DSC2_ARATH
ID DSC2_ARATH Reviewed; 1210 AA.
AC F4JWM0;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Disease resistance-like protein DSC2 {ECO:0000305};
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=Protein DOMINANT SUPRESSOR OF CAMTA3 NUMBER 2 {ECO:0000303|PubMed:28407487};
GN Name=DSC2 {ECO:0000303|PubMed:28407487};
GN OrderedLocusNames=At5g18370 {ECO:0000312|Araport:AT5G18370};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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, INTERACTION WITH DSC1, AND MUTAGENESIS OF 267-GLY-LYS-268.
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 DSC1. {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}.
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DR EMBL; AC051626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92545.1; -; Genomic_DNA.
DR RefSeq; NP_001318593.1; NM_001343545.1.
DR AlphaFoldDB; F4JWM0; -.
DR SMR; F4JWM0; -.
DR STRING; 3702.AT5G18370.1; -.
DR PaxDb; F4JWM0; -.
DR PRIDE; F4JWM0; -.
DR EnsemblPlants; AT5G18370.1; AT5G18370.1; AT5G18370.
DR GeneID; 831955; -.
DR Gramene; AT5G18370.1; AT5G18370.1; AT5G18370.
DR KEGG; ath:AT5G18370; -.
DR Araport; AT5G18370; -.
DR TAIR; locus:2146253; AT5G18370.
DR eggNOG; ENOG502SUNR; Eukaryota.
DR HOGENOM; CLU_001561_0_1_1; -.
DR InParanoid; F4JWM0; -.
DR OMA; MAKETQW; -.
DR OrthoDB; 1085197at2759; -.
DR PhylomeDB; F4JWM0; -.
DR PRO; PR:F4JWM0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4JWM0; 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; IPR003593; AAA+_ATPase.
DR InterPro; IPR042197; Apaf_helical.
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 InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11017; PTHR11017; 1.
DR Pfam; PF07725; LRR_3; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
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..1210
FT /note="Disease resistance-like protein DSC2"
FT /id="PRO_0000442294"
FT DOMAIN 59..223
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 241..511
FT /note="NB-ARC"
FT /evidence="ECO:0000255"
FT REPEAT 662..685
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 686..709
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 711..732
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 756..780
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 783..804
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 805..828
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 830..848
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 849..873
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 940..970
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT ACT_SITE 134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT MUTAGEN 267..268
FT /note="GK->AA: Loss of function."
FT /evidence="ECO:0000269|PubMed:28407487"
SQ SEQUENCE 1210 AA; 137786 MW; A2412556A6565B23 CRC64;
MAIAEVIGFF TLVCVIWYWV YKKHKNLQLK ICRSSIESSS SSSSLSSPPS LSSPISRTWT
HQVFPSFRGE DVRKGFLSHI QKEFKSKGIV PFIDDEMKRG ESIGPGLFQA IRESKIAIVL
LSKNYASSSW CLNELVEIMN CREEIGQTVM TVFYQVDPSD VRKQTGDFGK AFKKTCVGKT
QEVKQRWSRA LMDVANILGQ DSRKWDKEAD MIVKVAKDVS DVLSYTPSRD FDDYVGIRPH
ITRINSLLCL ESSDVRMIGI LGPPGIGKTT IARVLYDQIS EKFQFSAFIE NIRLSYWKGW
HDEGNLDFPV EIMTGDRQRK LNLQRRLLSE LFNQKDIQVR HLGAVQERLR DHKVLVILDG
VDQLEQLTAL AKETQWFGYG SRIIITTQDQ RLLRAHEINH VYKVDLPATD EALQIFCLYA
FGQKFPYDGF KKLAREFTAL AGELPLGLRV LGSYLRGMSL EEWKNALPRL RTSLDGEIEK
TLRFAYNVLS DKDKSLFLHI ACLFNGCQVN HVKQWLANSS LDVNHGFEVL SNKSLISTDM
GLVRMHSLLQ QLGVDIVRKQ SIGEPEKRQF LVDVNEISDV ITDNTGTGTI LGIMLHVSKI
EDVLVIEETV FDRMTNLQFL ILDECLRDKL NLPLGLNCLP RKIRLLRWDY CPLSIWPSKF
SAKFLVELIM RANKFEKLWE GIQPLKNLKR MELGDARNLK EIPDLSNATN LESLLLSFCT
SLLEIPSSIR GTTNLKELDL GGCASLVKLS SCICNATSLE ELNLSACSNL VELPCALPGD
SNMRSLSKLL LNGSSRLKTF PEISTNIQEL NLSGTAIEEV PSSIRLWSRL DKLDMSRCKN
LKMFPPVPDG ISVLNLSETE IEDIPPWVEN LSQLRHFVMI RCKKLDNISL SRISKMEGVH
CLQITRGDED VSGDSIVNIR WYSNFPNQWT LQSDMLQICL PELVYTSPVS LHFISNEFKT
IPDCIKNLSQ LHQLSFYRCH KLVSLPQLSD CLSSLDAENC VSLETIDGSF HNPDIRLNFL
NCNNLNQEAR ELIQKSVCKH ALLPSGEVPA YFIHRAIGDS VTIHLKERHL PLYLIFKASL
VLFNDDEINY DYDDDDDDDY DEEVIVYGDY DSYPHSDDYT KQETMRLSCR VEGKQNGLTI
QYGSSVHLLP TPHRYTEHVY IFEASFSLGE CNSPEAESEL VFDFKVHDYF WAIKECGLRL
LELPHAHGDD
