AML1_ARATH
ID AML1_ARATH Reviewed; 915 AA.
AC Q8W4I9; O23866;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Protein MEI2-like 1;
DE Short=AML1;
DE AltName: Full=MEI2-like protein 1;
GN Name=ML1; OrderedLocusNames=At5g61960; ORFNames=K22G18.9;
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 TISSUE SPECIFICITY.
RX PubMed=9287109; DOI=10.1016/s0014-5793(97)00871-5;
RA Hirayama T., Ishida C., Kuromori T., Obata S., Shimoda C., Yamamoto M.,
RA Shinozaki K., Ohto C.;
RT "Functional cloning of a cDNA encoding Mei2-like protein from Arabidopsis
RT thaliana using a fission yeast pheromone receptor deficient mutant.";
RL FEBS Lett. 413:16-20(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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;
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 GENE FAMILY, AND DEVELOPMENTAL STAGE.
RX PubMed=15356386; DOI=10.1023/b:plan.0000040819.33383.b6;
RA Anderson G.H., Alvarez N.D., Gilman C., Jeffares D.C., Trainor V.C.,
RA Hanson M.R., Veit B.;
RT "Diversification of genes encoding mei2 -like RNA binding proteins in
RT plants.";
RL Plant Mol. Biol. 54:653-670(2004).
RN [7]
RP FUNCTION, INTERACTION WITH RAPTOR1, AND DISRUPTION PHENOTYPE.
RX PubMed=15720729; DOI=10.1186/1471-2229-5-2;
RA Anderson G.H., Hanson M.R.;
RT "The Arabidopsis Mei2 homologue AML1 binds AtRaptor1B, the plant homologue
RT of a major regulator of eukaryotic cell growth.";
RL BMC Plant Biol. 5:2-2(2005).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16473967; DOI=10.1105/tpc.105.039156;
RA Kaur J., Sebastian J., Siddiqi I.;
RT "The Arabidopsis-mei2-like genes play a role in meiosis and vegetative
RT growth in Arabidopsis.";
RL Plant Cell 18:545-559(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Probable RNA-binding transcriptional activator that plays a
CC role in meiosis and vegetative growth. May be a downstream effector of
CC TOR signaling pathway and recruited by RAPTOR1 for TOR substrate.
CC {ECO:0000269|PubMed:15720729, ECO:0000269|PubMed:16473967}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:16473967, ECO:0000269|PubMed:9287109}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryo at the heart and torpedo
CC stages. Weakly expressed throughout the vegetative shoot apex. Highly
CC expressed in organogenic regions of floral apices.
CC {ECO:0000269|PubMed:15356386}.
CC -!- DISRUPTION PHENOTYPE: Early flowering. {ECO:0000269|PubMed:15720729}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA22374.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB08883.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D86122; BAA22374.1; ALT_SEQ; mRNA.
DR EMBL; AB022212; BAB08883.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP002688; AED97542.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97543.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69060.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69062.1; -; Genomic_DNA.
DR EMBL; AY062536; AAL32614.1; -; mRNA.
DR EMBL; BT008806; AAP68245.1; -; mRNA.
DR EMBL; AK316683; BAH19410.1; -; mRNA.
DR RefSeq; NP_001032122.1; NM_001037045.1.
DR RefSeq; NP_001318861.1; NM_001345511.1.
DR RefSeq; NP_001330765.1; NM_001345512.1.
DR RefSeq; NP_568946.1; NM_125589.5.
DR AlphaFoldDB; Q8W4I9; -.
DR SMR; Q8W4I9; -.
DR BioGRID; 21561; 1.
DR IntAct; Q8W4I9; 1.
DR STRING; 3702.AT5G61960.1; -.
DR iPTMnet; Q8W4I9; -.
DR PaxDb; Q8W4I9; -.
DR PRIDE; Q8W4I9; -.
DR ProteomicsDB; 244401; -.
DR EnsemblPlants; AT5G61960.1; AT5G61960.1; AT5G61960.
