY.
RX PubMed=12366802; DOI=10.1046/j.1365-313x.2002.01404.x;
RA Meyers B.C., Morgante M., Michelmore R.W.;
RT "TIR-X and TIR-NBS proteins: two new families related to disease resistance
RT TIR-NBS-LRR proteins encoded in Arabidopsis and other plant genomes.";
RL Plant J. 32:77-92(2002).
RN [5]
RP MUTAGENESIS OF ALA-10.
RC STRAIN=cv. Columbia;
RX PubMed=10811971; DOI=10.1007/s002320001058;
RA Dordas C., Brown P.H.;
RT "Permeability of boric acid across lipid bilayers and factors affecting
RT it.";
RL J. Membr. Biol. 175:95-105(2000).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ALA-10, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=23617639; DOI=10.1111/tpj.12219;
RA Zbierzak A.M., Porfirova S., Griebel T., Melzer M., Parker J.E.,
RA Doermann P.;
RT "A TIR-NBS protein encoded by Arabidopsis CHILLING SENSITIVE 1 (CHS1)
RT limits chloroplast damage and cell death at low temperature.";
RL Plant J. 75:539-552(2013).
RN [7]
RP FUNCTION, MUTAGENESIS OF ALA-10, INDUCTION BY LOW TEMPERATURES, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=23651299; DOI=10.1111/tpj.12232;
RA Wang Y., Zhang Y., Wang Z., Zhang X., Yang S.;
RT "A missense mutation in CHS1, a TIR-NB protein, induces chilling
RT sensitivity in Arabidopsis.";
RL Plant J. 75:553-565(2013).
CC -!- FUNCTION: Confers resistance to low temperatures by limiting
CC chloroplast damage and cell death, thus maintaining growth homeostasis
CC (PubMed:16667557, PubMed:23617639, PubMed:23651299). Regulates steryl-
CC esters and sterols accumulation (PubMed:16667557). Limits leaf necrosis
CC associated with virulent bacterial infection (e.g. Pseudomonas syringae
CC pv. tomato DC3000) (PubMed:23617639). {ECO:0000269|PubMed:16667557,
CC ECO:0000269|PubMed:23617639, ECO:0000269|PubMed:23651299}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23617639,
CC ECO:0000269|PubMed:23651299}. Nucleus {ECO:0000269|PubMed:23651299}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves and flowers (mainly in
CC sepals), and, at a lower intensity, in stems (PubMed:23617639,
CC PubMed:23651299). Present at low levels in roots and seeds
CC (PubMed:23617639). {ECO:0000269|PubMed:23617639,
CC ECO:0000269|PubMed:23651299}.
CC -!- INDUCTION: Stabilized by low temperatures (at protein level).
CC {ECO:0000269|PubMed:23651299}.
CC -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
CC Self-association of TIR domains is required for NADase activity.
CC {ECO:0000255|PROSITE-ProRule:PRU00204}.
CC -!- DISRUPTION PHENOTYPE: RNAi lines display chilling sensitivity. Massive
CC necrotic response to virulent Pseudomonas syringae pv. tomato
CC infection, but normal bacterial proliferation.
CC {ECO:0000269|PubMed:23617639}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79471.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC022492; AAF79471.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29613.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59197.1; -; Genomic_DNA.
DR RefSeq; NP_001319029.1; NM_001332314.1.
DR RefSeq; NP_173204.1; NM_101623.4.
DR AlphaFoldDB; F4I902; -.
DR SMR; F4I902; -.
DR STRING; 3702.AT1G17610.1; -.
DR PaxDb; F4I902; -.
DR PRIDE; F4I902; -.
DR ProteomicsDB; 246965; -.
DR EnsemblPlants; AT1G17610.1; AT1G17610.1; AT1G17610.
DR EnsemblPlants; AT1G17610.2; AT1G17610.2; AT1G17610.
DR GeneID; 838337; -.
DR Gramene; AT1G17610.1; AT1G17610.1; AT1G17610.
DR Gramene; AT1G17610.2; AT1G17610.2; AT1G17610.
DR KEGG; ath:AT1G17610; -.
DR Araport; AT1G17610; -.
DR TAIR; locus:2007873; AT1G17610.
DR HOGENOM; CLU_001561_2_3_1; -.
DR InParanoid; F4I902; -.
DR OMA; HGTHRIK; -.
DR OrthoDB; 759253at2759; -.
DR PRO; PR:F4I902; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I902; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0046713; P:borate transport; IMP:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.8.430; -; 1.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR044974; Disease_R_plants.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR11017; PTHR11017; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF01582; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; NAD; Nucleus; Plant defense; Reference proteome.
FT CHAIN 1..420
FT /note="Disease resistance protein CHS1"
FT /id="PRO_0000438137"
FT DOMAIN 12..167
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 185..406
FT /note="NB-ARC"
FT /evidence="ECO:0000255"
FT ACT_SITE 86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT MUTAGEN 10
FT /note="A->T: In chs1-1 and chs1-2; Increased leaves
FT sensitivity to chilling stress in an EDS1- and PAD4-
FT dependent manner, killed by several days of exposure to
FT temperatures below 18 degrees Celsius. Alterations in
FT photosynthetic complexes, chloroplast ultrastructure, and
FT thylakoid membrane integrity and lipid composition precede
FT leaf cell death. Leaf chlorosis and electrolyte leakage
FT after exposure to chilling temperatures associated with
FT abnormal steryl-esters accumulation and reduced sterols
FT levels. Chilling leads to xanthophyll cycle activation and
FT accumulation of tocopherol. Activation of immune responses
FT by chilling; increased salicylic acid (SA) and hydrogen
FT peroxide H(2)O(2) production, extensive cell death and
FT pathogenesis-related (PR) genes expression at 13 degrees
FT Celsius. Massive necrotic response to virulent Pseudomonas
FT syringae pv. tomato infection, but normal bacterial
FT proliferation. Increased permeability to boric acid."
FT /evidence="ECO:0000269|PubMed:10811971,
FT ECO:0000269|PubMed:16667557, ECO:0000269|PubMed:23617639,
FT ECO:0000269|PubMed:23651299"
SQ SEQUENCE 420 AA; 47577 MW; 1E3491567279750C CRC64;
MSTSYSFLLA GRELDVFLSF SGKIALDVDF GYDLSRNGIK AFKSESWKES SFKPIDLRTL
EALTESKVAV VMTSDEEVSS VGFLEELIVI IEFQEKRSLT VIPVFLTKHP LDVEKVSQIF
PERAKIWRTA IAKLDNIAAQ YSFSRNLAVM HGTHRIKQIA DDIRLMFLSS ASSDFKGLAG
MDRHMKALYA LLALESDEKV RTIGIWGSSG VGKTTLARYT YAEISVKFQA HVFLENVENM
KEMLLPSENF EGEDLRSVNH EMNEMAEAKQ KHRKVLLIAD GVNNIEQGKW IAENANWFAP
GSRVILITQE KSLLVQSGVN HVYEVGSLRY DEALQLFSRF AFKQPYPSPD FERLSVRAVQ
LAGFLPVTIR LFGSFLTGRD KEEWEATLLK LNAKQGKDIK EVWKIMEALE DKDIVEASQR
