SEP3_ARATH
ID SEP3_ARATH Reviewed; 251 AA.
AC O22456; Q8GWQ4; Q8L9R5;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Developmental protein SEPALLATA 3;
DE AltName: Full=Agamous-like MADS-box protein AGL9;
GN Name=SEP3; Synonyms=AGL9; OrderedLocusNames=At1g24260; ORFNames=F3I6.19;
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] (ISOFORM 1).
RC STRAIN=cv. Landsberg erecta;
RX AGRICOLA=IND21642003; DOI=10.1007/s004970050116;
RA Mandel M.A., Yanofsky M.F.;
RT "The Arabidopsis AGL9 MADS box gene is expressed in young flower
RT primordia.";
RL Sex. Plant Reprod. 11:22-28(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-251.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP CHARACTERIZATION.
RX PubMed=9418042; DOI=10.1046/j.1365-313x.1997.12050999.x;
RA Fan H.-Y., Hu Y., Tudor M., Ma H.;
RT "Specific interactions between the K domains of AG and AGLs, members of the
RT MADS domain family of DNA binding proteins.";
RL Plant J. 12:999-1010(1997).
RN [7]
RP CHARACTERIZATION, AND DISRUPTION PHENOTYPE.
RX PubMed=10821278; DOI=10.1038/35012103;
RA Pelaz S., Ditta G.S., Baumann E., Wisman E., Yanofsky M.F.;
RT "B and C floral organ identity functions require SEPALLATA MADS-box
RT genes.";
RL Nature 405:200-203(2000).
RN [8]
RP CHARACTERIZATION.
RX PubMed=11206550; DOI=10.1038/35054083;
RA Honma T., Goto K.;
RT "Complexes of MADS-box proteins are sufficient to convert leaves into
RT floral organs.";
RL Nature 409:525-529(2001).
RN [9]
RP FUNCTION, AND INTERACTION WITH TT16/AGL32.
RX PubMed=16080001; DOI=10.1007/s00438-005-0010-y;
RA Kaufmann K., Anfang N., Saedler H., Theissen G.;
RT "Mutant analysis, protein-protein interactions and subcellular localization
RT of the Arabidopsis B sister (ABS) protein.";
RL Mol. Genet. Genomics 274:103-118(2005).
RN [10]
RP INTERACTION WITH AGL16.
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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 75-178, AND HOMODIMERIZATION.
RX PubMed=25228343; DOI=10.1105/tpc.114.127910;
RA Puranik S., Acajjaoui S., Conn S., Costa L., Conn V., Vial A.,
RA Marcellin R., Melzer R., Brown E., Hart D., Theissen G., Silva C.S.,
RA Parcy F., Dumas R., Nanao M., Zubieta C.;
RT "Structural basis for the oligomerization of the MADS domain transcription
RT factor SEPALLATA3 in Arabidopsis.";
RL Plant Cell 26:3603-3615(2014).
CC -!- FUNCTION: Probable transcription factor active in inflorescence
CC development and floral organogenesis. Functions with SEPALLATA1/AGL2
CC and SEPALLATA2/AGL4 to ensure proper development of petals, stamens and
CC carpels and to prevent the indeterminate growth of the flower meristem.
CC Interacts with APETALA1, AGAMOUS or APETALA3/PISTILLATA to form
CC complexes, that could be involved in genes regulation during floral
CC meristem development (PubMed:10821278, PubMed:11206550). Binds
CC specifically to the CArG box DNA sequence 5'-CC (A/T)6 GG-3'
CC (PubMed:16080001). {ECO:0000269|PubMed:10821278,
CC ECO:0000269|PubMed:11206550, ECO:0000269|PubMed:16080001}.
CC -!- SUBUNIT: Forms homodimers (PubMed:25228343). Heterodimer with AP1 or AG
CC capable of binding to CArG-box sequences. Binds AP3/PI to form a
CC ternary complex. Interacts with AGL16 (PubMed:15805477). Interacts with
CC TT16/AGL32 (PubMed:16080001). {ECO:0000269|PubMed:15805477,
CC ECO:0000269|PubMed:16080001, ECO:0000269|PubMed:25228343}.
CC -!- INTERACTION:
CC O22456; P17839: AG; NbExp=4; IntAct=EBI-592020, EBI-592365;
CC O22456; P29381: AGL1; NbExp=5; IntAct=EBI-592020, EBI-592304;
CC O22456; Q38836: AGL11; NbExp=3; IntAct=EBI-592020, EBI-592343;
CC O22456; P35631: AP1; NbExp=4; IntAct=EBI-592020, EBI-592003;
CC O22456; Q6EVK6: BRM; NbExp=2; IntAct=EBI-592020, EBI-2025535;
CC O22456; P48007: PI; NbExp=3; IntAct=EBI-592020, EBI-1395334;
CC O22456; Q8W234: SEU; NbExp=2; IntAct=EBI-592020, EBI-1771131;
CC O22456; Q5XXE7: SHP2; NbExp=3; IntAct=EBI-592020, EBI-592328;
CC O22456; F4IHS2: SYD; NbExp=2; IntAct=EBI-592020, EBI-15967899;
CC O22456; Q8RYD9: TT16; NbExp=7; IntAct=EBI-592020, EBI-621993;
CC O22456; Q2NJQ2: AYWB_224; Xeno; NbExp=4; IntAct=EBI-592020, EBI-16100490;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O22456-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O22456-2; Sequence=VSP_008893;
CC -!- DEVELOPMENTAL STAGE: Expressed early during flower development within
CC petals, stamens, and carpels.