DR EnsemblPlants; AT5G61960.10; AT5G61960.10; AT5G61960.
DR EnsemblPlants; AT5G61960.2; AT5G61960.2; AT5G61960.
DR EnsemblPlants; AT5G61960.3; AT5G61960.3; AT5G61960.
DR GeneID; 836317; -.
DR Gramene; AT5G61960.1; AT5G61960.1; AT5G61960.
DR Gramene; AT5G61960.10; AT5G61960.10; AT5G61960.
DR Gramene; AT5G61960.2; AT5G61960.2; AT5G61960.
DR Gramene; AT5G61960.3; AT5G61960.3; AT5G61960.
DR KEGG; ath:AT5G61960; -.
DR Araport; AT5G61960; -.
DR TAIR; locus:2156166; AT5G61960.
DR eggNOG; KOG4660; Eukaryota.
DR HOGENOM; CLU_012447_1_0_1; -.
DR InParanoid; Q8W4I9; -.
DR OrthoDB; 1464915at2759; -.
DR PhylomeDB; Q8W4I9; -.
DR PRO; PR:Q8W4I9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8W4I9; baseline and differential.
DR Genevisible; Q8W4I9; AT.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR CDD; cd12524; RRM1_MEI2_like; 1.
DR CDD; cd12531; RRM3_MEI2_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034453; MEI2-like_RRM1.
DR InterPro; IPR034454; MEI2-like_RRM3.
DR InterPro; IPR007201; Mei2-like_Rrm_C.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR Pfam; PF04059; RRM_2; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Activator; Meiosis; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..915
FT /note="Protein MEI2-like 1"
FT /id="PRO_0000409341"
FT DOMAIN 217..290
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 302..375
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 915 AA; 100788 MW; AECFBDC1F0154570 CRC64;
MPSDIMEQRG VSTPSHFHED IHITSERQFG FMKTDMMPEN QGGRDRLSSM PKSSWTSESY
QLKPQSSFSG SHPSGSPNAR NTTNGSQWES SLFSSSMSDL FSRKLRLQGS DMLSTMSANT
VVTHREEEPS ESLEEIEAQT IGNLLPDEDD LFAEVTGEVG RKSRANTGDE LDEFDLFSSV
GGMELDGDIF SSVSHRNGER GGNNSVGELN RGEIPSRTLL VGNISSNVED YELKVLFEQF
GDIQALHTAC KNRGFIMVSY CDIRAAQNAA RALQNKLLRG TKLDIRYSIS KENPSQKDTS
KGALLVNNLD SSISNQELNR LVKSYGEVKE IRRTMHDNSQ IYIEFFDVRA AAAALGGLNG
LEVAGKKLQL VPTYPEGTRY TSQCAANDTE GCLPKTSYSN TSSGHIGRHF PGMISSTSSD
GGSMRVIHNS IGSPVNSFIE RHRSLSIPIG FPPSANGISA SKPVGLQEHG HHFDNSNMGI
QSMPNLHPHS FSEYVDNFAN GSPYTSSAFS EMVSDGSKAN EGFMIHNVRG VEGFSGGGIG
SPMHQSSRRP INLWSNSNTQ QQNPSSGMMW PNSPSHINSI PTQRPPVTVF SRAPPIMVNM
ASSPVHHHIG SAPVLNSPFW DRRQAYVAES LESSGFHIGS HGSMGIPGSS PSHPMDIGSH
KTFSVGGNRM DVNSQNAVLR SPQQLSHLFP GRSPMGSMPG SFDSPNERYR NLSHRRSESS
SSNADKKLYE LDVDRILRGE DRRTTLMIKN IPNKYTSKML LSAIDEHCKG TYDFLYLPID
FKNKCNVGYA FINLIEPEKI VPFFKAFNGK KWEKFNSEKV ATLTYARIQG KTALIAHFQN
SSLMNEDKRC RPILFHTDGP NAGDQEPFPM GSNIRSRPGK PRSSSIDNYN SFSISSVSEN
REETPNGTDP FLKEN
