UNI_ARATH
ID UNI_ARATH Reviewed; 889 AA.
AC Q940K0; O22728;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Disease resistance protein UNI {ECO:0000305};
DE AltName: Full=Protein UNI {ECO:0000303|PubMed:18315541};
GN Name=UNI {ECO:0000303|PubMed:18315541};
GN OrderedLocusNames=At1g61180 {ECO:0000312|Araport:AT1G61180};
GN ORFNames=F11P17.10 {ECO:0000312|EMBL:AAB71477.1};
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=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 [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 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 [4]
RP FUNCTION, AND MUTAGENESIS OF 763-VAL--GLU-767.
RX PubMed=18315541; DOI=10.1111/j.1365-313x.2008.03466.x;
RA Igari K., Endo S., Hibara K., Aida M., Sakakibara H., Kawasaki T.,
RA Tasaka M.;
RT "Constitutive activation of a CC-NB-LRR protein alters morphogenesis
RT through the cytokinin pathway in Arabidopsis.";
RL Plant J. 55:14-27(2008).
RN [5]
RP INTERACTION WITH RPT2A.
RX PubMed=21791544; DOI=10.1093/pcp/pcr099;
RA Chung K., Tasaka M.;
RT "RPT2a, a 26S proteasome AAA-ATPase, is directly involved in Arabidopsis
RT CC-NBS-LRR protein uni-1D-induced signaling pathways.";
RL Plant Cell Physiol. 52:1657-1664(2011).
RN [6]
RP FUNCTION.
RX PubMed=27016096; DOI=10.1093/pcp/pcw060;
RA Ogawa T., Mori A., Igari K., Morita M.T., Tasaka M., Uchida N.;
RT "Efficient in planta detection and dissection of de novo mutation events in
RT the Arabidopsis thaliana disease resistance gene UNI.";
RL Plant Cell Physiol. 57:1123-1132(2016).
CC -!- FUNCTION: Involved in disease resistance via the salicylic acid (SA)
CC signaling pathway (PubMed:18315541, PubMed:27016096). Involved in shoot
CC architecture development via the cytokinin signaling pathway
CC (PubMed:18315541, PubMed:27016096). {ECO:0000269|PubMed:18315541,
CC ECO:0000269|PubMed:27016096}.
CC -!- SUBUNIT: Interacts with RPT2A. {ECO:0000269|PubMed:21791544}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q940K0-1; Sequence=Displayed;
CC -!- DOMAIN: The LRR repeats probably act as specificity determinant of
CC pathogen recognition. {ECO:0000250|UniProtKB:Q8W4J9}.
CC -!- MISCELLANEOUS: The gain-of-function mutant uni-1D (T-DNA tagging)
CC exhibits bushy and severe dwarf phenotype, due to altered shoot
CC architecture caused by enhanced axillary branch formation via the
CC cytokinin pathway (PubMed:18315541). Uni-1D plants exhibit constitutive
CC expression of pathogenesis-related (PR) genes through salicylic acid
CC accumulation (PubMed:18315541). 'Uni' means sea urchin in Japanese
CC (PubMed:18315541). {ECO:0000269|PubMed:18315541,
CC ECO:0000303|PubMed:18315541}.
CC -!- SIMILARITY: Belongs to the disease resistance NB-LRR family.
CC {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; AC002294; AAB71477.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33799.1; -; Genomic_DNA.
DR EMBL; AY054518; AAK96709.1; -; mRNA.
DR PIR; F96637; F96637.
DR RefSeq; NP_176313.1; NM_104799.4. [Q940K0-1]
DR AlphaFoldDB; Q940K0; -.
DR SMR; Q940K0; -.
DR BioGRID; 27635; 2.
DR STRING; 3702.AT1G61180.2; -.
DR iPTMnet; Q940K0; -.
DR PaxDb; Q940K0; -.
