MARD1_ARATH
ID MARD1_ARATH Reviewed; 263 AA.
AC Q8LGS1; Q8LA86; Q8VZ84; Q9M1W8;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Protein MARD1 {ECO:0000303|PubMed:15159630};
DE AltName: Full=FCS-Like Zinc finger 9 {ECO:0000303|PubMed:24901469};
DE AltName: Full=Mediator of ABA-regulated dormancy1 {ECO:0000303|PubMed:15159630};
DE AltName: Full=Senescence-associated protein SAG102 {ECO:0000303|PubMed:11402199};
GN Name=MARD1 {ECO:0000303|PubMed:15159630};
GN Synonyms=DUF581-19 {ECO:0000303|PubMed:24600465},
GN FLZ9 {ECO:0000303|PubMed:24901469}, SAG102 {ECO:0000303|PubMed:11402199};
GN OrderedLocusNames=At3g63210 {ECO:0000312|Araport:AT3G63210};
GN ORFNames=F16M2.6 {ECO:0000312|EMBL:AAL38351.1};
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 [GENOMIC DNA], DEVELOPMENTAL STAGE, AND INDUCTION BY
RP ABSCISIC ACID.
RX PubMed=11402199; DOI=10.1104/pp.126.2.707;
RA He Y., Tang W., Swain J.D., Green A.L., Jack T.P., Gan S.;
RT "Networking senescence-regulating pathways by using Arabidopsis enhancer
RT trap lines.";
RL Plant Physiol. 126:707-716(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION
RP BY ABSCISIC ACID.
RX PubMed=15159630; DOI=10.1023/b:plan.0000028730.10834.e3;
RA He Y., Gan S.;
RT "A novel zinc-finger protein with a proline-rich domain mediates ABA-
RT regulated seed dormancy in Arabidopsis.";
RL Plant Mol. Biol. 54:1-9(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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].
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 [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 INDUCTION BY ERF114.
RX PubMed=23616605; DOI=10.1104/pp.113.214049;
RA Mehrnia M., Balazadeh S., Zanor M.I., Mueller-Roeber B.;
RT "EBE, an AP2/ERF transcription factor highly expressed in proliferating
RT cells, affects shoot architecture in Arabidopsis.";
RL Plant Physiol. 162:842-857(2013).
RN [8]
RP GENE FAMILY, INTERACTION WITH KIN10 AND KIN11, AND FUNCTION.
RX PubMed=24600465; DOI=10.3389/fpls.2014.00054;
RA Nietzsche M., Schiessl I., Boernke F.;
RT "The complex becomes more complex: protein-protein interactions of SnRK1
RT with DUF581 family proteins provide a framework for cell- and stimulus
RT type-specific SnRK1 signaling in plants.";
RL Front. Plant Sci. 5:54-54(2014).
RN [9]
RP ERRATUM OF PUBMED:24600465.
RX PubMed=25544057; DOI=10.3389/fpls.2014.00693;
RA Boernke F.;
RT "Corrigendum: The complex becomes more complex: protein-protein
RT interactions of SnRK1 with DUF581 family proteins provide a framework for
RT cell- and stimulus type-specific SnRK1 signaling in plants.";
RL Front. Plant Sci. 5:693-693(2014).
RN [10]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=24901469; DOI=10.1371/journal.pone.0099074;
RA Jamsheer K M., Laxmi A.;
RT "DUF581 is plant specific FCS-like zinc finger involved in protein-protein
RT interaction.";
RL PLoS ONE 9:E99074-E99074(2014).
RN [11]
RP INDUCTION.
RX PubMed=26442059; DOI=10.3389/fpls.2015.00746;
RA Jamsheer K M., Laxmi A.;
RT "Expression of Arabidopsis FCS-Like Zinc finger genes is differentially
RT regulated by sugars, cellular energy level, and abiotic stress.";
RL Front. Plant Sci. 6:746-746(2015).
RN [12]
RP INTERACTION WITH KIN10; KIN11; MPK3 AND MPK6.
RX DOI=10.1016/j.cpb.2015.10.004;
RA Nietzsche M., Landgraf R., Tohge T., Boernke F.;
RT "A protein-protein interaction network linking the energy-sensor kinase
RT SnRK1 to multiple signaling pathways in Arabidopsis thaliana.";
RL Curr. Plant Biol. 5:36-44(2016).
RN [13]
RP INTERACTION WITH TZF4; TZF5 AND TZF6, AND SUBCELLULAR LOCATION.
RX PubMed=26978070; DOI=10.1371/journal.pone.0151574;
RA Bogamuwa S., Jang J.C.;
RT "Plant tandem CCCH zinc finger proteins interact with ABA, drought, and
RT stress response regulators in processing-bodies and stress granules.";
RL PLoS ONE 11:E0151574-E0151574(2016).
RN [14]
RP INTERACTION WITH KIN10; KIN11; KINB1 AND KINB2, AND SUBCELLULAR LOCATION.
RX PubMed=29945970; DOI=10.1074/jbc.ra118.002073;
RA Jamsheer K M., Shukla B.N., Jindal S., Gopan N., Mannully C.T., Laxmi A.;
RT "The FCS-like zinc finger scaffold of the kinase SnRK1 is formed by the
RT coordinated actions of the FLZ domain and intrinsically disordered
RT regions.";
RL J. Biol. Chem. 293:13134-13150(2018).
