SPL14_ARATH
ID SPL14_ARATH Reviewed; 1035 AA.
AC Q8RY95; Q9SMW6; Q9SMX0; Q9SYN9;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Squamosa promoter-binding-like protein 14;
DE AltName: Full=Protein FUMONISIN B1-RESISTANT 6;
DE AltName: Full=SPL1-related protein 2;
GN Name=SPL14; Synonyms=FBR6, SPL1R2; OrderedLocusNames=At1g20980;
GN ORFNames=F9H16.3;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 224-1035.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 722-1035.
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15703061; DOI=10.1111/j.1365-313x.2005.02334.x;
RA Stone J.M., Liang X., Nekl E.R., Stiers J.J.;
RT "Arabidopsis AtSPL14, a plant-specific SBP-domain transcription factor,
RT participates in plant development and sensitivity to fumonisin B1.";
RL Plant J. 41:744-754(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
CC -!- FUNCTION: Trans-acting factor that binds specifically to the consensus
CC nucleotide sequence 5'-TNCGTACAA-3' (By similarity). May play a role in
CC plant development. {ECO:0000250, ECO:0000269|PubMed:15703061}.
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 -!- INTERACTION:
CC Q8RY95; O80748: B-box domain protein 26; NbExp=3; IntAct=EBI-15208462, EBI-15191535;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15703061}. Cytoplasm
CC {ECO:0000269|PubMed:15703061}. Note=Mostly located in the nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in vasculature of aerial parts. Expressed
CC in cotyledons and leaf petioles. {ECO:0000269|PubMed:15703061}.
CC -!- DOMAIN: The SBP-type zinc finger is required for the binding to DNA.
CC -!- DISRUPTION PHENOTYPE: Plants display elongated petioles and enhanced
CC leaf margin serration and are able to germinate and develop in the
CC presence of the programmed cell death (PCD)-inducing fungal toxin
CC fumonisin B1 (FB1). {ECO:0000269|PubMed:15703061}.
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DR EMBL; AC007369; AAD30593.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30050.1; -; Genomic_DNA.
DR EMBL; AJ242957; CAB56770.1; -; mRNA.
DR EMBL; AJ243094; CAB56773.1; -; Genomic_DNA.
DR EMBL; AY074499; AAL69483.2; -; mRNA.
DR PIR; G86342; G86342.
DR PIR; T52569; T52569.
DR RefSeq; NP_173522.1; NM_101951.4.
DR AlphaFoldDB; Q8RY95; -.
DR SMR; Q8RY95; -.
DR BioGRID; 23931; 4.
DR IntAct; Q8RY95; 4.
DR STRING; 3702.AT1G20980.1; -.
DR iPTMnet; Q8RY95; -.
DR PaxDb; Q8RY95; -.
DR PRIDE; Q8RY95; -.
DR ProteomicsDB; 228459; -.
DR EnsemblPlants; AT1G20980.1; AT1G20980.1; AT1G20980.
DR GeneID; 838692; -.
DR Gramene; AT1G20980.1; AT1G20980.1; AT1G20980.
DR KEGG; ath:AT1G20980; -.
DR Araport; AT1G20980; -.
DR TAIR; locus:2037355; AT1G20980.
DR eggNOG; ENOG502QS71; Eukaryota.
DR HOGENOM; CLU_006255_0_0_1; -.
DR InParanoid; Q8RY95; -.
DR OMA; TYPMCQV; -.
DR OrthoDB; 144179at2759; -.
DR PhylomeDB; Q8RY95; -.
DR PRO; PR:Q8RY95; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RY95; baseline and differential.
DR Genevisible; Q8RY95; 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:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA: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; 1.
DR Pfam; PF03110; SBP; 1.
DR SUPFAM; SSF103612; SSF103612; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS51141; ZF_SBP; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1035
FT /note="Squamosa promoter-binding-like protein 14"
FT /id="PRO_0000132735"
FT REPEAT 780..809
FT /note="ANK 1"
FT REPEAT 823..853
FT /note="ANK 2"
FT REPEAT 869..899
FT /note="ANK 3"
FT ZN_FING 117..194
FT /note="SBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT REGION 186..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 177..193
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 358..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT CONFLICT 851..852
FT /note="LT -> SA (in Ref. 3; CAB56770)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1035 AA; 114814 MW; D96DA5E1885B0278 CRC64;
MDEVGAQVAA PMFIHQSLGR KRDLYYPMSN RLVQSQPQRR DEWNSKMWDW DSRRFEAKPV
DVEVQEFDLT LRNRSGEERG LDLNLGSGLT AVEETTTTTQ NVRPNKKVRS GSPGGNYPMC
QVDNCTEDLS HAKDYHRRHK VCEVHSKATK ALVGKQMQRF CQQCSRFHLL SEFDEGKRSC
RRRLAGHNRR RRKTTQPEEV ASGVVVPGNH DTTNNTANAN MDLMALLTAL ACAQGKNAVK
PPVGSPAVPD REQLLQILNK INALPLPMDL VSKLNNIGSL ARKNMDHPTV NPQNDMNGAS
PSTMDLLAVL STTLGSSSPD ALAILSQGGF GNKDSEKTKL SSYENGVTTN LEKRTFGFSS
VGGERSSSSN QSPSQDSDSR GQDTRSSLSL QLFTSSPEDE SRPTVASSRK YYSSASSNPV
EDRSPSSSPV MQELFPLQAS PETMRSKNHK NSSPRTGCLP LELFGASNRG AADPNFKGFG
QQSGYASSGS DYSPPSLNSD AQDRTGKIVF KLLDKDPSQL PGTLRSEIYN WLSNIPSEME
SYIRPGCVVL SVYVAMSPAA WEQLEQKLLQ RLGVLLQNSP SDFWRNARFI VNTGRQLASH
KNGKVRCSKS WRTWNSPELI SVSPVAVVAG EETSLVVRGR SLTNDGISIR CTHMGSYMAM
EVTRAVCRQT IFDELNVNSF KVQNVHPGFL GRCFIEVENG FRGDSFPLII ANASICKELN
RLGEEFHPKS QDMTEEQAQS SNRGPTSREE VLCFLNELGW LFQKNQTSEL REQSDFSLAR
FKFLLVCSVE RDYCALIRTL LDMLVERNLV NDELNREALD MLAEIQLLNR AVKRKSTKMV
ELLIHYLVNP LTLSSSRKFV FLPNITGPGG ITPLHLAACT SGSDDMIDLL TNDPQEIGLS
SWNTLRDATG QTPYSYAAIR NNHNYNSLVA RKLADKRNKQ VSLNIEHEVV DQTGLSKRLS
LEMNKSSSSC ASCATVALKY QRRVSGSQRL FPTPIIHSML AVATVCVCVC VFMHAFPIVR
QGSHFSWGGL DYGSI
