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SPL3_ARATH
ID   SPL3_ARATH              Reviewed;         131 AA.
AC   P93015; Q8LGE8; Q9LF84;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1999, sequence version 2.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Squamosa promoter-binding-like protein 3;
GN   Name=SPL3; OrderedLocusNames=At2g33810; ORFNames=T1B8.11;
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 [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Columbia, and cv. Landsberg erecta; TISSUE=Flower;
RX   PubMed=9301089; DOI=10.1046/j.1365-313x.1997.12020367.x;
RA   Cardon G.H., Hoehmann S., Nettesheim K., Saedler H., Huijser P.;
RT   "Functional analysis of the Arabidopsis thaliana SBP-box gene SPL3: a novel
RT   gene involved in the floral transition.";
RL   Plant J. 12:367-377(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Landsberg erecta; TISSUE=Flower;
RX   PubMed=10524240; DOI=10.1016/s0378-1119(99)00308-x;
RA   Cardon G.H., Hoehmann S., Klein J., Nettesheim K., Saedler H., Huijser P.;
RT   "Molecular characterization of the Arabidopsis SBP-box genes.";
RL   Gene 237:91-104(1999).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [8]
RP   INDUCTION.
RX   PubMed=12202040; DOI=10.1016/s0092-8674(02)00863-2;
RA   Rhoades M.W., Reinhart B.J., Lim L.P., Burge C.B., Bartel B., Bartel D.P.;
RT   "Prediction of plant microRNA targets.";
RL   Cell 110:513-520(2002).
RN   [9]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=14573523; DOI=10.1242/dev.00842;
RA   Schmid M., Uhlenhaut N.H., Godard F., Demar M., Bressan R., Weigel D.,
RA   Lohmann J.U.;
RT   "Dissection of floral induction pathways using global expression
RT   analysis.";
RL   Development 130:6001-6012(2003).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, REGION, AND
RP   MUTAGENESIS OF ASP-108; ARG-112; SER-113 AND CYS-114.
RX   PubMed=16095614; DOI=10.1016/j.jmb.2005.07.013;
RA   Birkenbihl R.P., Jach G., Saedler H., Huijser P.;
RT   "Functional dissection of the plant-specific SBP-domain: overlap of the
RT   DNA-binding and nuclear localization domains.";
RL   J. Mol. Biol. 352:585-596(2005).
RN   [11]
RP   FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=16914499; DOI=10.1242/dev.02521;
RA   Wu G., Poethig R.S.;
RT   "Temporal regulation of shoot development in Arabidopsis thaliana by miR156
RT   and its target SPL3.";
RL   Development 133:3539-3547(2006).
CC   -!- FUNCTION: Trans-acting factor that binds specifically to the consensus
CC       nucleotide sequence 5'-TNCGTACAA-3' of AP1 promoter. Binds specifically
CC       to the 5'-GTAC-3' core sequence. Promotes both vegetative phase change
CC       and flowering. Regulates phase-specific patterns of leaf epidermal
CC       differentiation and flowering time, but does not seem to affect leaf
CC       shape. {ECO:0000269|PubMed:16095614, ECO:0000269|PubMed:16914499,
CC       ECO:0000269|PubMed:9301089}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16095614}. Cytoplasm
CC       {ECO:0000269|PubMed:16095614}. Note=Mostly located in nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in vegetative and inflorescence apical
CC       meristems, floral meristems, leaf and flower organ primordia,
CC       inflorescence stem tissue and to lower extent in roots.
CC       {ECO:0000269|PubMed:10524240, ECO:0000269|PubMed:9301089}.
CC   -!- DEVELOPMENTAL STAGE: Increases during floral transition and stay high
CC       thereafter. {ECO:0000269|PubMed:10524240, ECO:0000269|PubMed:14573523,
CC       ECO:0000269|PubMed:16914499, ECO:0000269|PubMed:9301089}.
CC   -!- INDUCTION: Negatively regulated by microRNAs miR156.
CC       {ECO:0000269|PubMed:12202040, ECO:0000269|PubMed:16914499}.
CC   -!- DOMAIN: The SBP-type zinc finger is required for the binding to DNA.
CC   -!- DISRUPTION PHENOTYPE: Plants flower early and have a significantly
CC       reduced number of juvenile, adult and cauline leaves, with a shorter
CC       petiole and a more acute leaf base in the first two leaves.
CC       {ECO:0000269|PubMed:16914499}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB94233.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Y09427; CAA70578.1; -; mRNA.
