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WR52N_ARATH
ID   WR52N_ARATH             Reviewed;        1378 AA.
AC   E1B328; Q0WWA0; Q689Y9; Q8GZ83; Q9FH83; Q9FH84;
DT   26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Disease resistance protein RRS1 {ECO:0000303|PubMed:11842188};
DE   AltName: Full=Disease resistance protein RCH2;
DE   AltName: Full=Disease resistance protein SLH1;
DE   AltName: Full=Probable WRKY transcription factor 52;
DE   AltName: Full=Protein RPS4-homolog;
DE   AltName: Full=Protein SENSITIVE TO LOW HUMIDITY 1 {ECO:0000303|PubMed:16146526};
DE   AltName: Full=Resistance to Colletotrichum higginsianum 2 protein;
DE   AltName: Full=Resistance to Ralstonia solanacearum 1 protein {ECO:0000303|PubMed:11842188};
DE   AltName: Full=WRKY DNA-binding protein 52;
GN   Name=RRS1 {ECO:0000303|PubMed:11842188};
GN   Synonyms=RCH2, RRS1-R {ECO:0000303|PubMed:11842188}, RSH4,
GN   SLH1 {ECO:0000303|PubMed:16146526}, WRKY52;
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:ADM88042.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RC   STRAIN=cv. Nd-1;
RX   PubMed=11842188; DOI=10.1073/pnas.032485099;
RA   Deslandes L., Olivier J., Theulieres F., Hirsch J., Feng D.X.,
RA   Bittner-Eddy P., Beynon J., Marco Y.;
RT   "Resistance to Ralstonia solanacearum in Arabidopsis thaliana is conferred
RT   by the recessive RRS1-R gene, a member of a novel family of resistance
RT   genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:2404-2409(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LEU-1224, AND FUNCTION.
RC   STRAIN=cv. No-0;
RX   PubMed=16146526; DOI=10.1111/j.1365-313x.2005.02500.x;
RA   Noutoshi Y., Ito T., Seki M., Nakashita H., Yoshida S., Marco Y.,
RA   Shirasu K., Shinozaki K.;
RT   "A single amino acid insertion in the WRKY domain of the Arabidopsis TIR-
RT   NBS-LRR-WRKY-type disease resistance protein SLH1 (sensitive to low
RT   humidity 1) causes activation of defense responses and hypersensitive cell
RT   death.";
RL   Plant J. 43:873-888(2005).
RN   [3]
RP   INTERACTION WITH POPP2, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Nd-1;
RX   PubMed=12788974; DOI=10.1073/pnas.1230660100;
RA   Deslandes L., Olivier J., Peeters N., Feng D.X., Khounlotham M.,
RA   Boucher C., Somssich I., Genin S., Marco Y.;
RT   "Physical interaction between RRS1-R, a protein conferring resistance to
RT   bacterial wilt, and PopP2, a type III effector targeted to the plant
RT   nucleus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8024-8029(2003).
CC   -!- FUNCTION: Transcription factor. Interacts specifically with the W box
CC       (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-
CC       acting element. Acts also as a disease resistance protein involved in
CC       resistance to fungal and bacterial pathogens, including R.solanacearum,
CC       P.syringae pv. tomato and C.higginsianum. RRS1 mediated resistance
CC       depends on salicylic acid and NDR1 (AC O48915).
CC       {ECO:0000250|UniProtKB:P0DKH5, ECO:0000269|PubMed:11842188,
CC       ECO:0000305}.
CC   -!- SUBUNIT: Interacts with PopP2, a R.solanacearum type III effector.
CC       {ECO:0000269|PubMed:12788974}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12788974}. Cytoplasm
CC       {ECO:0000305|PubMed:12788974}. Note=The nuclear localization is only
CC       detected upon interaction with PopP2. {ECO:0000269|PubMed:12788974}.
CC   -!- MISCELLANEOUS: Ecotypes susceptible to C.higginsianum or
CC       R.solanacearum, such as cv. Columbia, contain a protein with a
CC       premature stop codon while the longer allele found in cv. Nd-1, cv.
CC       Wassilewskija or cv. RLD confers resistance. {ECO:0000305}.
CC   -!- MISCELLANEOUS: The slh1-induced phenotype (severely stunted growth when
CC       grown under conditions of low humidity) is suppressed under conditions
CC       of high humidity and high temperature. {ECO:0000269|PubMed:16146526}.
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DR   EMBL; HQ170631; ADM88042.1; -; mRNA.
DR   EMBL; AX103687; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR   EMBL; AX103688; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR   EMBL; AX103691; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR   EMBL; AB188827; BAD38678.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1B328; -.
DR   SMR; E1B328; -.
DR   ExpressionAtlas; E1B328; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
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; 2.20.25.80; -; 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; 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   InterPro; IPR003657; WRKY_dom.
DR   InterPro; IPR036576; WRKY_dom_sf.
DR   PANTHER; PTHR11017; PTHR11017; 2.
