位置:首页 > 蛋白库 > RPP1_ARATH
RPP1_ARATH
ID   RPP1_ARATH              Reviewed;        1194 AA.
AC   F4J339; Q9LXN9;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Probable disease resistance protein RPP1 {ECO:0000305};
DE   AltName: Full=Probable NAD(+) hydrolase RPP1;
DE            EC=3.2.2.6 {ECO:0000305|PubMed:31439792, ECO:0000305|PubMed:31439793};
DE   AltName: Full=Protein RECOGNITION OF PERONOSPORA PARASITICA 1 {ECO:0000305};
GN   Name=RPP1 {ECO:0000305};
GN   OrderedLocusNames=At3g44480 {ECO:0000312|Araport:AT3G44480};
GN   ORFNames=F14L2_30 {ECO:0000312|EMBL:CAB88530.1};
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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   INDUCTION.
RX   PubMed=20831409; DOI=10.1094/mpmi-01-10-0022;
RA   Mohr T.J., Mammarella N.D., Hoff T., Woffenden B.J., Jelesko J.G.,
RA   McDowell J.M.;
RT   "The Arabidopsis downy mildew resistance gene RPP8 is induced by pathogens
RT   and salicylic acid and is regulated by W box cis elements.";
RL   Mol. Plant Microbe Interact. 23:1303-1315(2010).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=31439792; DOI=10.1126/science.aax1911;
RA   Horsefield S., Burdett H., Zhang X., Manik M.K., Shi Y., Chen J., Qi T.,
RA   Gilley J., Lai J.S., Rank M.X., Casey L.W., Gu W., Ericsson D.J., Foley G.,
RA   Hughes R.O., Bosanac T., von Itzstein M., Rathjen J.P., Nanson J.D.,
RA   Boden M., Dry I.B., Williams S.J., Staskawicz B.J., Coleman M.P., Ve T.,
RA   Dodds P.N., Kobe B.;
RT   "NAD+ cleavage activity by animal and plant TIR domains in cell death
RT   pathways.";
RL   Science 365:793-799(2019).
RN   [5]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=31439793; DOI=10.1126/science.aax1771;
RA   Wan L., Essuman K., Anderson R.G., Sasaki Y., Monteiro F., Chung E.H.,
RA   Osborne Nishimura E., DiAntonio A., Milbrandt J., Dangl J.L.,
RA   Nishimura M.T.;
RT   "TIR domains of plant immune receptors are NAD+-cleaving enzymes that
RT   promote cell death.";
RL   Science 365:799-803(2019).
CC   -!- FUNCTION: TIR-NB-LRR receptor-like protein that confers resistance to
CC       the pathogen Hyaloperonospora arabidopsis (By similarity). Probably
CC       acts as a NAD(+) hydrolase (NADase): in response to activation,
CC       catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide;
CC       NAD(+) cleavage triggering a defense system that promotes cell death
CC       (PubMed:31439792, PubMed:31439793). {ECO:0000250|UniProtKB:F4JNA9,
CC       ECO:0000269|PubMed:31439792, ECO:0000269|PubMed:31439793}.
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:0000305|PubMed:31439792, ECO:0000305|PubMed:31439793};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC         Evidence={ECO:0000305|PubMed:31439792, ECO:0000305|PubMed:31439793};
CC   -!- INDUCTION: By infection with Hyaloperonospora arabidopsidis isolate
CC       Emco5. {ECO:0000269|PubMed:20831409}.
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 TIR-NB-LRR family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB88530.1; Type=Erroneous gene model prediction; Evidence={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; AL353818; CAB88530.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE77906.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM64388.1; -; Genomic_DNA.
DR   PIR; T48928; T48928.
DR   RefSeq; NP_001326419.1; NM_001339143.1.
DR   RefSeq; NP_190034.2; NM_114316.3.
DR   AlphaFoldDB; F4J339; -.
DR   SMR; F4J339; -.
DR   STRING; 3702.AT3G44480.1; -.
DR   iPTMnet; F4J339; -.
DR   PaxDb; F4J339; -.
DR   PRIDE; F4J339; -.
DR   ProteomicsDB; 226511; -.
DR   EnsemblPlants; AT3G44480.1; AT3G44480.1; AT3G44480.
DR   EnsemblPlants; AT3G44480.4; AT3G44480.4; AT3G44480.
DR   GeneID; 823573; -.
DR   Gramene; AT3G44480.1; AT3G44480.1; AT3G44480.
DR   Gramene; AT3G44480.4; AT3G44480.4; AT3G44480.
DR   KEGG; ath:AT3G44480; -.
DR   Araport; AT3G44480; -.
DR   TAIR; locus:2076043; AT3G44480.
DR   eggNOG; ENOG502SUNR; Eukaryota.
DR   HOGENOM; CLU_001561_0_1_1; -.
DR   InParanoid; F4J339; -.
