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ADR1_ARATH
ID   ADR1_ARATH              Reviewed;         787 AA.
AC   Q9FW44;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Disease resistance protein ADR1;
DE   AltName: Full=Activated disease resistance protein 1;
GN   Name=ADR1; OrderedLocusNames=At1g33560; ORFNames=F10C21.19, T1E4.6;
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], FUNCTION, AND INDUCTION.
RX   PubMed=12906111; DOI=10.1094/mpmi.2003.16.8.669;
RA   Grant J.J., Chini A., Basu D., Loake G.J.;
RT   "Targeted activation tagging of the Arabidopsis NBS-LRR gene, ADR1, conveys
RT   resistance to virulent pathogens.";
RL   Mol. Plant Microbe Interact. 16:669-680(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
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).
CC   -!- FUNCTION: Disease resistance (R) protein that mediates resistance
CC       against Hyaloperonospora parasitica in a salicylic acid-dependent
CC       manner. Also mediates resistance against Erysiphe cichoracearum is both
CC       salicylic acid-dependent and partially NPR1-dependent. Resistance
CC       proteins guard the plant against pathogens that contain an appropriate
CC       avirulence protein via an indirect interaction with this avirulence
CC       protein. That triggers a defense system including the hypersensitive
CC       response, which restricts the pathogen growth.
CC       {ECO:0000269|PubMed:12906111}.
CC   -!- INDUCTION: Accumulates in leaves 1.5 hours postinfiltration of
CC       Pseudomonas syringae. {ECO:0000269|PubMed:12906111}.
CC   -!- DOMAIN: The LRR repeats probably act as specificity determinant of
CC       pathogen recognition. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the disease resistance NB-LRR family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG26078.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAG51211.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=NIB-LRRS; Note=Functional and comparative genomics
CC       of disease resistance gene homologs;
CC       URL="http://niblrrs.ucdavis.edu";
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DR   EMBL; AJ581996; CAE46486.1; -; mRNA.
DR   EMBL; AC051630; AAG51211.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC069299; AAG26078.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE31605.1; -; Genomic_DNA.
DR   PIR; D86459; D86459.
DR   RefSeq; NP_174620.2; NM_103079.4.
DR   AlphaFoldDB; Q9FW44; -.
DR   SMR; Q9FW44; -.
DR   STRING; 3702.AT1G33560.1; -.
DR   iPTMnet; Q9FW44; -.
DR   PaxDb; Q9FW44; -.
DR   PRIDE; Q9FW44; -.
DR   ProteomicsDB; 244905; -.
DR   EnsemblPlants; AT1G33560.1; AT1G33560.1; AT1G33560.
DR   GeneID; 840250; -.
DR   Gramene; AT1G33560.1; AT1G33560.1; AT1G33560.
DR   KEGG; ath:AT1G33560; -.
DR   Araport; AT1G33560; -.
DR   TAIR; locus:2006932; AT1G33560.
DR   eggNOG; ENOG502QU6E; Eukaryota.
DR   HOGENOM; CLU_012216_1_0_1; -.
DR   InParanoid; Q9FW44; -.
DR   OMA; LPREWEK; -.
DR   OrthoDB; 175097at2759; -.
DR   PhylomeDB; Q9FW44; -.
DR   PRO; PR:Q9FW44; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FW44; baseline and differential.
DR   Genevisible; Q9FW44; AT.
DR   GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; TAS:TAIR.
DR   GO; GO:0042742; P:defense response to bacterium; IGI:TAIR.
DR   GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR   GO; GO:0051707; P:response to other organism; IEP:TAIR.
DR   GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.8.430; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR042197; Apaf_helical.
DR   InterPro; IPR044974; Disease_R_plants.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR002182; NB-ARC.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008808; Powdery_mildew-R_dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR11017; PTHR11017; 1.
DR   Pfam; PF00931; NB-ARC; 1.
DR   Pfam; PF05659; RPW8; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51153; RPW8; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Hypersensitive response; Leucine-rich repeat;
KW   Nucleotide-binding; Plant defense; Reference proteome; Repeat.
FT   CHAIN           1..787
FT                   /note="Disease resistance protein ADR1"
FT                   /id="PRO_0000212732"
FT   DOMAIN          1..149
FT                   /note="RPW8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00495"
FT   DOMAIN          247..414
FT                   /note="NB-ARC"
FT   REPEAT          549..575
FT                   /note="LRR 1"
FT   REPEAT          576..599
FT                   /note="LRR 2"
FT   REPEAT          650..674
FT                   /note="LRR 3"
FT   REPEAT          722..745
FT                   /note="LRR 4"
FT   COILED          96..112
FT                   /evidence="ECO:0000255"
FT   BINDING         193..200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   787 AA;  90129 MW;  DD13DC48D8071F59 CRC64;
     MASFIDLFAG DITTQLLKLL ALVANTVYSC KGIAERLITM IRDVQPTIRE IQYSGAELSN
     HHQTQLGVFY EILEKARKLC EKVLRCNRWN LKHVYHANKM KDLEKQISRF LNSQILLFVL
     AEVCHLRVNG DRIERNMDRL LTERNDSLSF PETMMEIETV SDPEIQTVLE LGKKKVKEMM
     FKFTDTHLFG ISGMSGSGKT TLAIELSKDD DVRGLFKNKV LFLTVSRSPN FENLESCIRE
     FLYDGVHQRK LVILDDVWTR ESLDRLMSKI RGSTTLVVSR SKLADPRTTY NVELLKKDEA
     MSLLCLCAFE QKSPPSPFNK YLVKQVVDEC KGLPLSLKVL GASLKNKPER YWEGVVKRLL
     RGEAADETHE SRVFAHMEES LENLDPKIRD CFLDMGAFPE DKKIPLDLLT SVWVERHDID
     EETAFSFVLR LADKNLLTIV NNPRFGDVHI GYYDVFVTQH DVLRDLALHM SNRVDVNRRE
     RLLMPKTEPV LPREWEKNKD EPFDAKIVSL HTGEMDEMNW FDMDLPKAEV LILNFSSDNY
     VLPPFIGKMS RLRVLVIINN GMSPARLHGF SIFANLAKLR SLWLKRVHVP ELTSCTIPLK
     NLHKIHLIFC KVKNSFVQTS FDISKIFPSL SDLTIDHCDD LLELKSIFGI TSLNSLSITN
     CPRILELPKN LSNVQSLERL RLYACPELIS LPVEVCELPC LKYVDISQCV SLVSLPEKFG
     KLGSLEKIDM RECSLLGLPS SVAALVSLRH VICDEETSSM WEMVKKVVPE LCIEVAKKCF
     TVDWLDD
 
 
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