TIR_ARATH
ID TIR_ARATH Reviewed; 176 AA.
AC Q9SSN3; A8MRJ7; B9DHJ4; Q9SE46;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Toll/interleukin-1 receptor-like protein;
DE Short=AtTIR;
GN Name=TIR; OrderedLocusNames=At1g72930; ORFNames=F3N23.13;
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], AND INTERACTION WITH MED37E.
RC STRAIN=cv. Columbia;
RA Kroczynska B., Ciesielski A., Stachnik K.;
RT "The nucleotide sequence of a cDNA encoding the AtTIR, a TIR-like
RT resistance protein in Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR99-172(1999).
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Flower, Rosette leaf, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP REVIEW, AND TISSUE SPECIFICITY.
RX PubMed=12366802; DOI=10.1046/j.1365-313x.2002.01404.x;
RA Meyers B.C., Morgante M., Michelmore R.W.;
RT "TIR-X and TIR-NBS proteins: two new families related to disease resistance
RT TIR-NBS-LRR proteins encoded in Arabidopsis and other plant genomes.";
RL Plant J. 32:77-92(2002).
RN [8]
RP REVIEW.
RX PubMed=12671079; DOI=10.1105/tpc.009308;
RA Meyers B.C., Kozik A., Griego A., Kuang H., Michelmore R.W.;
RT "Genome-wide analysis of NBS-LRR-encoding genes in Arabidopsis.";
RL Plant Cell 15:809-834(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
RX PubMed=19845004; DOI=10.1002/pro.275;
RA Chan S.L., Mukasa T., Santelli E., Low L.Y., Pascual J.;
RT "The crystal structure of a TIR domain from Arabidopsis thaliana reveals a
RT conserved helical region unique to plants.";
RL Protein Sci. 19:155-161(2010).
CC -!- FUNCTION: Disease resistance protein. Resistance proteins guard the
CC plant against pathogens that contain an appropriate avirulence protein
CC via a direct or indirect interaction with this avirulence protein. That
CC triggers a defense system including the hypersensitive response, which
CC restricts the pathogen growth (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MED37E. {ECO:0000269|Ref.1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SSN3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SSN3-2; Sequence=VSP_046493;
CC -!- TISSUE SPECIFICITY: Mostly present in shoots.
CC {ECO:0000269|PubMed:12366802}.
CC -!- CAUTION: In some plant proteins and in human SARM1, the TIR domain has
CC NAD(+) hydrolase (NADase) activity (By similarity). However, despite
CC the presence of the catalytic Asp residue, the isolated TIR domain of
CC human TLR4 lacks NADase activity (By similarity). Based on this, it is
CC unlikely that Toll-like receptors have NADase activity.
CC {ECO:0000250|UniProtKB:O00206, ECO:0000305}.
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DR EMBL; AF188334; AAF01328.1; -; mRNA.
DR EMBL; AC008017; AAD55640.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35392.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35393.1; -; Genomic_DNA.
DR EMBL; AY044312; AAK73253.1; -; mRNA.
DR EMBL; AY065114; AAL38290.1; -; mRNA.
DR EMBL; AY081663; AAM10225.1; -; mRNA.
DR EMBL; AK317547; BAH20211.1; -; mRNA.
DR EMBL; AK317731; BAH20388.1; -; mRNA.
DR EMBL; AY086809; AAM63858.1; -; mRNA.
DR PIR; E96754; E96754.
DR RefSeq; NP_001077816.1; NM_001084347.1. [Q9SSN3-2]
DR RefSeq; NP_177436.1; NM_105951.3. [Q9SSN3-1]
DR PDB; 3JRN; X-ray; 2.00 A; A=1-176.
DR PDBsum; 3JRN; -.
DR AlphaFoldDB; Q9SSN3; -.
DR SMR; Q9SSN3; -.
DR BioGRID; 28843; 3.
DR STRING; 3702.AT1G72930.1; -.
DR iPTMnet; Q9SSN3; -.
DR PaxDb; Q9SSN3; -.
DR PRIDE; Q9SSN3; -.
DR ProteomicsDB; 234306; -. [Q9SSN3-1]
DR DNASU; 843624; -.
DR EnsemblPlants; AT1G72930.1; AT1G72930.1; AT1G72930. [Q9SSN3-1]
DR EnsemblPlants; AT1G72930.2; AT1G72930.2; AT1G72930. [Q9SSN3-2]
DR GeneID; 843624; -.
DR Gramene; AT1G72930.1; AT1G72930.1; AT1G72930. [Q9SSN3-1]
DR Gramene; AT1G72930.2; AT1G72930.2; AT1G72930. [Q9SSN3-2]
DR KEGG; ath:AT1G72930; -.
DR Araport; AT1G72930; -.
DR TAIR; locus:2032733; AT1G72930.
DR InParanoid; Q9SSN3; -.
DR OMA; RTHTISK; -.
DR OrthoDB; 1765914at2759; -.
DR PhylomeDB; Q9SSN3; -.
DR EvolutionaryTrace; Q9SSN3; -.
DR PRO; PR:Q9SSN3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SSN3; baseline and differential.
DR Genevisible; Q9SSN3; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA: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; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.10140; -; 1.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; NAD; Plant defense;
KW Receptor; Reference proteome.
FT CHAIN 1..176
FT /note="Toll/interleukin-1 receptor-like protein"
FT /id="PRO_0000422275"
FT DOMAIN 7..170
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT VAR_SEQ 153..176
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046493"
FT CONFLICT 126..127
FT /note="SR -> RV (in Ref. 1; AAF01328)"
FT /evidence="ECO:0000305"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:3JRN"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:3JRN"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:3JRN"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:3JRN"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:3JRN"
FT TURN 72..76
FT /evidence="ECO:0007829|PDB:3JRN"
FT HELIX 78..92
FT /evidence="ECO:0007829|PDB:3JRN"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:3JRN"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:3JRN"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:3JRN"
FT HELIX 130..143
FT /evidence="ECO:0007829|PDB:3JRN"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:3JRN"
SQ SEQUENCE 176 AA; 20245 MW; A77AD072BF381216 CRC64;
MSSHTATKYD VFLSFRGHDT RHNFISFLYK ELVRRSIRTF KDDKELENGQ RFSPELKSPI
EVSRFAVVVV SENYAASSWC LDELVTIMDF EKKGSITVMP IFYGVEPNHV RWQTGVLAEQ
FKKHASREDP EKVLKWRQAL TNFAQLSGDC SGDDDSKLVD KIANEISNKK TIYATI