CC -!- FUNCTION: May act as an adapter to facilitate the interaction of SnRK1
CC complex with effector proteins, conferring tissue- and stimulus-type
CC specific differences in the SnRK1 regulation pathway (PubMed:24600465).
CC Involved in seed dormancy control (PubMed:15159630).
CC {ECO:0000269|PubMed:15159630, ECO:0000269|PubMed:24600465}.
CC -!- SUBUNIT: Interacts with KIN10 and KIN11 via its FLZ-type zinc finger
CC domain (PubMed:24600465, Ref.12, PubMed:29945970). Interacts with KINB1
CC and KINB2 via its N-terminal part (PubMed:29945970). Interacts with
CC TZF4, TZF5 and TZF6 (PubMed:26978070). Interacts with MPK3 and MPK6
CC (Ref.12). {ECO:0000269|PubMed:24600465, ECO:0000269|PubMed:26978070,
CC ECO:0000269|PubMed:29945970, ECO:0000269|Ref.12}.
CC -!- INTERACTION:
CC Q8LGS1; Q39021: MPK1; NbExp=5; IntAct=EBI-4443654, EBI-1238932;
CC Q8LGS1; Q39023: MPK3; NbExp=4; IntAct=EBI-4443654, EBI-349526;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:26978070}. Cytoplasm, P-body
CC {ECO:0000269|PubMed:26978070, ECO:0000269|PubMed:29945970}.
CC -!- DEVELOPMENTAL STAGE: Expressed at very low levels during early stages
CC of leaf development, but up-regulated during leaf senescence.
CC {ECO:0000269|PubMed:11402199}.
CC -!- INDUCTION: Up-regulated by abscisic acid (PubMed:11402199,
CC PubMed:15159630). Down-regulated by the transcription factor ERF114
CC (PubMed:23616605). Down-regulated by glucose, sucrose and mannose
CC (PubMed:26442059). Induced by abscissic acid (ABA) (PubMed:26442059).
CC {ECO:0000269|PubMed:11402199, ECO:0000269|PubMed:15159630,
CC ECO:0000269|PubMed:23616605, ECO:0000269|PubMed:26442059}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but reduced dormancy and
CC fast germination of the seeds. Strong resistance of the seeds to
CC abscisic acid. {ECO:0000269|PubMed:15159630}.
CC -!- SIMILARITY: Belongs to the FLZ family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM65522.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB86422.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY043289; AAK92226.1; -; mRNA.
DR EMBL; AL138648; CAB86422.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE80448.1; -; Genomic_DNA.
DR EMBL; AY065175; AAL38351.1; -; mRNA.
DR EMBL; AY081561; AAM10123.1; -; mRNA.
DR EMBL; AY087975; AAM65522.1; ALT_INIT; mRNA.
DR PIR; T48110; T48110.
DR RefSeq; NP_567143.1; NM_116186.4.
DR AlphaFoldDB; Q8LGS1; -.
DR IntAct; Q8LGS1; 11.
DR STRING; 3702.AT3G63210.1; -.
DR PaxDb; Q8LGS1; -.
DR PRIDE; Q8LGS1; -.
DR ProteomicsDB; 238514; -.
DR EnsemblPlants; AT3G63210.1; AT3G63210.1; AT3G63210.
DR GeneID; 825496; -.
DR Gramene; AT3G63210.1; AT3G63210.1; AT3G63210.
DR KEGG; ath:AT3G63210; -.
DR Araport; AT3G63210; -.
DR TAIR; locus:2077284; AT3G63210.
DR eggNOG; ENOG502QS8T; Eukaryota.
DR OMA; THIYGSC; -.
DR OrthoDB; 1206171at2759; -.
DR PhylomeDB; Q8LGS1; -.
DR PRO; PR:Q8LGS1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LGS1; baseline and differential.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009749; P:response to glucose; IEP:UniProtKB.
DR GO; GO:1905582; P:response to mannose; IEP:UniProtKB.
DR GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
DR GO; GO:0010162; P:seed dormancy process; IMP:TAIR.
DR InterPro; IPR044593; FLZ8/MARD1.
DR InterPro; IPR007650; Zf-FLZ_dom.
DR PANTHER; PTHR46443; PTHR46443; 1.
DR Pfam; PF04570; zf-FLZ; 1.
DR PROSITE; PS51795; ZF_FLZ; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..263
FT /note="Protein MARD1"
FT /id="PRO_0000436085"
FT ZN_FING 219..263
FT /note="FLZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01131"
FT CONFLICT 30
FT /note="N -> D (in Ref. 2; AAK92226 and 6; AAM65522)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="P -> R (in Ref. 6; AAM65522)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 29534 MW; C872AA3B683F970B CRC64;
MLRNKPRAAV TTKKQTSLLM ADQPPPPKPN TCHCSPSLFS SPKFRFFTSK MMMTPFDSDF
SLVSPTSILE ANPSIFSSKN PKPVSYFEPT IPNPQRFHSP DVFGLADLVK DGDSNRDHSR
KPVNKMVLFG SKLRVQIPSS ADFGTKTGIR YPPCQLSPCV QTKVLAVSEI DQTEDYTRVI
SHGPNPTITH IFDNSVFVEA TPCSVPLPQP AMETKSTESF LSRCFTCKKN LDQKQDIYIY
RGEKGFCSSE CRYQEMLLDQ MET
