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RPS4L_ARATH
ID   RPS4L_ARATH             Reviewed;        1217 AA.
AC   Q9SCX6;
DT   26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Disease resistance protein RPS4 {ECO:0000303|PubMed:10571887};
DE            EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE   AltName: Full=Resistance to Pseudomonas syringae 4 {ECO:0000303|PubMed:10571887};
GN   Name=RPS4 {ECO:0000303|PubMed:10571887};
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:CAB53785.1};
RN   [1] {ECO:0000312|EMBL:CAB53785.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=10571887; DOI=10.1046/j.1365-313x.1999.t01-1-00600.x;
RA   Gassmann W., Hinsch M.E., Staskawicz B.J.;
RT   "The Arabidopsis RPS4 bacterial-resistance gene is a member of the TIR-NBS-
RT   LRR family of disease-resistance genes.";
RL   Plant J. 20:265-277(1999).
RN   [2]
RP   FUNCTION, ALTERNATIVE SPLICING, AND MUTAGENESIS OF ASN-195 AND TYR-950.
RX   PubMed=14523247; DOI=10.1105/tpc013474;
RA   Zhang X.C., Gassmann W.;
RT   "RPS4-mediated disease resistance requires the combined presence of RPS4
RT   transcripts with full-length and truncated open reading frames.";
RL   Plant Cell 15:2333-2342(2003).
RN   [3]
RP   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).
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.
CC       {ECO:0000269|PubMed:14523247, ECO:0000269|PubMed:17951452}.
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. Alternative transcripts
CC         are necessary but not sufficient for resistance.;
CC       Name=1;
CC         IsoId=Q9SCX6-1; 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   -!- MISCELLANEOUS: Only two amino-acid changes (N195D and Y950H) are linked
CC       to a change from a resistant strain (cv. Columbia or cv. Landsberg
CC       erecta) to a susceptible one (cv. RLD). {ECO:0000269|PubMed:10571887}.
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DR   EMBL; AJ249264; CAB53785.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9SCX6; -.
DR   SMR; Q9SCX6; -.
DR   ExpressionAtlas; Q9SCX6; 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   1: Evidence at protein 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_0000431386"
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          682..706
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          708..728
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          729..749
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          750..774
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          796..818
FT                   /note="LRR 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          819..842
FT                   /note="LRR 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          861..887
FT                   /note="LRR 10"
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"
FT   MUTAGEN         195
FT                   /note="N->D: Loss of resistance. Loss of resistance; when
FT                   associated with H-950."
FT                   /evidence="ECO:0000269|PubMed:14523247"
FT   MUTAGEN         950
FT                   /note="Y->H: Loss of resistance. Loss of resistance; when
FT                   associated with D-195."
FT                   /evidence="ECO:0000269|PubMed:14523247"
SQ   SEQUENCE   1217 AA;  137761 MW;  34FD6949A2E2AEB5 CRC64;
     METSSISTVE DKPPQHQVFI NFRGADLRRR FVSHLVTALK LNNINVFIDD YEDRGQPLDV
     LLKRIEESKI VLAIFSGNYT ESVWCVRELE KIKDCTDEGT LVAIPIFYKL EPSTVRDLKG
     KFGDRFRSMA KGDERKKKWK EAFNLIPNIM GIIIDKKSVE 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 LYKFSREVDL KASNQDGSRQ RRLWLHQHII
     KGGIINVLQN KMKAANVRGI FLDLSEVEDE TSLDRDHFIN MGNLRYLKFY NSHCPQECKT
     NNKINIPDKL KLPLKEVRCL HWLKFPLETL PNDFNPINLV DLKLPYSETE 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 CAVISCLDPQ DQVSRLSVTC
     TFKVKDEDKS WVPYTCPVGS WTRHGGGKDK IELDHVFIGY TSCPHTIKCH EEGNSDECNP
     TEASLKFTVT GGTSENGKYK VFKCGLSLVY AKDKDKNSAL ETKYDMLIGK SFQETSEGVD
     GRVKKTKGKY VMPVEKNFQE TTEGVDGRVK KKKKTRMDNG RPKKKQRSGR DDNQTRMQVE
     LQEGNINSVI MHTVKNF
 
 
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