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RLM3_ARATH
ID   RLM3_ARATH              Reviewed;         796 AA.
AC   Q9FT77; F4JNC3; Q0WKX9; Q3EA02; Q682W8; Q9SUK2;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 142.
DE   RecName: Full=Disease resistance protein RLM3 {ECO:0000305};
DE            EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE   AltName: Full=Protein RESISTANCE TO LEPTOSPHAERIA MACULANS 3 {ECO:0000303|PubMed:18397376};
GN   Name=RLM3 {ECO:0000303|PubMed:18397376};
GN   OrderedLocusNames=At4g16990 {ECO:0000312|Araport:AT4G16990};
GN   ORFNames=dl4525w {ECO:0000312|EMBL:CAB46050.1};
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 [MRNA] (ISOFORM 1).
RA   Acarkan A., Schmidt R.H.;
RT   "Comparative analysis of the Arabidopsis thaliana and Capsella rubella
RT   genomes.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000312|Proteomes:UP000006548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia {ECO:0000312|Proteomes:UP000006548};
RX   PubMed=9461215; DOI=10.1038/35140;
RA   Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA   Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA   Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA   Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA   De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA   Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA   Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA   Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA   Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA   Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA   Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA   Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT   "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT   thaliana.";
RL   Nature 391:485-488(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   FUNCTION.
RX   PubMed=18397376; DOI=10.1111/j.1365-313x.2008.03503.x;
RA   Staal J., Kaliff M., Dewaele E., Persson M., Dixelius C.;
RT   "RLM3, a TIR domain encoding gene involved in broad-range immunity of
RT   Arabidopsis to necrotrophic fungal pathogens.";
RL   Plant J. 55:188-200(2008).
CC   -!- FUNCTION: TIR-NB-LRR receptor-like protein that confers resistance to
CC       the pathogens Leptosphaeria maculans (blackleg disease), Botrytis
CC       cinerea, Alternaria brassicicola and Alternaria brassicae. Required for
CC       efficient callose deposition downstream of RLM1 during infection with
CC       L.maculans. {ECO:0000269|PubMed:18397376}.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9FT77-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9FT77-2; Sequence=VSP_057759, VSP_057760, VSP_057761;
CC       Name=3;
CC         IsoId=Q9FT77-3; Sequence=VSP_057758;
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAB46050.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80970.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AJ299417; CAC14089.1; -; mRNA.
DR   EMBL; Z97342; CAB46050.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161545; CAB80970.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE83831.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83832.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83833.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM68095.1; -; Genomic_DNA.
DR   EMBL; AK175249; BAD43012.1; -; mRNA.
DR   EMBL; AK230430; BAF02228.1; -; mRNA.
DR   PIR; F85189; F85189.
DR   RefSeq; NP_001319972.1; NM_001341182.1. [Q9FT77-1]
DR   RefSeq; NP_193432.4; NM_117803.4. [Q9FT77-2]
DR   RefSeq; NP_849399.1; NM_179068.2. [Q9FT77-1]
DR   RefSeq; NP_849400.2; NM_179069.2. [Q9FT77-3]
DR   AlphaFoldDB; Q9FT77; -.
DR   SMR; Q9FT77; -.
DR   STRING; 3702.AT4G16990.2; -.
DR   iPTMnet; Q9FT77; -.
DR   PaxDb; Q9FT77; -.
DR   PRIDE; Q9FT77; -.
DR   ProteomicsDB; 228096; -. [Q9FT77-1]
DR   EnsemblPlants; AT4G16990.1; AT4G16990.1; AT4G16990. [Q9FT77-2]
DR   EnsemblPlants; AT4G16990.13; AT4G16990.13; AT4G16990. [Q9FT77-1]
DR   EnsemblPlants; AT4G16990.2; AT4G16990.2; AT4G16990. [Q9FT77-1]
DR   EnsemblPlants; AT4G16990.3; AT4G16990.3; AT4G16990. [Q9FT77-3]
DR   GeneID; 827407; -.
DR   Gramene; AT4G16990.1; AT4G16990.1; AT4G16990. [Q9FT77-2]
DR   Gramene; AT4G16990.13; AT4G16990.13; AT4G16990. [Q9FT77-1]
DR   Gramene; AT4G16990.2; AT4G16990.2; AT4G16990. [Q9FT77-1]
DR   Gramene; AT4G16990.3; AT4G16990.3; AT4G16990. [Q9FT77-3]
DR   KEGG; ath:AT4G16990; -.
