DSC1_ARATH
ID DSC1_ARATH Reviewed; 1219 AA.
AC Q9SZ66; Q680A4;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Disease resistance-like protein DSC1 {ECO:0000305};
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=Protein DOMINANT SUPPRESSOR OF CAMTA3 NUMBER 1 {ECO:0000303|PubMed:28407487};
GN Name=DSC1 {ECO:0000303|PubMed:28407487};
GN OrderedLocusNames=At4g12010 {ECO:0000312|Araport:AT4G12010};
GN ORFNames=F16J13.80 {ECO:0000312|EMBL:CAB40942.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-536.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, INTERACTION WITH CAMTA3 AND DSC2, AND MUTAGENESIS OF
RP 221-GLY-LYS-222.
RX PubMed=28407487; DOI=10.1016/j.chom.2017.03.005;
RA Lolle S., Greeff C., Petersen K., Roux M., Jensen M.K., Bressendorff S.,
RA Rodriguez E., Soemark K., Mundy J., Petersen M.;
RT "Matching NLR immune receptors to autoimmunity in camta3 mutants using
RT antimorphic NLR alleles.";
RL Cell Host Microbe 21:518-529(2017).
CC -!- FUNCTION: TIR-NB-LRR receptor-like protein involved in plant defense.
CC Acts as a trigger of hypersensitive response (HR). Functions as guard
CC of CAMTA3, a negative regulator of immunity, during pathogen infection.
CC {ECO:0000269|PubMed:28407487}.
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 -!- SUBUNIT: Interacts with CAMTA3 and DSC2. {ECO:0000269|PubMed:28407487}.
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 -!- SIMILARITY: Belongs to the disease resistance NB-LRR family.
CC {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; AL049638; CAB40942.1; -; Genomic_DNA.
DR EMBL; AL161533; CAB78244.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83083.1; -; Genomic_DNA.
DR EMBL; AK175839; BAD43602.1; -; mRNA.
DR EMBL; AK175963; BAD43726.1; -; mRNA.
DR PIR; T06608; T06608.
DR RefSeq; NP_192938.1; NM_117271.3.
DR AlphaFoldDB; Q9SZ66; -.
DR SMR; Q9SZ66; -.
DR STRING; 3702.AT4G12010.1; -.
DR iPTMnet; Q9SZ66; -.
DR PaxDb; Q9SZ66; -.
DR PRIDE; Q9SZ66; -.
DR ProteomicsDB; 224293; -.
DR EnsemblPlants; AT4G12010.1; AT4G12010.1; AT4G12010.
DR GeneID; 826809; -.
DR Gramene; AT4G12010.1; AT4G12010.1; AT4G12010.
DR KEGG; ath:AT4G12010; -.
DR Araport; AT4G12010; -.
DR TAIR; locus:2118106; AT4G12010.
DR eggNOG; ENOG502SI7S; Eukaryota.
DR HOGENOM; CLU_001561_0_1_1; -.
DR InParanoid; Q9SZ66; -.
DR OMA; TEMPNIK; -.
DR OrthoDB; 98974at2759; -.
DR PhylomeDB; Q9SZ66; -.
DR PRO; PR:Q9SZ66; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZ66; baseline and differential.
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:UniProtKB.
DR GO; GO:0009626; P:plant-type hypersensitive 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 Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR045344; C-JID.
DR InterPro; IPR044974; Disease_R_plants.
DR InterPro; IPR001611; Leu-rich_rpt.
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 InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11017; PTHR11017; 1.
DR Pfam; PF20160; C-JID; 1.
DR Pfam; PF07725; LRR_3; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51450; LRR; 5.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Hypersensitive response; Leucine-rich repeat; NAD;
KW Nucleotide-binding; Plant defense; Reference proteome; Repeat.
FT CHAIN 1..1219
FT /note="Disease resistance-like protein DSC1"
FT /id="PRO_0000442293"
FT DOMAIN 9..176
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 197..446
FT /note="NB-ARC"
FT /evidence="ECO:0000255"
FT REPEAT 468..493
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 538..563
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 597..619
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 620..642
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 665..689
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 690..713
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 733..757
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 759..780
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 804..827
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 854..877
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 878..899
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT ACT_SITE 83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT BINDING 216..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 221..222
FT /note="GK->AA: Loss of function."
FT /evidence="ECO:0000269|PubMed:28407487"
SQ SEQUENCE 1219 AA; 138416 MW; B7AF08DE3653E31D CRC64;
MESSSPSSAE FDVFLSFRGF DTRNNFTGHL QKALRLRGID SFIDDRLRRG DNLTALFDRI
EKSKIAIIVF STNYANSAWC LRELVKILEC RNSNQQLVVP IFYKVDKSDV EKQRNSFAVP
FKLPELTFPG VTPEEISSWK AALASASNIL GYVVKEISTS EAKLVDEIAV DTFKKLNDLA
PSGNEGLVGI ESRLKNLEKL LSWEDLDTVH IIGIVGMVGI GKTTLADCLY GRMRGQFDGS
CFLTNIRENS GRSGLESLLQ KLFSTVLNDR DLEIGAPGNA HERFERRLKS KRLLIVLDDV
NDEKQIRYLM GHCKWYQGGS RIIITTRDSK LIETIKGRKY VLPKLNDREA LKLFSLNAFS
NSFPLKEFEG LTNMVLDYAK GHPLALKVLG SDLCERDDLY WEAKLDRLKS RSHGDIYEVL
ETSYEELTTE QKNVFLDIAC FFRSENVDYV TSLLNSHGVD VSGVVKDLVD KCLITLSDNR
IEMHDMLQTM AKEISLKVET IGIRDCRWLS RHGNQCQWHI RLWDSEDICD LLTEGLGTDK
IRGIFLDTSK LRAMRLSAKA FQGMYNLKYL KIYDSHCSRG CEAEFKLHLR RGLSFLPNEL
TYLHWHGYPL QSIPLDFDPK NLVDLKLPHS QLEEIWDDEK DVGMLKWVDL SHSINLRQCL
GLANAHNLER LNLEGCTSLK KLPSTINCLE KLIYLNLRDC TSLRSLPKGI KTQSLQTLIL
SGCSSLKKFP LISENVEVLL LDGTVIKSLP ESIQTFRRLA LLNLKNCKKL KHLSSDLYKL
KCLQELILSG CSQLEVFPEI KEDMESLEIL LMDDTSITEM PKMMHLSNIK TFSLCGTSSH
VSVSMFFMPP TLGCSRLTDL YLSRCSLYKL PDNIGGLSSL QSLCLSGNNI ENLPESFNQL
NNLKWFDLKF CKMLKSLPVL PQNLQYLDAH ECESLETLAN PLTPLTVGER IHSMFIFSNC
YKLNQDAQAS LVGHARIKSQ LMANASAKRY YRGFVPEPLV GICYPATEIP SWFCHQRLGR
SLEIPLPPHW CDINFVGLAL SVVVSFKDYE DSAKRFSVKC CGNFENKDSS FTRFDFTLAG
WNEPCGSLSH ESRKLTSDHV FMGYNSCFLV KNVHGESNSC CYTKASFEFY VTDDETRKKI
ETCEVIKCGM SLMYVPEDDD CMLLKKTNIV QLSLKSGPSC SYDLDDVMDD VRPKRGLCQF
VGGEEPGCKR RKEEKITVR
