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AGL80_ARATH
ID   AGL80_ARATH             Reviewed;         321 AA.
AC   Q9FJK3;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Agamous-like MADS-box protein AGL80;
GN   Name=AGL80; Synonyms=FEM111; OrderedLocusNames=At5g48670;
GN   ORFNames=K15N18.16;
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], FUNCTION, MUTANT FEM111, TISSUE SPECIFICITY,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=16798889; DOI=10.1105/tpc.106.040824;
RA   Portereiko M.F., Lloyd A., Steffen J.G., Punwani J.A., Otsuga D.,
RA   Drews G.N.;
RT   "AGL80 is required for central cell and endosperm development in
RT   Arabidopsis.";
RL   Plant Cell 18:1862-1872(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA   Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT   features of the regions of 1,013,767 bp covered by sixteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:297-308(1998).
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;
RA   Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA   Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INTERACTION WITH AGL62.
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   [6]
RP   INTERACTION WITH AGL61.
RX   PubMed=18713950; DOI=10.1105/tpc.108.058958;
RA   Bemer M., Wolters-Arts M., Grossniklaus U., Angenent G.C.;
RT   "The MADS domain protein DIANA acts together with AGAMOUS-LIKE80 to specify
RT   the central cell in Arabidopsis ovules.";
RL   Plant Cell 20:2088-2101(2008).
RN   [7]
RP   INTERACTION WITH AGL61.
RX   PubMed=18599653; DOI=10.1104/pp.108.119404;
RA   Steffen J.G., Kang I.-H., Portereiko M.F., Lloyd A., Drews G.N.;
RT   "AGL61 interacts with AGL80 and is required for central cell development in
RT   Arabidopsis.";
RL   Plant Physiol. 148:259-268(2008).
RN   [8]
RP   INTERACTION WITH AGL62.
RX   PubMed=18334668; DOI=10.1105/tpc.107.055137;
RA   Kang I.-H., Steffen J.G., Portereiko M.F., Lloyd A., Drews G.N.;
RT   "The AGL62 MADS domain protein regulates cellularization during endosperm
RT   development in Arabidopsis.";
RL   Plant Cell 20:635-647(2008).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH ME14/CBP1.
RX   PubMed=26462908; DOI=10.1105/tpc.15.00370;
RA   Li H.J., Zhu S.S., Zhang M.X., Wang T., Liang L., Xue Y., Shi D.Q., Liu J.,
RA   Yang W.C.;
RT   "Arabidopsis CBP1 is a novel regulator of transcription initiation in
RT   central cell-mediated pollen tube guidance.";
RL   Plant Cell 27:2880-2893(2015).
CC   -!- FUNCTION: Probable transcription factor. Controls central cell
CC       differentiation during female gametophyte development. Required for the
CC       expression of DEMETER and DD46, but not for the expression of FIS2
CC       (PubMed:16798889). Probable transcription factor that may function in
CC       the maintenance of the proper function of the central cell in pollen
CC       tube attraction (Probable). {ECO:0000269|PubMed:16798889,
CC       ECO:0000305|PubMed:26462908}.
CC   -!- SUBUNIT: Interacts with AGL61 and AGL62. Forms a heterodimer with AGL61
CC       (PubMed:15805477, PubMed:18334668, PubMed:18599653, PubMed:18713950).
CC       Interacts with MEE14/CBP1 (PubMed:26462908).
CC       {ECO:0000269|PubMed:15805477, ECO:0000269|PubMed:18334668,
CC       ECO:0000269|PubMed:18599653, ECO:0000269|PubMed:18713950,
CC       ECO:0000269|PubMed:26462908}.
CC   -!- INTERACTION:
CC       Q9FJK3; Q4PSU4: AGL61; NbExp=4; IntAct=EBI-622424, EBI-1237976;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251,
CC       ECO:0000269|PubMed:16798889}.
CC   -!- TISSUE SPECIFICITY: Expressed in the central cell of the female
CC       gametophyte and in early endosperm. Also detected in ovaries, young
CC       siliques, roots, leaves, stems, young flowers and anthers.
CC       {ECO:0000269|PubMed:16798889}.
CC   -!- MISCELLANEOUS: Plants lacking AGL80 (mutant fem111) have defects in
CC       central cell and endosperm development.
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DR   EMBL; DQ406752; ABD66036.1; -; mRNA.
DR   EMBL; AB015468; BAB10700.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95709.1; -; Genomic_DNA.
DR   EMBL; DQ056710; AAY78856.1; -; mRNA.
DR   RefSeq; NP_199678.1; NM_124244.3.
DR   AlphaFoldDB; Q9FJK3; -.
DR   SMR; Q9FJK3; -.
DR   BioGRID; 20171; 13.
DR   IntAct; Q9FJK3; 12.
DR   STRING; 3702.AT5G48670.1; -.
DR   PaxDb; Q9FJK3; -.
DR   PRIDE; Q9FJK3; -.
DR   EnsemblPlants; AT5G48670.1; AT5G48670.1; AT5G48670.
DR   GeneID; 834925; -.
DR   Gramene; AT5G48670.1; AT5G48670.1; AT5G48670.
DR   KEGG; ath:AT5G48670; -.
DR   Araport; AT5G48670; -.
DR   TAIR; locus:2152511; AT5G48670.
DR   eggNOG; KOG0014; Eukaryota.
DR   HOGENOM; CLU_053053_7_1_1; -.
DR   InParanoid; Q9FJK3; -.
DR   OMA; WFMEMMN; -.
DR   OrthoDB; 1315166at2759; -.
DR   PhylomeDB; Q9FJK3; -.
DR   PRO; PR:Q9FJK3; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FJK3; baseline and differential.
DR   Genevisible; Q9FJK3; AT.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0043078; C:polar 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:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
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; 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   Coiled coil; DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..321
FT                   /note="Agamous-like MADS-box protein AGL80"
FT                   /id="PRO_0000363651"
FT   DOMAIN          1..61
FT                   /note="MADS-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT   COILED          89..114
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   321 AA;  36825 MW;  32026DC47F1B3241 CRC64;
     MTRKKVKLAY ISNDSSRKAT FKKRKKGLMK KVHELSTLCG ITACAIIYSP YDTNPEVWPS
     NSGVQRVVSE FRTLPEMDQH KKMVDQEGFL KQRIAKATET LRRQRKDSRE LEMTEVMFQC
     LIGNMEMFHL NIVDLNDLGY MIEQYLKDVN RRIEILRNSG TEIGESSSVA VAASEGNIPM
     PNLVATTAPT TTIYEVGSSS SFAAVANFVN PIDLQQFRHP AAQHVGLNEQ PQNLNLNLNQ
     NYNQNQEWFM EMMNHPEQMR YQTEQMGYQF MDDNHHNHIH HQPQEHQHQI HDESSNALDA
     ANSSSIIPVT SSSITNKTWF H
 
 
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