ASHR3_ARATH
ID ASHR3_ARATH Reviewed; 497 AA.
AC Q949T8; O65563;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Histone-lysine N-methyltransferase ASHR3;
DE EC=2.1.1.-;
DE AltName: Full=ASH1-related protein 3;
DE AltName: Full=Protein SET DOMAIN GROUP 4;
DE AltName: Full=Protein stamen loss;
GN Name=ASHR3; Synonyms=SDG4, SET4, SML; OrderedLocusNames=At4g30860;
GN ORFNames=F6I18.230;
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].
RA Cartagena J.A., Matsunaga S., Kurihara D., Fujimoto S., Azumi Y.,
RA Uchiyama S., Fukui K.;
RT "The chromosome-associated protein SML regulates lateral stamen development
RT in Arabidopsis.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NOMENCLATURE.
RX PubMed=11691919; DOI=10.1093/nar/29.21.4319;
RA Baumbusch L.O., Thorstensen T., Krauss V., Fischer A., Naumann K.,
RA Assalkhou R., Schulz I., Reuter G., Aalen R.B.;
RT "The Arabidopsis thaliana genome contains at least 29 active genes encoding
RT SET domain proteins that can be assigned to four evolutionarily conserved
RT classes.";
RL Nucleic Acids Res. 29:4319-4333(2001).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH AMS.
RX PubMed=17978851; DOI=10.1007/s11103-007-9251-y;
RA Thorstensen T., Grini P.E., Mercy I.S., Alm V., Erdal S., Aasland R.,
RA Aalen R.B.;
RT "The Arabidopsis SET-domain protein ASHR3 is involved in stamen development
RT and interacts with the bHLH transcription factor ABORTED MICROSPORES
RT (AMS).";
RL Plant Mol. Biol. 66:47-59(2008).
CC -!- FUNCTION: Histone methyltransferase (By similarity). Involved in stamen
CC development. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00911};
CC -!- SUBUNIT: Interacts with AMS/bHLH21 by its SET domain and PHD finger.
CC {ECO:0000269|PubMed:17978851}.
CC -!- INTERACTION:
CC Q949T8; Q17TI5: BRX; NbExp=3; IntAct=EBI-4457339, EBI-4426649;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17978851}. Chromosome
CC {ECO:0000305|PubMed:17978851}. Note=Associated to the euchromatin.
CC -!- TISSUE SPECIFICITY: Expressed in roots, flowers and buds, the anther
CC and in stamen filaments. {ECO:0000269|PubMed:17978851}.
CC -!- DEVELOPMENTAL STAGE: First observed at low levels in the vasculature
CC and around hydathodes of developing leaves. In flowers, restricted to
CC anthers tapetum at a post-meiosis stage, to filaments, and to
CC microspores during their development. Disappears as pollen matures. In
CC developing roots, expressed throughout the lower part, in the cap, in
CC the epidermis and in non-epidermal tissue in the division and
CC elongation zone. Also detected in cells lining lateral root formation.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00911}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18207.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79804.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB195469; BAD72877.1; -; Genomic_DNA.
DR EMBL; AL022198; CAA18207.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161577; CAB79804.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85821.1; -; Genomic_DNA.
DR EMBL; AY050894; AAK92831.1; -; mRNA.
DR EMBL; AY096675; AAM20309.1; -; mRNA.
DR PIR; C85361; C85361.
DR RefSeq; NP_567859.1; NM_119233.2.
DR AlphaFoldDB; Q949T8; -.
DR SMR; Q949T8; -.
DR BioGRID; 14497; 5.
DR IntAct; Q949T8; 4.
DR STRING; 3702.AT4G30860.1; -.
DR PaxDb; Q949T8; -.
DR PRIDE; Q949T8; -.
DR ProteomicsDB; 246789; -.
DR EnsemblPlants; AT4G30860.1; AT4G30860.1; AT4G30860.
DR GeneID; 829210; -.
DR Gramene; AT4G30860.1; AT4G30860.1; AT4G30860.
DR KEGG; ath:AT4G30860; -.
DR Araport; AT4G30860; -.
DR TAIR; locus:2126714; AT4G30860.
DR eggNOG; KOG1081; Eukaryota.
DR HOGENOM; CLU_020840_10_2_1; -.
DR InParanoid; Q949T8; -.
DR OMA; KCHCGAP; -.
DR OrthoDB; 507784at2759; -.
DR PhylomeDB; Q949T8; -.
DR PRO; PR:Q949T8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q949T8; baseline and differential.
DR Genevisible; Q949T8; AT.
DR GO; GO:0000785; C:chromatin; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR025787; Hist-Lys_N-MeTrfase_SET2_plant.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS51578; SAM_MT43_SET2_2; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Developmental protein; Metal-binding;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..497
FT /note="Histone-lysine N-methyltransferase ASHR3"
FT /id="PRO_0000233376"
FT DOMAIN 283..326
FT /note="AWS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT DOMAIN 326..443
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 449..465
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT ZN_FING 118..186
FT /note="PHD-type"
SQ SEQUENCE 497 AA; 56122 MW; 10D9C7EC779C2108 CRC64;
MLDLGNMSMS ASVALTCCPS FLPAASGPEL AKSINSPENL AGECNGKHLP MIPPEEEVKD
IKIANGVTAF TRKQNPSDRV KKGFVLDDHV KDWVKRRVAS GVSESTCFLP FLVGAKKMVD
CLVCHKPVYP GEDLSCSVRG CQGAYHSLCA KESLGFSKSS KFKCPQHECF VCKQRTQWRC
VKCPMAAHDK HSPWSKEILH LKDQPGRAVC WRHPTDWRLD TKHAVAQSEI EEVFCQLPLP
YVEEEFKIDL AWKDSVVKED PPSYVHIRRN IYLVKKKRDN ANDGVGCTNC GPNCDRSCVC
RVQCISCSKG CSCPESCGNR PFRKEKKIKI VKTEHCGWGV EAAESINKED FIVEYIGEVI
SDAQCEQRLW DMKHKGMKDF YMCEIQKDFT IDATFKGNAS RFLNHSCNPN CVLEKWQVEG
ETRVGVFAAR QIEAGEPLTY DYRFVQFGPE VKCNCGSENC QGYLGTKRKE PNCLVVSWGA
KRRRLFHRPI ARKPQQD
