ID   AP22_ORYSI              Reviewed;         434 AA.
AC   B8AMA9;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=APETALA2-like protein 2 {ECO:0000305};
GN   Name=AP2-2 {ECO:0000305}; ORFNames=OsI_14083 {ECO:0000312|EMBL:EEC76419.1};
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: Probable transcription factor (By similarity). Involved in
CC       spikelet transition. Together with SNB, controls synergistically
CC       inflorescence architecture and floral meristem establishment via the
CC       regulation of spatio-temporal expression of B- and E-function floral
CC       organ identity genes in the lodicules and of spikelet meristem genes.
CC       Prevents lemma and palea elongation as well as grain growth (By
CC       similarity). {ECO:0000250|UniProtKB:P47927,
CC       ECO:0000250|UniProtKB:Q84TB5}.
CC   -!- SUBUNIT: May form homodimer (By similarity). Interacts with TPR2/ASP1
CC       (By similarity). {ECO:0000250|UniProtKB:P47927,
CC       ECO:0000250|UniProtKB:Q84TB5}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366}.
CC   -!- SIMILARITY: Belongs to the AP2/ERF transcription factor family. AP2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CM000128; EEC76419.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8AMA9; -.
DR   SMR; B8AMA9; -.
DR   STRING; 39946.B8AMA9; -.
DR   EnsemblPlants; BGIOSGA013826-TA; BGIOSGA013826-PA; BGIOSGA013826.
DR   Gramene; BGIOSGA013826-TA; BGIOSGA013826-PA; BGIOSGA013826.
DR   HOGENOM; CLU_035462_0_0_1; -.
DR   OMA; SPQWTVH; -.
DR   Proteomes; UP000007015; Chromosome 3.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0009909; P:regulation of flower development; IEA:EnsemblPlants.
DR   GO; GO:0080050; P:regulation of seed development; IEA:EnsemblPlants.
DR   GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IEA:EnsemblPlants.
DR   CDD; cd00018; AP2; 2.
DR   Gene3D; 3.30.730.10; -; 2.
DR   InterPro; IPR001471; AP2/ERF_dom.
DR   InterPro; IPR036955; AP2/ERF_dom_sf.
DR   InterPro; IPR016177; DNA-bd_dom_sf.
DR   Pfam; PF00847; AP2; 2.
DR   PRINTS; PR00367; ETHRSPELEMNT.
DR   SMART; SM00380; AP2; 2.
DR   SUPFAM; SSF54171; SSF54171; 2.
DR   PROSITE; PS51032; AP2_ERF; 2.
PE   3: Inferred from homology;
KW   DNA-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..434
FT                   /note="APETALA2-like protein 2"
FT                   /id="PRO_0000445990"
FT   DNA_BIND        118..174
FT                   /note="AP2/ERF 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
FT   DNA_BIND        210..267
FT                   /note="AP2/ERF 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
FT   REGION          1..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           106..115
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           291..295
FT                   /note="EAR"
FT                   /evidence="ECO:0000250|UniProtKB:P47927"
FT   COMPBIAS        9..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..87
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   434 AA;  47293 MW;  C0C4D87EFAE2B210 CRC64;
     MLLDLNVESP ERSGTSSSSV LNSGDAGGGG GGGGGGGLFR FDLLASSPDD DECSGEQHQL
     PAASGIVTRQ LLPPPPPAAP SPAPAWQPPR RAAEDAALAQ RPVVAKKTRR GPRSRSSQYR
     GVTFYRRTGR WESHIWDCGK QVYLGGFDTA HAAARAYDRA AIKFRGLEAD INFNLSDYED
     DLKQMRNWTK EEFVHILRRQ STGFARGSSK FRGVTLHKCG RWEARMGQLL GKKYIYLGLF
     DTEVEAARAY DRAAIRFNGR EAVTNFEPAS YNVDALPDAG NEAIVDGDLD LDLRISQPNA
     RDSKSDVATT GLQLTCDSPE SSNITVHQPM GSSPQWTVHH QSTPLPPQHQ RLYPSHCLGF
     LPNLQERPMD RRLELGPMPF PTQAWQMQAP SHLPLLHAAA SSGFSAGAGA GVAAATRRQP
     PFPADHPFYF PPTA