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RPS4W_ARATH
ID   RPS4W_ARATH             Reviewed;        1217 AA.
AC   C4B7M7;
DT   26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Disease resistance protein RPS4 {ECO:0000303|PubMed:19519800};
DE            EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE   AltName: Full=Resistance to Pseudomonas syringae 4 {ECO:0000303|PubMed:19519800};
GN   Name=RPS4 {ECO:0000303|PubMed:19519800};
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 {ECO:0000312|EMBL:BAH59426.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Wassilewskija;
RX   PubMed=19519800; DOI=10.1111/j.1365-313x.2009.03949.x;
RA   Narusaka M., Shirasu K., Noutoshi Y., Kubo Y., Shiraishi T., Iwabuchi M.,
RA   Narusaka Y.;
RT   "RRS1 and RPS4 provide a dual Resistance-gene system against fungal and
RT   bacterial pathogens.";
RL   Plant J. 60:218-226(2009).
RN   [2]
RP   FUNCTION, ALTERNATIVE SPLICING, AND INDUCTION BY AVRRPS4.
RC   STRAIN=cv. Columbia, cv. Landsberg erecta, and cv. Wassilewskija;
RX   PubMed=17951452; DOI=10.1104/pp.107.108720;
RA   Zhang X.C., Gassmann W.;
RT   "Alternative splicing and mRNA levels of the disease resistance gene RPS4
RT   are induced during defense responses.";
RL   Plant Physiol. 145:1577-1587(2007).
RN   [3]
RP   FUNCTION.
RX   PubMed=19826224; DOI=10.4161/psb.4.10.9640;
RA   Narusaka M., Kubo Y., Shiraishi T., Iwabuchi M., Narusaka Y.;
RT   "A dual resistance gene system prevents infection by three distinct
RT   pathogens.";
RL   Plant Signal. Behav. 4:954-955(2009).
RN   [4]
RP   FUNCTION.
RC   STRAIN=cv. Columbia, and cv. Wassilewskija;
RX   PubMed=24146667; DOI=10.3389/fpls.2013.00403;
RA   Heidrich K., Tsuda K., Blanvillain-Baufume S., Wirthmueller L., Bautor J.,
RA   Parker J.E.;
RT   "Arabidopsis TNL-WRKY domain receptor RRS1 contributes to temperature-
RT   conditioned RPS4 auto-immunity.";
RL   Front. Plant Sci. 4:403-403(2013).
CC   -!- FUNCTION: Disease resistance (R) protein that specifically recognizes
CC       the AvrRps4 type III effector avirulence protein from Pseudomonas
CC       syringae. Resistance proteins guard the plant against pathogens that
CC       contain an appropriate avirulence protein via an indirect interaction
CC       with this avirulence protein. That triggers a defense system including
CC       the hypersensitive response, which restricts the pathogen growth. The
CC       combined presence of both regular and alternative RPS4 transcripts with
CC       truncated open reading frames (ORFs) is necessary for function. RPS4
CC       function is regulated at multiple levels, including gene expression,
CC       alternative splicing, and protein stability. Acts as a disease
CC       resistance protein involved in resistance to fungal and bacterial
CC       pathogens, including R.solanacearum, P.syringae pv. tomato and
CC       C.higginsianum. In presence of RRS1, elicites an EDS1-dependent
CC       hypersensitive response (PubMed:24146667).
CC       {ECO:0000269|PubMed:17951452, ECO:0000269|PubMed:19519800,
CC       ECO:0000269|PubMed:19826224, ECO:0000269|PubMed:24146667}.
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 EDS1. {ECO:0000250|UniProtKB:Q9XGM3}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced.
CC         {ECO:0000269|PubMed:17951452};
CC       Name=1;
CC         IsoId=C4B7M7-1; Sequence=Displayed;
CC   -!- INDUCTION: Up-regulated by AvrRps4 in an EDS1-dependent manner.
CC       {ECO:0000269|PubMed:17951452}.
CC   -!- DOMAIN: The TIR domain is a signaling domain involved in cell death
CC       induction. {ECO:0000250|UniProtKB:Q9XGM3}.
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: Loss of resistance to C.higginsianum.
CC       {ECO:0000269|PubMed:19519800}.
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DR   EMBL; AB470473; BAH59426.1; -; mRNA.
DR   AlphaFoldDB; C4B7M7; -.
