DAR4_ARATH
ID DAR4_ARATH Reviewed; 1613 AA.
AC Q9FKN7; Q9FKN8;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Protein DA1-related 4 {ECO:0000303|PubMed:18483219};
DE AltName: Full=Protein CHILLING SENSITIVE 3 {ECO:0000303|PubMed:20444230};
GN Name=DAR4 {ECO:0000303|PubMed:18483219};
GN Synonyms=CHS3 {ECO:0000303|PubMed:20444230}; OrderedLocusNames=At5g17890;
GN ORFNames=MPI7.5, MPI7.6;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18483219; DOI=10.1101/gad.463608;
RA Li Y., Zheng L., Corke F., Smith C., Bevan M.W.;
RT "Control of final seed and organ size by the DA1 gene family in Arabidopsis
RT thaliana.";
RL Genes Dev. 22:1331-1336(2008).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-201 AND ASP-278.
RX PubMed=20444230; DOI=10.1111/j.1365-313x.2010.04241.x;
RA Yang H., Shi Y., Liu J., Guo L., Zhang X., Yang S.;
RT "A mutant CHS3 protein with TIR-NB-LRR-LIM domains modulates growth, cell
RT death and freezing tolerance in a temperature-dependent manner in
RT Arabidopsis.";
RL Plant J. 63:283-296(2010).
CC -!- FUNCTION: NB-LRR receptor-like protein that modulates growth, cell
CC death and freezing tolerance in a temperature-dependent manner. May be
CC involved in defense responses. {ECO:0000269|PubMed:20444230}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:20444230}.
CC -!- MISCELLANEOUS: The gain-of-function mutants chs3-1 show no visible
CC phenotype when grown at the permissive temperature of 22 degrees
CC Celsius. Mutant plants (chs3-1) germinated and grown at 16 degrees
CC Celsius show developmental defects, including dwarfism, with small and
CC curly leaves, early senescence of cotyledons, constitutively activated
CC defense responses and enhanced tolerance to freezing temperatures.
CC {ECO:0000269|PubMed:20444230}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AY079160; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB11222.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB11223.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB011480; BAB11222.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB011480; BAB11223.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92482.1; -; Genomic_DNA.
DR EMBL; AY079160; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_197291.2; NM_121795.4.
DR AlphaFoldDB; Q9FKN7; -.
DR SMR; Q9FKN7; -.
DR BioGRID; 16933; 1.
DR STRING; 3702.AT5G17890.1; -.
DR iPTMnet; Q9FKN7; -.
DR PaxDb; Q9FKN7; -.
DR PRIDE; Q9FKN7; -.
DR ProteomicsDB; 222195; -.
DR EnsemblPlants; AT5G17890.1; AT5G17890.1; AT5G17890.
DR GeneID; 831657; -.
DR Gramene; AT5G17890.1; AT5G17890.1; AT5G17890.
DR KEGG; ath:AT5G17890; -.
DR Araport; AT5G17890; -.
DR TAIR; locus:2170338; AT5G17890.
DR eggNOG; KOG1703; Eukaryota.
DR HOGENOM; CLU_001561_0_3_1; -.
DR InParanoid; Q9FKN7; -.
DR OMA; QCWAPTE; -.
DR OrthoDB; 132512at2759; -.
DR PhylomeDB; Q9FKN7; -.
DR PRO; PR:Q9FKN7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKN7; baseline and differential.
DR Genevisible; Q9FKN7; AT.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; 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 Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR045218; DA1-like.
DR InterPro; IPR022087; DA1-like_dom.
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 InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24209; PTHR24209; 1.
DR Pfam; PF12315; DA1-like; 1.
DR Pfam; PF00412; LIM; 1.
DR Pfam; PF07725; LRR_3; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS50104; TIR; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Leucine-rich repeat; LIM domain; Metal-binding;
KW Nucleotide-binding; Reference proteome; Repeat; Zinc.
FT CHAIN 1..1613
FT /note="Protein DA1-related 4"
FT /id="PRO_0000396939"
FT DOMAIN 15..163
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 178..427
FT /note="NB-ARC"
FT REPEAT 448..473
FT /note="LRR 1"
FT REPEAT 516..540
FT /note="LRR 2"
FT REPEAT 569..592
FT /note="LRR 3"
FT REPEAT 594..615
FT /note="LRR 4"
FT REPEAT 617..637
FT /note="LRR 5"
FT REPEAT 638..661
FT /note="LRR 6"
FT REPEAT 662..682
FT /note="LRR 7"
FT REPEAT 683..703
FT /note="LRR 8"
FT REPEAT 723..747
FT /note="LRR 9"
FT REPEAT 748..770
FT /note="LRR 10"
FT REPEAT 771..791
FT /note="LRR 11"
FT REPEAT 792..816
FT /note="LRR 12"
FT REPEAT 822..847
FT /note="LRR 13"
FT REPEAT 888..911
FT /note="LRR 14"
FT DOMAIN 1238..1297
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1057..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1109..1234
FT /evidence="ECO:0000255"
FT COMPBIAS 1057..1074
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 201
FT /note="G->D: In chs3-r1; suppression of the chs3-1
FT phenotype."
