SPL2_ARATH
ID SPL2_ARATH Reviewed; 419 AA.
AC Q9S840; Q1EBV0; Q9SMY0;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Squamosa promoter-binding-like protein 2;
GN Name=SPL2; OrderedLocusNames=At5g43270; ORFNames=MNL12.9;
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], AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia, and 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
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 Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
RP INDUCTION.
RX PubMed=12586064; DOI=10.1016/s1534-5807(03)00025-x;
RA Kasschau K.D., Xie Z., Allen E., Llave C., Chapman E.J., Krizan K.A.,
RA Carrington J.C.;
RT "P1/HC-Pro, a viral suppressor of RNA silencing, interferes with
RT Arabidopsis development and miRNA function.";
RL Dev. Cell 4:205-217(2003).
CC -!- FUNCTION: Trans-acting factor that binds specifically to the consensus
CC nucleotide sequence 5'-TNCGTACAA-3'.
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:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed constitutively during plant development,
CC weak increase during flowering. {ECO:0000269|PubMed:10524240,
CC ECO:0000269|PubMed:14573523}.
CC -!- INDUCTION: Negatively regulated by microRNAs miR156 and miR157
CC (Probable). Up-regulated by Turnip mosaic virus P1/HC-Pro protein, that
CC acts as an antagonist of miR156. {ECO:0000269|PubMed:12202040,
CC ECO:0000269|PubMed:12586064, ECO:0000305}.
CC -!- DOMAIN: The SBP-type zinc finger is required for the binding to DNA.
CC {ECO:0000250}.
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DR EMBL; AJ011624; CAB56576.1; -; Genomic_DNA.
DR EMBL; AJ011625; CAB56577.1; -; mRNA.
DR EMBL; AJ011626; CAB56578.1; -; mRNA.
DR EMBL; AB017070; BAB10590.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94933.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94934.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94935.1; -; Genomic_DNA.
DR EMBL; BT025984; ABG25073.1; -; mRNA.
DR EMBL; AK230160; BAF01969.1; -; mRNA.
DR PIR; T52603; T52603.
DR PIR; T52604; T52604.
DR RefSeq; NP_199141.1; NM_123693.6.
DR RefSeq; NP_851122.1; NM_180791.3.
DR RefSeq; NP_974875.1; NM_203146.4.
DR AlphaFoldDB; Q9S840; -.
DR SMR; Q9S840; -.
DR STRING; 3702.AT5G43270.1; -.
DR PaxDb; Q9S840; -.
DR PRIDE; Q9S840; -.
DR ProteomicsDB; 245200; -.
DR EnsemblPlants; AT5G43270.1; AT5G43270.1; AT5G43270.
DR EnsemblPlants; AT5G43270.2; AT5G43270.2; AT5G43270.
DR EnsemblPlants; AT5G43270.3; AT5G43270.3; AT5G43270.
DR GeneID; 834345; -.
DR Gramene; AT5G43270.1; AT5G43270.1; AT5G43270.
DR Gramene; AT5G43270.2; AT5G43270.2; AT5G43270.
DR Gramene; AT5G43270.3; AT5G43270.3; AT5G43270.
DR KEGG; ath:AT5G43270; -.
DR Araport; AT5G43270; -.
DR TAIR; locus:2169248; AT5G43270.
DR eggNOG; ENOG502QPVZ; Eukaryota.
DR HOGENOM; CLU_026055_1_0_1; -.
DR InParanoid; Q9S840; -.
DR OMA; MEWEIDG; -.
DR OrthoDB; 607491at2759; -.
DR PhylomeDB; Q9S840; -.
DR PRO; PR:Q9S840; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9S840; baseline and differential.
DR Genevisible; Q9S840; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0048653; P:anther development; IGI:TAIR.
DR GO; GO:0090356; P:negative regulation of auxin metabolic process; IMP:TAIR.
DR GO; GO:0048510; P:regulation of timing of transition from vegetative to reproductive phase; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR Gene3D; 4.10.1100.10; -; 1.
DR InterPro; IPR004333; SBP_dom.
DR InterPro; IPR036893; SBP_sf.
DR InterPro; IPR044817; SPL.
DR PANTHER; PTHR31251; PTHR31251; 1.
DR Pfam; PF03110; SBP; 1.
DR SUPFAM; SSF103612; SSF103612; 1.
DR PROSITE; PS51141; ZF_SBP; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..419
FT /note="Squamosa promoter-binding-like protein 2"
FT /id="PRO_0000132723"
FT ZN_FING 166..243
FT /note="SBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT REGION 77..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 226..242
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 77..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT CONFLICT 50
FT /note="F -> FDAV (in Ref. 1; CAB56577)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="A -> G (in Ref. 1; CAB56577)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="A -> T (in Ref. 1; CAB56577)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="S -> T (in Ref. 1; CAB56577)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="T -> S (in Ref. 1; CAB56577)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="I -> L (in Ref. 1; CAB56577)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="H -> P (in Ref. 1; CAB56577)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="D -> NKLF (in Ref. 1; CAB56577)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="N -> S (in Ref. 1; CAB56577)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="T -> S (in Ref. 1; CAB56577)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..373
FT /note="VAH -> IAN (in Ref. 1; CAB56577)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="N -> S (in Ref. 1; CAB56577)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="V -> A (in Ref. 1; CAB56577)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 46860 MW; 092C3A1DF034EBFF CRC64;
MECNAKPPFQ WELENLISFG TSTAEVPRKL KPMEWEIDGF DCTSLYSSSF AYAGSSGSDI
AHAFSKSSKS TSISSSSAEV RTHNFTSETG ESLPGEFAKG IDTSPSLELS FGSGDPVLGL
KLGKRTYFED FWEVENAKGL GLPVTLASSS VSPVKKSKSI PQRLQTPHCQ VEGCNLDLSS
AKDYHRKHRI CENHSKFPKV VVSGVERRFC QQCSRFHCLS EFDEKKRSCR RRLSDHNARR
RKPNPGRTYD GKPQVDFVWN RFALIHPRSE EKFIWPSSKH VPSRVLMPQP AKTEISDTEH
NRFGLLDPKT KTARAELFSK EKVTISSHMG ASQDLDGALS LLSNSTTWVS SSDQPRRFTL
DHHPSSNLQP VAHRSAAQLN SVSGYWQPDP PAVEGPTALH RNGVGQFNEN YFSLNQFYN