DR   SMR; C4B7M7; -.
DR   ExpressionAtlas; C4B7M7; baseline and differential.
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: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   Gene3D; 3.80.10.10; -; 2.
DR   InterPro; IPR042197; Apaf_helical.
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   2: Evidence at transcript level;
KW   Alternative splicing; Hydrolase; Leucine-rich repeat; NAD; Nucleus;
KW   Plant defense; Repeat.
FT   CHAIN           1..1217
FT                   /note="Disease resistance protein RPS4"
FT                   /id="PRO_0000431366"
FT   DOMAIN          14..175
FT                   /note="TIR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT   DOMAIN          211..472
FT                   /note="NB-ARC"
FT                   /evidence="ECO:0000255"
FT   REPEAT          260..285
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          436..459
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          614..636
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          637..659
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          682..706
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          708..728
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          729..749
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          750..774
FT                   /note="LRR 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          796..818
FT                   /note="LRR 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          819..842
FT                   /note="LRR 10"
FT                   /evidence="ECO:0000255"
FT   REPEAT          861..887
FT                   /note="LRR 11"
FT                   /evidence="ECO:0000255"
FT   REGION          1162..1195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1170..1177
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   ACT_SITE        88
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
SQ   SEQUENCE   1217 AA;  137745 MW;  9CAB2C913968EBA9 CRC64;
     METSSISTVE DKPPQHQVFI NFRGADLRRR FVSHLVTALK LNNINVFIDD YEDRGQPLDV
     LLKRIEESKI VLAIFSGNYT ESVWCVRELE KIKDCTDEGT LVAIPIFYKL EPSTVRDLKG
     KFGDRFRSMA KGDERKKKWK EAFNLIPNIM GITIDKKSVE SEKVNEIVKA VKTALTGIPP
     EGSHNAVVGA LGNSNAGTSS GDKKHETFGN EQRLKDLEEK LDRDKYKGTR IIGVVGMPGI
     GKTTLLKELY KTWQGKFSRH ALIDQIRVKS KHLELDRLPQ MLLGELSKLN NPHVDNLKDP
     YSQLHERKVL VVLDDVSKRE QIDALREILD WIKEGKEGSR VVIATSDMSL TNGLVDDTYM
     VQNLNHRDSL QLFHYHAFID DQANPQKKDF MKLSEGFVHY ARGHPLALKV LGGELNKKSM
     DHWNSKMKKL AQSPSPNIVS VFQVSYDELT TAQKDAFLDI ACFRSQDKDY VESLLASSDL
     GSAEAMSAVK SLTDKFLINT CDGRVEMHDL LYKFSREIDL KASNQDGSRQ RRLWLHQHII
     KGGIINVLQN KMKAANVRGI FLDLSEVEDE TSLDRDHFIN MGNLRYLKFY NSHCPQECKT
     NNKINIPDKL KLPLKEVRCL HWLKFPLETL PNDFNPINLV DLKLPYSEME QLWEGDKDTP
     CLRWVDLNHS SKLCSLSGLS KAEKLQRLNL EGCTTLKAFP HDMKKMKMLA FLNLKGCTSL
     ESLPEMNLIS LKTLTLSGCS TFKEFPLISD NIETLYLDGT AISQLPMNME KLQRLVVLNM
     KDCKMLEEIP GRVGELKALQ ELILSDCLNL KIFPEIDISF LNILLLDGTA IEVMPQLPSV
     QYLCLSRNAK ISCLPVGISQ LSQLKWLDLK YCTSLTSVPE FPPNLQCLDA HGCSSLKTVS
     KPLARIMPTE QNHSTFIFTN CENLEQAAKE EITSYAQRKC QLLSYARKRY NGGLVSESLF
     STCFPGCEVP SWFCHETVGS ELEVKLLPHW HDKKLAGIAL CAVVSCLDPQ DQVSRLSVTC
     TFKVKDEDKS WVPYTCPVGS WTRHGGGKDK IELDHVFIGY TSCPHTIKCH EEGNSDECNP
     TEASLKFTVT GGTSENGKYK VLKCGLSLVY AKDKDKNSAL ETKYDMLIGK SFQETSEGVD
     GRVKKTKGKY VMPVEKNFQE TTEGVDGRVK KKKKTRMDNG RPKKKQRSGR DDNQTRMQVE
     LQEGNINSVI MHTVKNF
 
 
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