FT /evidence="ECO:0000269|PubMed:20444230"
FT MUTAGEN 278
FT /note="D->N: In chs3-r2; suppression of the chs3-1
FT phenotype."
FT /evidence="ECO:0000269|PubMed:20444230"
FT CONFLICT 251
FT /note="F -> L (in Ref. 3; AY079160)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="N -> S (in Ref. 3; AY079160)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1613 AA; 185137 MW; 9E55F0B203DC79A8 CRC64;
MEPPAARVTP SIKADCSHSV NIICEETVLH SLVSHLSAAL RREGISVFVD ACGLQETKFF
SIKQNQPLTD GARVLVVVIS DEVEFYDPWF PKFLKVIQGW QNNGHVVVPV FYGVDSLTRV
YGWANSWLEA EKLTSHQSKI LSNNVLTDSE LVEEIVRDVY GKLYPAERVG IYARLLEIEK
LLYKQHRDIR SIGIWGMPGI GKTTLAKAVF NHMSTDYDAS CFIENFDEAF HKEGLHRLLK
ERIGKILKDE FDIESSYIMR PTLHRDKLYD KRILVVLDDV RDSLAAESFL KRLDWFGSGS
LIIITSVDKQ VFAFCQINQI YTVQGLNVHE ALQLFSQSVF GINEPEQNDR KLSMKVIDYV
NGNPLALSIY GRELMGKKSE METAFFELKH CPPLKIQDVL KNAYSALSDN EKNIVLDIAF
FFKGETVNYV MQLLEESHYF PRLAIDVLVD KCVLTISENT VQMNNLIQDT CQEIFNGEIE
TCTRMWEPSR IRYLLEYDEL EGSGETKAMP KSGLVAEHIE SIFLDTSNVK FDVKHDAFKN
MFNLKFLKIY NSCSKYISGL NFPKGLDSLP YELRLLHWEN YPLQSLPQDF DFGHLVKLSM
PYSQLHKLGT RVKDLVMLKR LILSHSLQLV ECDILIYAQN IELIDLQGCT GLQRFPDTSQ
LQNLRVVNLS GCTEIKCFSG VPPNIEELHL QGTRIREIPI FNATHPPKVK LDRKKLWNLL
ENFSDVEHID LECVTNLATV TSNNHVMGKL VCLNMKYCSN LRGLPDMVSL ESLKVLYLSG
CSELEKIMGF PRNLKKLYVG GTAIRELPQL PNSLEFLNAH GCKHLKSINL DFEQLPRHFI
FSNCYRFSSQ VIAEFVEKGL VASLARAKQE ELIKAPEVII CIPMDTRQRS SFRLQAGRNA
MTDLVPWMQK PISGFSMSVV VSFQDDYHND VGLRIRCVGT WKTWNNQPDR IVERFFQCWA
PTEAPKVVAD HIFVLYDTKM HPSDSEENHI SMWAHEVKFE FHTVSGENNP LGASCKVTEC
GVEVITAATG DTSVSGIIRE SETITIIEKE DTIIDEEDTP LLSRKPEETN RSRSSSELQK
LSSTSSKVRS KGNVFWKWLG CFPLQPKNLR SRSRRTTALE EALEEALKER EKLEDTRELQ
IALIESKKIK KIKQADERDQ IKHADEREQR KHSKDHEEEE IESNEKEERR HSKDYVIEEL
VLKGKGKRKQ LDDDKADEKE QIKHSKDHVE EEVNPPLSKC KDCKSAIEDG ISINAYGSVW
HPQCFCCLRC REPIAMNEIS DLRGMYHKPC YKELRHPNCY VCEKKIPRTA EGLKYHEHPF
WMETYCPSHD GDGTPKCCSC ERLEHCGTQY VMLADFRWLC RECMDSAIMD SDECQPLHFE
IREFFEGLHM KIEEEFPVYL VEKNALNKAE KEEKIDKQGD QCLMVVRGIC LSEEQIVTSV
SQGVRRMLNK QILDTVTESQ RVVRKCEVTA ILILYGLPRL LTGYILAHEM MHAYLRLNGY
RNLNMVLEEG LCQVLGYMWL ECQTYVFDTA TIASSSSSSR TPLSTTTSKK VDPSDFEKRL
VNFCKHQIET DESPFFGDGF RKVNKMMASN NHSLKDTLKE IISISKTPQY SKL