CC -!- DISRUPTION PHENOTYPE: Triple mutations in the SEP1, SEP2 and SEP3 genes
CC result in the replacement of the stamens and petals by sepals and of
CC the carpels by a new mutant flower with sepaloid organs.
CC {ECO:0000269|PubMed:10821278}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC43290.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF015552; AAB67832.1; -; mRNA.
DR EMBL; AC002396; AAC00586.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30502.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30503.1; -; Genomic_DNA.
DR EMBL; AY088272; AAM65812.1; -; mRNA.
DR EMBL; AK118696; BAC43290.1; ALT_INIT; mRNA.
DR PIR; T00656; T00656.
DR RefSeq; NP_564214.2; NM_102272.4. [O22456-1]
DR RefSeq; NP_850953.1; NM_180622.3. [O22456-2]
DR PDB; 4OX0; X-ray; 2.49 A; A/B/C/D=75-178.
DR PDB; 7NB0; X-ray; 2.10 A; A/B/C/D=18-74.
DR PDBsum; 4OX0; -.
DR PDBsum; 7NB0; -.
DR AlphaFoldDB; O22456; -.
DR SMR; O22456; -.
DR BioGRID; 24278; 25.
DR DIP; DIP-33800N; -.
DR IntAct; O22456; 23.
DR STRING; 3702.AT1G24260.2; -.
DR PaxDb; O22456; -.
DR PRIDE; O22456; -.
DR ProteomicsDB; 234508; -. [O22456-1]
DR EnsemblPlants; AT1G24260.1; AT1G24260.1; AT1G24260. [O22456-2]
DR EnsemblPlants; AT1G24260.2; AT1G24260.2; AT1G24260. [O22456-1]
DR GeneID; 839040; -.
DR Gramene; AT1G24260.1; AT1G24260.1; AT1G24260. [O22456-2]
DR Gramene; AT1G24260.2; AT1G24260.2; AT1G24260. [O22456-1]
DR KEGG; ath:AT1G24260; -.
DR Araport; AT1G24260; -.
DR TAIR; locus:2032372; AT1G24260.
DR eggNOG; KOG0014; Eukaryota.
DR InParanoid; O22456; -.
DR OMA; YQGQQDH; -.
DR PhylomeDB; O22456; -.
DR PRO; PR:O22456; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O22456; baseline and differential.
DR Genevisible; O22456; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; 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:0001708; P:cell fate specification; IMP:TAIR.
DR GO; GO:0009908; P:flower development; TAS:TAIR.
DR GO; GO:0080001; P:mucilage extrusion from seed coat; IMP:TAIR.
DR GO; GO:0048481; P:plant ovule development; IMP: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 GO; GO:0010214; P:seed coat development; IMP:TAIR.
DR GO; GO:0010093; P:specification of floral organ identity; IMP:TAIR.
DR GO; GO:0048833; P:specification of floral organ number; IMP:TAIR.
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 3D-structure; Activator; Alternative splicing; Coiled coil;
KW Developmental protein; Differentiation; DNA-binding; Flowering; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..251
FT /note="Developmental protein SEPALLATA 3"
FT /id="PRO_0000199485"
FT DOMAIN 3..57
FT /note="MADS-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT DOMAIN 91..181
FT /note="K-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00629"
FT COILED 94..177
FT /evidence="ECO:0000255"
FT VAR_SEQ 90
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_008893"
FT HELIX 21..39
FT /evidence="ECO:0007829|PDB:7NB0"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:7NB0"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:7NB0"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:7NB0"
FT HELIX 85..114
FT /evidence="ECO:0007829|PDB:4OX0"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:4OX0"
FT HELIX 125..168
FT /evidence="ECO:0007829|PDB:4OX0"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:4OX0"
SQ SEQUENCE 251 AA; 29066 MW; 0057CABD3F1AFC40 CRC64;
MGRGRVELKR IENKINRQVT FAKRRNGLLK KAYELSVLCD AEVALIIFSN RGKLYEFCSS
SSMLRTLERY QKCNYGAPEP NVPSREALAV ELSSQQEYLK LKERYDALQR TQRNLLGEDL
GPLSTKELES LERQLDSSLK QIRALRTQFM LDQLNDLQSK ERMLTETNKT LRLRLADGYQ
MPLQLNPNQE EVDHYGRHHH QQQQHSQAFF QPLECEPILQ IGYQGQQDGM GAGPSVNNYM
LGWLPYDTNS I