DR   Araport; AT4G16990; -.
DR   TAIR; locus:2130319; AT4G16990.
DR   HOGENOM; CLU_353156_0_0_1; -.
DR   InParanoid; Q9FT77; -.
DR   OMA; WYENCER; -.
DR   PhylomeDB; Q9FT77; -.
DR   PRO; PR:Q9FT77; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9FT77; baseline and differential.
DR   Genevisible; Q9FT77; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IDA: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:0050832; P:defense response to fungus; IMP:TAIR.
DR   GO; GO:2000071; P:regulation of defense response by callose deposition; IMP:TAIR.
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   InterPro; IPR042197; Apaf_helical.
DR   InterPro; IPR013591; Brevis_radix_dom.
DR   InterPro; IPR044974; Disease_R_plants.
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; PF08381; BRX; 3.
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; PS51514; BRX; 3.
DR   PROSITE; PS50104; TIR; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Hydrolase; NAD; Nucleotide-binding;
KW   Plant defense; Reference proteome; Repeat.
FT   CHAIN           1..796
FT                   /note="Disease resistance protein RLM3"
FT                   /id="PRO_0000433381"
FT   DOMAIN          7..171
FT                   /note="TIR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT   DOMAIN          185..413
FT                   /note="NB-ARC"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          434..486
FT                   /note="BRX 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00847"
FT   DOMAIN          538..594
FT                   /note="BRX 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00847"
FT   DOMAIN          719..772
FT                   /note="BRX 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00847"
FT   REGION          502..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          607..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..531
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT   VAR_SEQ         1..158
FT                   /note="Missing (in isoform 3)"
FT                   /id="VSP_057758"
FT   VAR_SEQ         567
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_057759"
FT   VAR_SEQ         667..671
FT                   /note="LTDVN -> KGSDI (in isoform 2)"
FT                   /id="VSP_057760"
FT   VAR_SEQ         672..796
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_057761"
FT   CONFLICT        601
FT                   /note="R -> G (in Ref. 6; BAF02228)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   796 AA;  91154 MW;  30E0AF0590B6BA94 CRC64;
     MKSSSSQSYD VFPNFRGEDV RHSLVSHLRK ELDRKFINTF NDNRIERSRK ITPELLLAIE
     NSRISLVVFS KNYASSTWCL DELVKIQECY EKLDQMVIPI FYKVDPSHVR KQTGEFGMVF
     GETCKGRTEN EKRKWMRALA EVAHLAGEDL RNWRSEAEML ENIAKDVSNK LFPPSNNFSD
     FVGIEAHIEA LISMLRFDSK KARMIGICGP SETGKTTIGR ALYSRLKSDF HHRAFVAYKR
     KIRSDYDQKL YWEEQFLSEI LCQKDIKIEE CGAVEQRLKH TKVLIVLDDV DDIELLKTLV
     GRIRWFGSES KIVVITQKRE LLKAHNIAHV YEVGFPSEEL AHQMFCRYAF GKNSPPHGFN
     ELADEAAKIA GNRPKALKYV GSSFRRLDKE QWVKMLSEFR SNGNKLKISY DELDGKGQDY
     VACLTNGSNS QVKAEWIHLA LGVSILLNIR SDGTTILKHL SYNRSMAQQA KIWWYENLER
     VCKKYNICGI DSSTDGGGST YGQCSNSQFQ RNMDASPGGN KTSNQSTKDS PRASQVEKEK
     IEYCEPHVYI TPAIFSDGTR APKYVESSSR RVTQVHHAKT WWPENCEKVY ENHNNIYGID
     RSIDGGDKFE GKSKVSDGGL DGKDQGSMYG QSSNSELQIN MDADNRRCEP VSEMLFKNYN
     VCSPNGLTDV NCSNPQSQRK LDASLKKDKI VHEWIRTGSG FFFDFQGPKS IVSAAQVDEK
     NFEYCEQGVY ITLGILSGGI IVLKHLEFSR RMAQQAKVWW SENWIKVYQE HNICGIDKSF
     DGRFDDRRVI RQLRPN
 
 
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