DR   PRO; PR:F4J339; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; F4J339; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR   GO; GO:0000139; C:Golgi membrane; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140376; F:innate immune receptor activity; EXP:PHI-base.
DR   GO; GO:0030275; F:LRR domain binding; ISS:TAIR.
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; TAS:TAIR.
DR   GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR   GO; GO:0002758; P:innate immune response-activating signal transduction; IMP:PHI-base.
DR   GO; GO:0034052; P:positive regulation of plant-type hypersensitive response; IMP:PHI-base.
DR   GO; GO:0002239; P:response to oomycetes; IDA:TAIR.
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; -; 3.
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   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11017; PTHR11017; 3.
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; 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; Leucine-rich repeat; NAD; Nucleotide-binding;
KW   Plant defense; Reference proteome; Repeat.
FT   CHAIN           1..1194
FT                   /note="Probable disease resistance protein RPP1"
FT                   /id="PRO_0000433378"
FT   DOMAIN          96..260
FT                   /note="TIR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT   DOMAIN          280..535
FT                   /note="NB-ARC"
FT                   /evidence="ECO:0000255"
FT   REPEAT          623..647
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          658..681
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          690..713
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          714..737
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          739..760
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          761..784
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          786..807
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          808..831
FT                   /note="LRR 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          832..855
FT                   /note="LRR 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          866..878
FT                   /note="LRR 10"
FT                   /evidence="ECO:0000255"
FT   REPEAT          879..899
FT                   /note="LRR 11"
FT                   /evidence="ECO:0000255"
FT   REPEAT          900..922
FT                   /note="LRR 12"
FT                   /evidence="ECO:0000255"
FT   REPEAT          943..965
FT                   /note="LRR 13"
FT                   /evidence="ECO:0000255"
FT   REPEAT          966..991
FT                   /note="LRR 14"
FT                   /evidence="ECO:0000255"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1170..1194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1170..1185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT   BINDING         105..110
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:V9M398"
SQ   SEQUENCE   1194 AA;  136132 MW;  8A09D6203D35DA1A CRC64;
     MGSVMSLGCS KRKATNQDVD SESRKRRKIC STNDAENCRF IQDESSWKHP WSLCANRVIS
     VAAVALTNFR FQQDNQESNS SSLSLPSPAT SVSRNWKHDV FPSFHGADVR RTFLSHIMES
     FRRKGIDTFI DNNIERSKSI GPELKEAIKG SKIAIVLLSR KYASSSWCLD ELAEIMKCRQ
     MVGQIVMTIF YEVDPTDIKK QTGEFGKAFT KTCRGKPKEQ VERWRKALED VATIAGYHSH
     SWRNEADMIE KISTDVSNML NSFTPSRDFD GLVGMRAHMD MLEQLLRLDL DEVRMIGIWG
     PPGIGKTTIA RFLFNQVSDR FQLSAIMVNI KGCYPRPCFD EYSAQLQLQN QMLSQMINHK
     DIMISHLGVA QERLRDKKVF LVLDEVDQLG QLDALAKETR WFGPGSRIII TTEDLGVLKA
     HGINHVYKVE YPSNDEAFQI FCMNAFGQKQ PHEGFDEIAW EVTCLAGELP LGLKVLGSAL
     RGKSKREWER TLPRLKTSLD GKIGSIIQFS YDVLCDEDKY LFLYIACLFN GESTTKVKEL
     LGKFLDVKQG LHLLAQKSLI SFDGERIHMH TLLEQFGRET SRKQFVHHGF TKRQLLVGAR
     GICEVLDDDT TDSRRFIGIH LELSNTEEEL NISEKVLERV HDFHFVRIDA SFQPERLQLA
     LQDLIYHSPK IRSLNWYGYE SLCLPSTFNP EFLVELDMRS SNLRKLWEGT KQLRNLKWMD
     LSYSSYLKEL PNLSTATNLE ELKLRNCSSL VELPSSIEKL TSLQILDLEN CSSLEKLPAI
     ENATKLRELK LQNCSSLIEL PLSIGTATNL KQLNISGCSS LVKLPSSIGD ITDLEVFDLS
     NCSSLVTLPS SIGNLQNLCK LIMRGCSKLE ALPININLKS LDTLNLTDCS QLKSFPEIST
     HISELRLKGT AIKEVPLSIM SWSPLADFQI SYFESLMEFP HAFDIITKLH LSKDIQEVPP
     WVKRMSRLRD LSLNNCNNLV SLPQLSDSLD YIYADNCKSL ERLDCCFNNP EIRLYFPKCF
     KLNQEARDLI MHTCIDAMFP GTQVPACFIH RATSGDSLKI KLKESPLPTT LRFKACIMLV
     KVNEELMSYD QTPMIVDIVI RDEHNDLKEK IYPSIYPSIY PLLTEHIYTF ELDVEEVTST
     ELVFEFPQLN KRNWKIGECG ILQRETRSLR RSSSPDLSPE SSRVSSYDHC LRGD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024