DR ProteomicsDB; 224312; -. [Q940K0-1]
DR EnsemblPlants; AT1G61180.1; AT1G61180.1; AT1G61180. [Q940K0-1]
DR GeneID; 842411; -.
DR Gramene; AT1G61180.1; AT1G61180.1; AT1G61180. [Q940K0-1]
DR KEGG; ath:AT1G61180; -.
DR Araport; AT1G61180; -.
DR eggNOG; KOG4658; Eukaryota.
DR HOGENOM; CLU_000427_4_0_1; -.
DR InParanoid; Q940K0; -.
DR OMA; NISWIQR; -.
DR PhylomeDB; Q940K0; -.
DR PRO; PR:Q940K0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q940K0; baseline and differential.
DR Genevisible; Q940K0; AT.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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; -; 2.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR044974; Disease_R_plants.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR23155; PTHR23155; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; Leucine-rich repeat;
KW Nucleotide-binding; Plant defense; Reference proteome; Repeat.
FT CHAIN 1..889
FT /note="Disease resistance protein UNI"
FT /id="PRO_0000212747"
FT DOMAIN 137..440
FT /note="NB-ARC"
FT /evidence="ECO:0000255"
FT REPEAT 510..532
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 533..555
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 557..580
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 581..603
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 604..625
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 626..652
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 653..676
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 698..721
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 825..848
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REGION 131..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 19..64
FT /evidence="ECO:0000255"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 763..767
FT /note="VLLIE->YLYIG: In uni-1D; constitutive activation of
FT UNI."
FT /evidence="ECO:0000269|PubMed:18315541"
FT CONFLICT 465
FT /note="G -> S (in Ref. 3; AAK96709)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 889 AA; 101673 MW; 9156D13EFD56643D CRC64;
MGSCFSLQVS DQTLNRIFNC LIGKSYIRTL EKNLRALQRE MEDLRAIQHE VQNKVARDEA
RHQRRLEAVQ VWLDRVNSVD IECKDLLSVT PVELQKLCLC GLCSKYVCSS YKYGKKVFLL
LEEVKKLNSE GNFDEVSQPP PRSEVEERPT QPTIGQEDML EKAWNRLMED GVGIMGLHGM
GGVGKTTLFK KIHNKFAEIG GTFDIVIWIV VSKGVMISKL QEDIAEKLHL CDDLWKNKNE
SDKATDIHRV LKGKRFVLML DDIWEKVDLE AIGIPYPSEV NKCKVAFTTR SREVCGEMGD
HKPMQVNCLE PEDAWELFKN KVGDNTLSSD PVIVELAREV AQKCRGLPLA LNVIGETMSS
KTMVQEWEHA IHVFNTSAAE FSDMQNKILP ILKYSYDSLG DEHIKSCFLY CALFPEDGEI
YNEKLIDYWI CEGFIGEDQV IKRARNKGYA MLGTLTRANL LTKVGTYYCV MHDVVREMAL
WIASDFGKQK ENFVVQAGVG LHEIPKVKDW GAVRKMSLMD NDIEEITCES KCSELTTLFL
QSNKLKNLPG AFIRYMQKLV VLDLSYNRDF NKLPEQISGL VSLQFLDLSN TSIEHMPIGL
KELKKLTFLD LTYTDRLCSI SGISRLLSLR LLRLLGSKVH GDASVLKELQ QLQNLQELAI
TVSAELISLD QRLAKLISNL CIEGFLQKPF DLSFLASMEN LSSLRVENSY FSEIKCRESE
TESSYLRINP KIPCFTNLSR LEIMKCHSMK DLTWILFAPN LVVLLIEDSR EVGEIINKEK
ATNLTSITPF LKLEWLILYN LPKLESIYWS PLPFPVLLTM DVSNCPKLRK LPLNATSVSK
VEEFEIHMYP PPEQENELEW EDDDTKNRFL PSIKPYKYFV YPGMSFLTV