DR   Pfam; PF07725; LRR_3; 1.
DR   Pfam; PF00931; NB-ARC; 1.
DR   Pfam; PF03106; WRKY; 1.
DR   SMART; SM00774; WRKY; 1.
DR   SUPFAM; SSF118290; SSF118290; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF52200; SSF52200; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50104; TIR; 1.
DR   PROSITE; PS50811; WRKY; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; DNA-binding; Leucine-rich repeat;
KW   Nucleotide-binding; Nucleus; Plant defense; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1378
FT                   /note="Disease resistance protein RRS1"
FT                   /id="PRO_0000431360"
FT   DOMAIN          5..146
FT                   /note="TIR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT   DOMAIN          170..421
FT                   /note="NB-ARC"
FT                   /evidence="ECO:0000255"
FT   REPEAT          498..522
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          535..553
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          554..575
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          577..598
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          621..646
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          665..688
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          742..766
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          768..793
FT                   /note="LRR 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          831..854
FT                   /note="LRR 9"
FT                   /evidence="ECO:0000255"
FT   DNA_BIND        1204..1272
FT                   /note="WRKY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT   REGION          1300..1321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           988..1005
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   BINDING         179..186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT   MUTAGEN         1224
FT                   /note="L->LL: In slh1; loss of DNA-binding activity and
FT                   constitutive defense activation."
FT                   /evidence="ECO:0000269|PubMed:16146526"
SQ   SEQUENCE   1378 AA;  156108 MW;  DB20F541F0BB73F0 CRC64;
     MTNCEKDEEF VCISCVEEVR YSFVSHLSEA LRRKGINNVV VDVDIDDLLF KESQAKIEKA
     GVSVMVLPGN CDPSEVWLDK FAKVLECQRN NKDQAVVSVL YGDSLLRDQW LSELDFRGLS
     RIHQSRKECS DSILVEEIVR DVYETHFYVG RIGIYSKLLE IENMVNKQPI GIRCVGIWGM
     PGIGKTTLAK AVFDQMSSAF DASCFIEDYD KSIHEKGLYC LLEEQLLPGN DATIMKLSSL
     RDRLNSKRVL VVLDDVCNAL VAESFLEGFD WLGPGSLIII TSRDKQVFRL CGINQIYEVQ
     GLNEKEARQL FLLSASIMED MGEQNLHELS VRVISYANGN PLAISVYGRE LKGKKKLSEM
     ETAFLKLKRR PPFKIVDAFK SSYDTLSDNE KNIFLDIACF FQGENVNYVI QLLEGCGFFP
     HVEIDVLVDK CLVTISENRV WLHKLTQDIG REIINGETVQ IERRRRLWEP WSIKYLLEYN
     EHKANGEPKT TFKRAQGSEE IEGLFLDTSN LRFDLQPSAF KNMLNLRLLK IYCSNPEVHP
     VINFPTGSLH SLPNELRLLH WENYPLKSLP QNFDPRHLVE INMPYSQLQK LWGGTKNLEM
     LRTIRLCHSQ HLVDIDDLLK AENLEVIDLQ GCTRLQNFPA AGRLLRLRVV NLSGCIKIKS
     VLEIPPNIEK LHLQGTGILA LPVSTVKPNH RELVNFLTEI PGLSEASKLE RLTSLLESNS
     SCQDLGKLIC LELKDCSCLQ SLPNMANLDL NVLDLSGCSS LNSIQGFPRF LKQLYLGGTA
     IREVPQLPQS LEILNAHGSC LRSLPNMANL EFLKVLDLSG CSELETIQGF PRNLKELYFA
     GTTLREVPQL PLSLEVLNAH GSDSEKLPMH YKFNNFFDLS QQVVNDFFLK ALTYVKHIPR
     GYTQELINKA PTFSFSAPSH TNQNATFDLQ PGSSVMTRLN HSWRNTLVGF GMLVEVAFPE
     DYCDATDVGI SCVCRWSNKE GRSCRIERNF HCWAPGKVVP KVRKDHTFVF SDVNMRPSTG
     EGNDPDIWAG LVVFEFFPIN QQTKCLNDRF TVTRCGVRVI NVATGNTSLE NISLVLSLDP
     VEVSGYEVLR VSYDDLQEMD KVLFLYIASL FNDEDVDFVA PLIAGIDLDV SSGLKVLADV
     SLISVSSNGE IVMHSLQRQM GKEILHGQSM LLSDCESSMT ENLSDVPKKE KKHRESKVKK
     VVSIPAIDEG DLWTWRKYGQ KDILGSRFPR GYYRCAYKFT HGCKATKQVQ RSETDSNMLA
     ITYLSEHNHP RPTKRKALAD STRSTSSSIC SAITTSASSR VFQNKDEPNQ PHLPSSSTPP
     RNAAVLFKMT DMEEFQDNME VDNDVVDTRT LALFPEFQHQ PEEEDPWSTF FDDYNFYF
 
 
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