SPL1_ARATH
ID SPL1_ARATH Reviewed; 881 AA.
AC Q9SMX9; O80717; O80718; O82651; Q0WLD6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Squamosa promoter-binding-like protein 1;
GN Name=SPL1; OrderedLocusNames=At2g47070/At2g47080;
GN ORFNames=F14M4.9/F14M4.10;
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, AND DEVELOPMENTAL
RP 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=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 [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 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 [5]
RP FUNCTION, REGION, AND MUTAGENESIS OF CYS-111; HIS-122; HIS-131; CYS-147;
RP ARG-152; HIS-154; ARG-164 AND CYS-166.
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).
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. {ECO:0000269|PubMed:10524240,
CC ECO:0000269|PubMed:16095614}.
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 {ECO:0000269|PubMed:10524240}.
CC -!- DOMAIN: The SBP-type zinc finger is required for the binding to DNA.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC34220.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At2g47070 and At2g47080.; Evidence={ECO:0000305};
CC Sequence=AAC34221.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At2g47070 and At2g47080.; Evidence={ECO:0000305};
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DR EMBL; AJ011577; CAA09698.1; -; Genomic_DNA.
DR EMBL; AJ011628; CAB56580.1; -; mRNA.
DR EMBL; AJ011629; CAB56581.1; -; mRNA.
DR EMBL; AC004411; AAC34220.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC004411; AAC34221.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10798.1; -; Genomic_DNA.
DR EMBL; AK230269; BAF02071.1; -; mRNA.
DR PIR; T02179; T02179.
DR PIR; T02180; T02180.
DR PIR; T52601; T52601.
DR PIR; T52602; T52602.
DR RefSeq; NP_850468.1; NM_180137.3.
DR AlphaFoldDB; Q9SMX9; -.
DR SMR; Q9SMX9; -.
DR BioGRID; 4656; 4.
DR STRING; 3702.AT2G47070.1; -.
DR PaxDb; Q9SMX9; -.
DR PRIDE; Q9SMX9; -.
DR ProteomicsDB; 228395; -.
DR EnsemblPlants; AT2G47070.1; AT2G47070.1; AT2G47070.
DR GeneID; 819321; -.
DR Gramene; AT2G47070.1; AT2G47070.1; AT2G47070.
DR KEGG; ath:AT2G47070; -.
DR Araport; AT2G47070; -.
DR TAIR; locus:2041329; AT2G47070.
DR eggNOG; ENOG502QS71; Eukaryota.
DR HOGENOM; CLU_006255_3_0_1; -.
DR InParanoid; Q9SMX9; -.
DR OrthoDB; 216262at2759; -.
DR PhylomeDB; Q9SMX9; -.
DR PRO; PR:Q9SMX9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SMX9; baseline and differential.
DR Genevisible; Q9SMX9; AT.
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; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 4.10.1100.10; -; 1.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR004333; SBP_dom.
DR InterPro; IPR036893; SBP_sf.
DR InterPro; IPR044817; SPL.
DR PANTHER; PTHR31251; PTHR31251; 2.
DR Pfam; PF03110; SBP; 1.
DR SUPFAM; SSF103612; SSF103612; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS51141; ZF_SBP; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..881
FT /note="Squamosa promoter-binding-like protein 1"
FT /id="PRO_0000132722"
FT ZN_FING 103..180
FT /note="SBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT REGION 49..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..187
FT /note="Sufficient and necessary for DNA binding"
FT REGION 170..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 163..179
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 312..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT MUTAGEN 111
FT /note="C->A: Almost complete loss of DNA binding."
FT /evidence="ECO:0000269|PubMed:16095614"
FT MUTAGEN 122
FT /note="H->A: Slight decrease in DNA binding efficiency."
FT /evidence="ECO:0000269|PubMed:16095614"
FT MUTAGEN 131
FT /note="H->A: Almost complete loss of DNA binding."
FT /evidence="ECO:0000269|PubMed:16095614"
FT MUTAGEN 147
FT /note="C->A: Complete loss of DNA binding."
FT /evidence="ECO:0000269|PubMed:16095614"
FT MUTAGEN 152
FT /note="R->Q: No effect on DNA binding efficiency."
FT /evidence="ECO:0000269|PubMed:16095614"
FT MUTAGEN 154
FT /note="H->A: Reduction of DNA binding efficiency by half."
FT /evidence="ECO:0000269|PubMed:16095614"
FT MUTAGEN 164
FT /note="R->Q: Slight decrease in DNA binding efficiency."
FT /evidence="ECO:0000269|PubMed:16095614"
FT MUTAGEN 166
FT /note="C->A: Complete loss of DNA binding."
FT /evidence="ECO:0000269|PubMed:16095614"
FT CONFLICT 140
FT /note="G -> E (in Ref. 1; CAB56580)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="Q -> R (in Ref. 1; CAB56580)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 881 AA; 98460 MW; 8A932C26D9A6259B CRC64;
MEARIDEGGE AQQFYGSVGK RSVEWDLNDW KWDGDLFLAT QTTRGRQFFP LGNSSNSSSS
CSDEGNDKKR RAVAIQGDTN GALTLNLNGE SDGLFPAKKT KSGAVCQVEN CEADLSKVKD
YHRRHKVCEM HSKATSATVG GILQRFCQQC SRFHLLQEFD EGKRSCRRRL AGHNKRRRKT
NPEPGANGNP SDDHSSNYLL ITLLKILSNM HNHTGDQDLM SHLLKSLVSH AGEQLGKNLV
ELLLQGGGSQ GSLNIGNSAL LGIEQAPQEE LKQFSARQDG TATENRSEKQ VKMNDFDLND
IYIDSDDTDV ERSPPPTNPA TSSLDYPSWI HQSSPPQTSR NSDSASDQSP SSSSEDAQMR
TGRIVFKLFG KEPNEFPIVL RGQILDWLSH SPTDMESYIR PGCIVLTIYL RQAETAWEEL
SDDLGFSLGK LLDLSDDPLW TTGWIYVRVQ NQLAFVYNGQ VVVDTSLSLK SRDYSHIISV
KPLAIAATEK AQFTVKGMNL RQRGTRLLCS VEGKYLIQET THDSTTREDD DFKDNSEIVE
CVNFSCDMPI LSGRGFMEIE DQGLSSSFFP FLVVEDDDVC SEIRILETTL EFTGTDSAKQ
AMDFIHEIGW LLHRSKLGES DPNPGVFPLI RFQWLIEFSM DREWCAVIRK LLNMFFDGAV
GEFSSSSNAT LSELCLLHRA VRKNSKPMVE MLLRYIPKQQ RNSLFRPDAA GPAGLTPLHI
AAGKDGSEDV LDALTEDPAM VGIEAWKTCR DSTGFTPEDY ARLRGHFSYI HLIQRKINKK
STTEDHVVVN IPVSFSDREQ KEPKSGPMAS ALEITQIPCK LCDHKLVYGT TRRSVAYRPA
MLSMVAIAAV CVCVALLFKS CPEVLYVFQP FRWELLDYGT S
