CSA1_ARATH
ID CSA1_ARATH Reviewed; 1197 AA.
AC F4KIF3; Q9FKN9;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Disease resistance-like protein CSA1 {ECO:0000305};
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=Protein CONSTITUTIVE SHADE-AVOIDANCE 1 {ECO:0000303|PubMed:17114357};
GN Name=CSA1 {ECO:0000303|PubMed:17114357};
GN OrderedLocusNames=At5g17880 {ECO:0000312|Araport:AT5G17880};
GN ORFNames=MPI7.4 {ECO:0000312|EMBL:BAB11221.1};
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 DISRUPTION PHENOTYPE.
RX PubMed=17114357; DOI=10.1105/tpc.105.038810;
RA Faigon-Soverna A., Harmon F.G., Storani L., Karayekov E., Staneloni R.J.,
RA Gassmann W., Mas P., Casal J.J., Kay S.A., Yanovsky M.J.;
RT "A constitutive shade-avoidance mutant implicates TIR-NBS-LRR proteins in
RT Arabidopsis photomorphogenic development.";
RL Plant Cell 18:2919-2928(2006).
CC -!- FUNCTION: TIR-NB-LRR receptor-like protein that functions in
CC photomorphogenic development. May function downstream of phytochrome B
CC (phyB) signaling. {ECO:0000269|PubMed:17114357}.
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 -!- 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: Shade avoidance phenotype in the absence of shade
CC and enhanced growth of the bacterial pathogen P.syringae pv. tomato
CC DC3000 (avirulent avrRpt2 strain). The constitutive shade avoidance
CC phenotype can be rescued by RPS4, a TIR-NBS-LRR protein that confers
CC resistance against bacterium Pseudomonas syringae.
CC {ECO:0000269|PubMed:17114357}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11221.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB011480; BAB11221.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92481.1; -; Genomic_DNA.
DR RefSeq; NP_197290.1; NM_121794.2.
DR AlphaFoldDB; F4KIF3; -.
DR SMR; F4KIF3; -.
DR STRING; 3702.AT5G17880.1; -.
DR iPTMnet; F4KIF3; -.
DR PaxDb; F4KIF3; -.
DR PRIDE; F4KIF3; -.
DR ProteomicsDB; 222765; -.
DR EnsemblPlants; AT5G17880.1; AT5G17880.1; AT5G17880.
DR GeneID; 831656; -.
DR Gramene; AT5G17880.1; AT5G17880.1; AT5G17880.
DR KEGG; ath:AT5G17880; -.
DR Araport; AT5G17880; -.
DR TAIR; locus:2170333; AT5G17880.
DR eggNOG; ENOG502SI7S; Eukaryota.
DR HOGENOM; CLU_001561_0_3_1; -.
DR InParanoid; F4KIF3; -.
DR OrthoDB; 79598at2759; -.
DR PRO; PR:F4KIF3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KIF3; baseline and differential.
DR Genevisible; F4KIF3; AT.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IMP:TAIR.
DR GO; GO:0010114; P:response to red light; IMP:TAIR.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR045344; C-JID.
DR InterPro; IPR044974; Disease_R_plants.
DR InterPro; IPR011713; Leu-rich_rpt_3.
DR InterPro; IPR032675; LRR_dom_sf.
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; PF20160; C-JID; 1.
DR Pfam; PF07725; LRR_3; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50104; TIR; 1.
PE 3: Inferred from homology;
KW ATP-binding; Developmental protein; Hydrolase; Leucine-rich repeat; NAD;
KW Nucleotide-binding; Plant defense; Reference proteome; Repeat.
FT CHAIN 1..1197
FT /note="Disease resistance-like protein CSA1"
FT /id="PRO_0000433382"
FT DOMAIN 15..178
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 210..480
FT /note="NB-ARC"
FT /evidence="ECO:0000255"
FT REPEAT 614..636
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 638..659
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 694..716
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 728..749
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 750..774
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 776..796
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 797..819
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 820..843
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 845..862
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 863..889
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT ACT_SITE 89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
SQ SEQUENCE 1197 AA; 135859 MW; 30D07B1DC53B0872 CRC64;
MTSSSSWVKT DGETPQDQVF INFRGVELRK NFVSHLEKGL KRKGINAFID TDEEMGQELS
VLLERIEGSR IALAIFSPRY TESKWCLKEL AKMKERTEQK ELVVIPIFYK VQPVTVKELK
GDFGDKFREL VKSTDKKTKK EWKEALQYVP FLTGIVLDEK SDEDEVINII IRKVKEILNR
RSEGPPSKCS ALPPQRHQKR HETFWGIELR IKQLEEKLRF GSDETTRTIG VVGMPGIGKT
TLATMLYEKW NDRFLRHVLI RDIHEASEED GLNYLATKFL QGLLKVENAN IESVQAAHEA
YKDQLLETKV LVILDNVSNK DQVDALLGER NWIKKGSKIL ITTSDKSLMI QSLVNDTYEV
PPLSDKDAIK HFIRYAFDGN EGAAPGPGQG NFPKLSKDFV HYTKGNPLAL QMLGKELLGK
DESHWGLKLN ALDQHHNSPP GQSICKMLQR VWEGSYKALS QKEKDALLDI ACFRSQDENY
VASLLDSDGP SNILEDLVNK FMINIYAGKV DMHDTLYMLS KELGREATAT DRKGRHRLWH
HHTIIAVLDK NKGGSNIRSI FLDLSDITRK WCFYRHAFAM MRDLRYLKIY STHCPQECES
DIKLNFPEGL LLPLNEVRYL HWLKFPLKEV PQDFNPGNLV DLKLPYSEIE RVWEDNKDAP
KLKWVNLNHS KKLNTLAGLG KAQNLQELNL EGCTALKEMH VDMENMKFLV FLNLRGCTSL
KSLPEIQLIS LKTLILSGCS KFKTFQVISD KLEALYLDGT AIKELPCDIG RLQRLVMLNM
KGCKKLKRLP DSLGQLKALE ELILSGCSKL NEFPETWGNM SRLEILLLDE TAIKDMPKIL
SVRRLCLNKN EKISRLPDLL NKFSQLQWLH LKYCKNLTHV PQLPPNLQYL NVHGCSSLKT
VAKPLVCSIP MKHVNSSFIF TNCNELEQAA KEEIVVYAER KCHLLASALK RCDESCVPEI
LFCTSFPGCE MPSWFSHDAI GSMVEFELPP HWNHNRLSGI ALCVVVSFKN CKSHANLIVK
FSCEQNNGEG SSSSITWKVG SLIEQDNQEE TVESDHVFIG YTNCLDFIKL VKGQGGPKCA
PTKASLEFSV RTGTGGEATL EVLKSGFSFV FEPEENRVPS PRNDDVKGKV KINKTPSANG
CFKDQAKGNE SPKGQWQTYI ENSSTNIPSE AHSSQKTGFN GFNGMYSVCV LYEMYSH
