ID   AGL21_ARATH             Reviewed;         228 AA.
AC   Q9SZJ6; Q548I8;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Agamous-like MADS-box protein AGL21;
GN   Name=AGL21; OrderedLocusNames=At4g37940; ORFNames=F20D10.60;
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], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia; TISSUE=Root;
RX   PubMed=11855641; DOI=10.1007/s004250100637;
RA   Burgeff C., Liljegren S.J., Tapia-Lopez R., Yanofsky M.F.,
RA   Alvarez-Buylla E.R.;
RT   "MADS-box gene expression in lateral primordia, meristems and
RT   differentiated tissues of Arabidopsis thaliana roots.";
RL   Planta 214:365-372(2002).
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   INTERACTION WITH AGL15; AGL16 AND AGL19.
RX   PubMed=15805477; DOI=10.1105/tpc.105.031831;
RA   de Folter S., Immink R.G.H., Kieffer M., Parenicova L., Henz S.R.,
RA   Weigel D., Busscher M., Kooiker M., Colombo L., Kater M.M., Davies B.,
RA   Angenent G.C.;
RT   "Comprehensive interaction map of the Arabidopsis MADS Box transcription
RT   factors.";
RL   Plant Cell 17:1424-1433(2005).
RN   [5]
RP   INTERACTION WITH SIEL.
RX   PubMed=21924907; DOI=10.1016/j.cub.2011.08.013;
RA   Koizumi K., Wu S., MacRae-Crerar A., Gallagher K.L.;
RT   "An essential protein that interacts with endosomes and promotes movement
RT   of the SHORT-ROOT transcription factor.";
RL   Curr. Biol. 21:1559-1564(2011).
CC   -!- FUNCTION: Probable transcription factor.
CC   -!- SUBUNIT: Interacts with AGL15, AGL16 and AGL19 (PubMed:15805477).
CC       Interacts with SIEL (PubMed:21924907). {ECO:0000269|PubMed:15805477,
CC       ECO:0000269|PubMed:21924907}.
CC   -!- INTERACTION:
CC       Q9SZJ6; P29381: AGL1; NbExp=4; IntAct=EBI-621986, EBI-592304;
CC       Q9SZJ6; Q38841: AGL12; NbExp=4; IntAct=EBI-621986, EBI-621976;
CC       Q9SZJ6; Q38847: AGL15; NbExp=5; IntAct=EBI-621986, EBI-622076;
CC       Q9SZJ6; A2RVQ5: AGL16; NbExp=5; IntAct=EBI-621986, EBI-621930;
CC       Q9SZJ6; Q38840: AGL17; NbExp=4; IntAct=EBI-621986, EBI-622087;
CC       Q9SZJ6; O82794: AGL24; NbExp=4; IntAct=EBI-621986, EBI-592083;
CC       Q9SZJ6; Q9FIS1: AGL42; NbExp=4; IntAct=EBI-621986, EBI-622017;
CC       Q9SZJ6; P29385: AGL5; NbExp=4; IntAct=EBI-621986, EBI-621949;
CC       Q9SZJ6; Q9SI38: ANR1; NbExp=4; IntAct=EBI-621986, EBI-622096;
CC       Q9SZJ6; P35631: AP1; NbExp=4; IntAct=EBI-621986, EBI-592003;
CC       Q9SZJ6; O80438: MAK3; NbExp=3; IntAct=EBI-621986, EBI-15205450;
CC       Q9SZJ6; Q9FVC1: SVP; NbExp=5; IntAct=EBI-621986, EBI-592058;
CC       Q9SZJ6; Q8LPR5: TCP4; NbExp=3; IntAct=EBI-621986, EBI-15192325;
CC       Q9SZJ6; Q9ZSI7: WRKY47; NbExp=3; IntAct=EBI-621986, EBI-2367993;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in root.
CC       {ECO:0000269|PubMed:11855641}.
CC   -!- DEVELOPMENTAL STAGE: Primarily expressed during lateral root formation
CC       and embryogenesis. {ECO:0000269|PubMed:11855641}.
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DR   EMBL; AF336979; AAL73213.1; -; mRNA.
DR   EMBL; AL035538; CAB37534.1; -; Genomic_DNA.
DR   EMBL; AL161592; CAB80459.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86856.1; -; Genomic_DNA.
DR   PIR; T05621; T05621.
DR   RefSeq; NP_195507.1; NM_119955.3.
DR   AlphaFoldDB; Q9SZJ6; -.
DR   SMR; Q9SZJ6; -.
DR   BioGRID; 15231; 41.
DR   IntAct; Q9SZJ6; 41.
DR   STRING; 3702.AT4G37940.1; -.
DR   PaxDb; Q9SZJ6; -.
DR   PRIDE; Q9SZJ6; -.
DR   ProteomicsDB; 244688; -.
DR   EnsemblPlants; AT4G37940.1; AT4G37940.1; AT4G37940.
DR   GeneID; 829950; -.
DR   Gramene; AT4G37940.1; AT4G37940.1; AT4G37940.
DR   KEGG; ath:AT4G37940; -.
DR   Araport; AT4G37940; -.
DR   TAIR; locus:2121070; AT4G37940.
DR   eggNOG; KOG0014; Eukaryota.
DR   HOGENOM; CLU_053053_2_0_1; -.
DR   InParanoid; Q9SZJ6; -.
DR   OMA; QKRYLIH; -.
DR   OrthoDB; 1227337at2759; -.
DR   PhylomeDB; Q9SZJ6; -.
DR   PRO; PR:Q9SZJ6; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SZJ6; baseline and differential.
DR   Genevisible; Q9SZJ6; AT.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd00265; MADS_MEF2_like; 1.
DR   Gene3D; 3.40.1810.10; -; 1.
DR   InterPro; IPR033896; MADS_MEF2-like.
DR   InterPro; IPR002487; TF_Kbox.
DR   InterPro; IPR002100; TF_MADSbox.
DR   InterPro; IPR036879; TF_MADSbox_sf.
DR   Pfam; PF01486; K-box; 1.
DR   Pfam; PF00319; SRF-TF; 1.
DR   PRINTS; PR00404; MADSDOMAIN.
DR   SMART; SM00432; MADS; 1.
DR   SUPFAM; SSF55455; SSF55455; 1.
DR   PROSITE; PS51297; K_BOX; 1.
DR   PROSITE; PS00350; MADS_BOX_1; 1.
DR   PROSITE; PS50066; MADS_BOX_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..228
FT                   /note="Agamous-like MADS-box protein AGL21"
FT                   /id="PRO_0000199479"
FT   DOMAIN          3..57
FT                   /note="MADS-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT   DOMAIN          86..176
FT                   /note="K-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00629"
SQ   SEQUENCE   228 AA;  26411 MW;  87077BFE6CC4F7A6 CRC64;
     MGRGKIVIQR IDDSTSRQVT FSKRRKGLIK KAKELAILCD AEVGLIIFSS TGKLYDFASS
     SMKSVIDRYN KSKIEQQQLL NPASEVKFWQ REAAVLRQEL HALQENHRQM MGEQLNGLSV
     NELNSLENQI EISLRGIRMR KEQLLTQEIQ ELSQKRNLIH QENLDLSRKV QRIHQENVEL
     YKKAYMANTN GFTHREVAVA DDESHTQIRL QLSQPEHSDY DTPPRANE