ID   AGL30_ARATH             Reviewed;         386 AA.
AC   Q1PFA4; A0MEI3; O80619;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Agamous-like MADS-box protein AGL30 {ECO:0000305};
GN   Name=AGL30 {ECO:0000303|PubMed:12837945};
GN   OrderedLocusNames=At2g03060 {ECO:0000312|Araport:AT2G03060};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=12949148; DOI=10.1093/molbev/msg216;
RA   Kofuji R., Sumikawa N., Yamasaki M., Kondo K., Ueda K., Ito M., Hasebe M.;
RT   "Evolution and divergence of the MADS-box gene family based on genome-wide
RT   expression analyses.";
RL   Mol. Biol. Evol. 20:1963-1977(2003).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12837945; DOI=10.1105/tpc.011544;
RA   Parenicova L., de Folter S., Kieffer M., Horner D.S., Favalli C.,
RA   Busscher J., Cook H.E., Ingram R.M., Kater M.M., Davies B., Angenent G.C.,
RA   Colombo L.;
RT   "Molecular and phylogenetic analyses of the complete MADS-box transcription
RT   factor family in Arabidopsis: new openings to the MADS world.";
RL   Plant Cell 15:1538-1551(2003).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH AGL66 AND AGL104.
RX   PubMed=19211705; DOI=10.1104/pp.109.135806;
RA   Adamczyk B.J., Fernandez D.E.;
RT   "MIKC* MADS domain heterodimers are required for pollen maturation and tube
RT   growth in Arabidopsis.";
RL   Plant Physiol. 149:1713-1723(2009).
CC   -!- FUNCTION: Probable transcription factor that forms heterodimers with
CC       the MADS-box proteins AGL66 and AGL104 and is involved in the
CC       regulation of pollen maturation at the late stages of pollen
CC       development and pollen tube growth. {ECO:0000269|PubMed:19211705}.
CC   -!- SUBUNIT: Forms heterodimers with AGL66 and AGL104.
CC       {ECO:0000269|PubMed:19211705}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences. {ECO:0000305};
CC       Name=1;
CC         IsoId=Q1PFA4-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in pollen. {ECO:0000269|PubMed:12949148}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC32924.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=ABK28481.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC004138; AAC32924.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC05661.1; -; Genomic_DNA.
DR   EMBL; DQ446459; ABE65796.1; -; mRNA.
DR   EMBL; DQ652954; ABK28481.1; ALT_SEQ; mRNA.
DR   PIR; H84443; H84443.
DR   RefSeq; NP_001318187.1; NM_001335152.1. [Q1PFA4-1]
DR   AlphaFoldDB; Q1PFA4; -.
DR   SMR; Q1PFA4; -.
DR   IntAct; Q1PFA4; 1.
DR   STRING; 3702.AT2G03060.2; -.
DR   PaxDb; Q1PFA4; -.
DR   ProteomicsDB; 244757; -. [Q1PFA4-1]
DR   EnsemblPlants; AT2G03060.2; AT2G03060.2; AT2G03060. [Q1PFA4-1]
DR   GeneID; 814835; -.
DR   Gramene; AT2G03060.2; AT2G03060.2; AT2G03060. [Q1PFA4-1]
DR   KEGG; ath:AT2G03060; -.
DR   Araport; AT2G03060; -.
DR   TAIR; locus:2056760; AT2G03060.
DR   eggNOG; KOG0014; Eukaryota.
DR   HOGENOM; CLU_034796_0_0_1; -.
DR   InParanoid; Q1PFA4; -.
DR   OrthoDB; 961118at2759; -.
DR   PhylomeDB; Q1PFA4; -.
DR   PRO; PR:Q1PFA4; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q1PFA4; baseline and differential.
DR   Genevisible; Q1PFA4; AT.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0009555; P:pollen development; IGI:TAIR.
DR   GO; GO:0010152; P:pollen maturation; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0080092; P:regulation of pollen tube growth; IMP:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd00266; MADS_SRF_like; 1.
DR   Gene3D; 3.40.1810.10; -; 1.
DR   InterPro; IPR033897; MADS_SRF-like.
DR   InterPro; IPR002100; TF_MADSbox.
DR   InterPro; IPR036879; TF_MADSbox_sf.
DR   Pfam; PF00319; SRF-TF; 1.
DR   PRINTS; PR00404; MADSDOMAIN.
DR   SMART; SM00432; MADS; 1.
DR   SUPFAM; SSF55455; SSF55455; 1.
DR   PROSITE; PS50066; MADS_BOX_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..386
FT                   /note="Agamous-like MADS-box protein AGL30"
FT                   /id="PRO_0000433966"
FT   DOMAIN          1..53
FT                   /note="MADS-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT   REGION          341..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   386 AA;  43789 MW;  4817C1564A1F2E4B CRC64;
     MGRVKLKIKK LENTNGRQST FAKRKNGILK KANELSILCD IDIVLLMFSP TGKAAICCGT
     RSSMEEVIAK FSQVTPQERT KRKFESLENL KKTFQKLDHD VNIREFIASS NSTVEDLSTQ
     ARILQARISE IHGRLSYWTE PDKINNVEHL GQLEISIRQS LDQLRAHKEH FGQQQQAMQI
     ENANFVKDWS TCSMQDGIQI PLEQQLQSMS WILNSNTTNI VTEEHNSIPQ REVECSASSS
     FGSYPGYFGT GKSPEMTIPG QETSFLDELN TGQLKQDTSS QQQFTNNNNI TAYNPNLHND
     MNHHQTLPPP PLPLTLPHAQ VYIPMNQREY HMNGFFEAPP PDSSAYNDNT NQTRFGSSSS
     SLPCSISMFD EYLFSQVTKT KLSQRF