SRM1_ARATH
ID SRM1_ARATH Reviewed; 298 AA.
AC Q9FNN6;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Transcription factor SRM1 {ECO:0000305};
DE AltName: Full=Myb-related protein SRM1 {ECO:0000305};
DE AltName: Full=Protein SALT-RELATED MYB 1 {ECO:0000303|PubMed:26243618};
GN Name=SRM1 {ECO:0000303|PubMed:26243618};
GN OrderedLocusNames=At5g08520 {ECO:0000312|Araport:AT5G08520};
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], INDUCTION BY SALICYLIC ACID AND GIBBERELLIC
RP ACID, AND GENE FAMILY.
RX PubMed=16463103; DOI=10.1007/s11103-005-2910-y;
RA Chen Y., Yang X., He K., Liu M., Li J., Gao Z., Lin Z., Zhang Y., Wang X.,
RA Qiu X., Shen Y., Zhang L., Deng X., Luo J., Deng X.-W., Chen Z., Gu H.,
RA Qu L.-J.;
RT "The MYB transcription factor superfamily of Arabidopsis: expression
RT analysis and phylogenetic comparison with the rice MYB family.";
RL Plant Mol. Biol. 60:107-124(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION BY DEHYDRATION AND SALT STRESS.
RC STRAIN=cv. Columbia;
RX PubMed=26243618; DOI=10.1104/pp.15.00962;
RA Wang T., Tohge T., Ivakov A., Mueller-Roeber B., Fernie A.R., Mutwil M.,
RA Schippers J.H., Persson S.;
RT "Salt-related MYB1 coordinates abscisic acid biosynthesis and signaling
RT during salt stress in Arabidopsis.";
RL Plant Physiol. 169:1027-1041(2015).
CC -!- FUNCTION: Transcription activator that coordinates abscisic acid (ABA)
CC biosynthesis and signaling-related genes via binding to the specific
CC promoter motif 5'-(A/T)AACCAT-3'. Represses ABA-mediated salt (e.g.
CC NaCl and KCl) stress tolerance. Regulates leaf shape and promotes
CC vegetative growth. {ECO:0000269|PubMed:26243618}.
CC -!- INTERACTION:
CC Q9FNN6; P94077: LSD1; NbExp=5; IntAct=EBI-15195055, EBI-5849461;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624,
CC ECO:0000269|PubMed:26243618}.
CC -!- TISSUE SPECIFICITY: Expressed in young seedlings, developing leaves,
CC sepals and trichomes. {ECO:0000269|PubMed:26243618}.
CC -!- INDUCTION: Induced by salicylic acid (SA) and gibberellic acid (GA)
CC (PubMed:16463103). Triggered by dehydration and salt stress
CC (PubMed:26243618). {ECO:0000269|PubMed:16463103,
CC ECO:0000269|PubMed:26243618}.
CC -!- DISRUPTION PHENOTYPE: Increased tolerance to salt stress leading to
CC better seedling survival and enhanced seed germination on NaCl- and
CC KCl-containing medium, due to a reduced sensitivity to and reduced
CC levels of abscisic acid (ABA), as well as a reduced induction of
CC stress-related genes. Altered leaf morphology, both in shape and in
CC size. {ECO:0000269|PubMed:26243618}.
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DR EMBL; AY519532; AAS10002.1; -; mRNA.
DR EMBL; AB006697; BAB10001.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91314.1; -; Genomic_DNA.
DR EMBL; AY072090; AAL59913.1; -; mRNA.
DR EMBL; AY096571; AAM20221.1; -; mRNA.
DR RefSeq; NP_196469.1; NM_120937.5.
DR AlphaFoldDB; Q9FNN6; -.
DR IntAct; Q9FNN6; 4.
DR STRING; 3702.AT5G08520.1; -.
DR iPTMnet; Q9FNN6; -.
DR PaxDb; Q9FNN6; -.
DR PRIDE; Q9FNN6; -.
DR ProteomicsDB; 226732; -.
DR EnsemblPlants; AT5G08520.1; AT5G08520.1; AT5G08520.
DR GeneID; 830751; -.
DR Gramene; AT5G08520.1; AT5G08520.1; AT5G08520.
DR KEGG; ath:AT5G08520; -.
DR Araport; AT5G08520; -.
DR TAIR; locus:2159607; AT5G08520.
DR eggNOG; KOG0724; Eukaryota.
DR HOGENOM; CLU_060837_2_0_1; -.
DR InParanoid; Q9FNN6; -.
DR OMA; GFELMAV; -.
DR OrthoDB; 1106382at2759; -.
DR PhylomeDB; Q9FNN6; -.
DR PRO; PR:Q9FNN6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNN6; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:1901001; P:negative regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0010116; P:positive regulation of abscisic acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:1905615; P:positive regulation of developmental vegetative growth; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0009787; P:regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:1901371; P:regulation of leaf morphogenesis; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0009739; P:response to gibberellin; IEP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR CDD; cd00167; SANT; 2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR006447; Myb_dom_plants.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR Pfam; PF00249; Myb_DNA-binding; 2.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; SSF46689; 2.
DR TIGRFAMs; TIGR01557; myb_SHAQKYF; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Activator; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..298
FT /note="Transcription factor SRM1"
FT /id="PRO_0000438822"
FT DOMAIN 7..62
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 111..168
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 140..164
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 68..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 298 AA; 31814 MW; 1D8C2130B2571A5B CRC64;
MTVEEVSDGS VWSREDDIAF ERALANNTDE SEERWEKIAA DVPGKSVEQI KEHYELLVED
VTRIESGCVP LPAYGSPEGS NGHAGDEGAS SKKGGNSHAG ESNQAGKSKS DQERRKGIAW
TEDEHRLFLL GLDKYGKGDW RSISRNFVVT RTPTQVASHA QKYFIRLNSM NKDRRRSSIH
DITSVGNADV STPQGPITGQ NNSNNNNNNN NNNSSPAVAG GGNKSAKQAV SQAPPGPPMY
GTPAIGQPAV GTPVNLPAPP HMAYGVHAAP VPGSVVPGAA MNIGQMPYTM PRTPTAHR