DR   EMBL; AJ011627; CAB56579.1; -; Genomic_DNA.
DR   EMBL; AJ242959; CAB94233.1; ALT_INIT; mRNA.
DR   EMBL; AJ011633; CAB56585.1; -; mRNA.
DR   EMBL; U78721; AAC69133.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08889.1; -; Genomic_DNA.
DR   EMBL; AK118179; BAC42802.1; -; mRNA.
DR   EMBL; BT005443; AAO63863.1; -; mRNA.
DR   EMBL; AY084312; AAM67271.1; -; mRNA.
DR   PIR; H84749; H84749.
DR   PIR; T52597; T52597.
DR   RefSeq; NP_565771.1; NM_128940.2.
DR   AlphaFoldDB; P93015; -.
DR   SMR; P93015; -.
DR   BioGRID; 3295; 1.
DR   STRING; 3702.AT2G33810.1; -.
DR   iPTMnet; P93015; -.
DR   PaxDb; P93015; -.
DR   PRIDE; P93015; -.
DR   ProteomicsDB; 234096; -.
DR   EnsemblPlants; AT2G33810.1; AT2G33810.1; AT2G33810.
DR   GeneID; 817948; -.
DR   Gramene; AT2G33810.1; AT2G33810.1; AT2G33810.
DR   KEGG; ath:AT2G33810; -.
DR   Araport; AT2G33810; -.
DR   TAIR; locus:2057656; AT2G33810.
DR   eggNOG; ENOG502RZTN; Eukaryota.
DR   HOGENOM; CLU_065896_2_0_1; -.
DR   InParanoid; P93015; -.
DR   OMA; CTADMSK; -.
DR   OrthoDB; 1525145at2759; -.
DR   PhylomeDB; P93015; -.
DR   PRO; PR:P93015; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P93015; differential.
DR   Genevisible; P93015; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0009908; P:flower development; TAS:TAIR.
DR   GO; GO:0010229; P:inflorescence development; IMP:TAIR.
DR   GO; GO:0009911; P:positive regulation of flower development; IMP:TAIR.
DR   GO; GO:0010321; P:regulation of vegetative phase change; IMP:TAIR.
DR   GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR   Gene3D; 4.10.1100.10; -; 1.
DR   InterPro; IPR004333; SBP_dom.
DR   InterPro; IPR017238; SBP_fam.
DR   InterPro; IPR036893; SBP_sf.
DR   InterPro; IPR044817; SPL.
DR   PANTHER; PTHR31251; PTHR31251; 1.
DR   Pfam; PF03110; SBP; 1.
DR   PIRSF; PIRSF037575; SBP; 1.
DR   SUPFAM; SSF103612; SSF103612; 1.
DR   PROSITE; PS51141; ZF_SBP; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Developmental protein; Differentiation; DNA-binding; Flowering;
KW   Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..131
FT                   /note="Squamosa promoter-binding-like protein 3"
FT                   /id="PRO_0000132724"
FT   ZN_FING         51..128
FT                   /note="SBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          45..129
FT                   /note="Sufficient and necessary for DNA binding"
FT   MOTIF           111..127
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..36
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         54
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT   MUTAGEN         108
FT                   /note="D->A: Slight decrease in DNA binding efficiency."
FT                   /evidence="ECO:0000269|PubMed:16095614"
FT   MUTAGEN         112
FT                   /note="R->Q: Slight decrease in DNA binding efficiency."
FT                   /evidence="ECO:0000269|PubMed:16095614"
FT   MUTAGEN         113
FT                   /note="S->A: Slight decrease in DNA binding efficiency."
FT                   /evidence="ECO:0000269|PubMed:16095614"
FT   MUTAGEN         113
FT                   /note="S->D: Complete loss of DNA binding."
FT                   /evidence="ECO:0000269|PubMed:16095614"
FT   MUTAGEN         114
FT                   /note="C->A: Increase in nuclear import efficiency."
FT                   /evidence="ECO:0000269|PubMed:16095614"
FT   CONFLICT        63
FT                   /note="M -> I (in Ref. 7; AAM67271)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   131 AA;  15304 MW;  F3B4C7D8F6537501 CRC64;
     MSMRRSKAEG KRSLRELSEE EEEEEETEDE DTFEEEEALE KKQKGKATSS SGVCQVESCT
     ADMSKAKQYH KRHKVCQFHA KAPHVRISGL HQRFCQQCSR FHALSEFDEA KRSCRRRLAG
     HNERRRKSTT D
 
 
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