SPL7_ARATH
ID SPL7_ARATH Reviewed; 801 AA.
AC Q8S9G8; Q8VZV0; Q9S723; Q9SMY1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Squamosa promoter-binding-like protein 7;
GN Name=SPL7; OrderedLocusNames=At5g18830; ORFNames=F17K4.80;
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] (ISOFORM 1), 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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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] (ISOFORMS 1 AND 2).
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.
RX PubMed=19122104; DOI=10.1105/tpc.108.060137;
RA Yamasaki H., Hayashi M., Fukazawa M., Kobayashi Y., Shikanai T.;
RT "SQUAMOSA promoter binding protein-like7 is a central regulator for copper
RT homeostasis in Arabidopsis.";
RL Plant Cell 21:347-361(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22374396; DOI=10.1105/tpc.111.090431;
RA Bernal M., Casero D., Singh V., Wilson G.T., Grande A., Yang H.,
RA Dodani S.C., Pellegrini M., Huijser P., Connolly E.L., Merchant S.S.,
RA Kraemer U.;
RT "Transcriptome sequencing identifies SPL7-regulated copper acquisition
RT genes FRO4/FRO5 and the copper dependence of iron homeostasis in
RT Arabidopsis.";
RL Plant Cell 24:738-761(2012).
RN [7]
RP SUBUNIT.
RX PubMed=25207797; DOI=10.1186/s12870-014-0231-5;
RA Garcia-Molina A., Xing S., Huijser P.;
RT "Functional characterisation of Arabidopsis SPL7 conserved protein domains
RT suggests novel regulatory mechanisms in the Cu deficiency response.";
RL BMC Plant Biol. 14:231-231(2014).
RN [8]
RP FUNCTION, AND INTERACTION WITH HY5.
RX PubMed=25516599; DOI=10.1105/tpc.114.127340;
RA Zhang H., Zhao X., Li J., Cai H., Deng X.W., Li L.;
RT "MicroRNA408 is critical for the HY5-SPL7 gene network that mediates the
RT coordinated response to light and copper.";
RL Plant Cell 26:4933-4953(2014).
RN [9]
RP INTERACTION WITH KIN17, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24335506; DOI=10.1104/pp.113.228239;
RA Garcia-Molina A., Xing S., Huijser P.;
RT "A conserved KIN17 curved DNA-binding domain protein assembles with
RT SQUAMOSA PROMOTER-BINDING PROTEIN-LIKE7 to adapt Arabidopsis growth and
RT development to limiting copper availability.";
RL Plant Physiol. 164:828-840(2014).
RN [10]
RP FUNCTION.
RX PubMed=26511915; DOI=10.1104/pp.15.01011;
RA Zhao Y., Lin S., Qiu Z., Cao D., Wen J., Deng X., Wang X., Lin J., Li X.;
RT "MicroRNA857 is involved in the regulation of secondary growth of vascular
RT tissues in Arabidopsis.";
RL Plant Physiol. 169:2539-2552(2015).
RN [11]
RP FUNCTION.
RX PubMed=27352843; DOI=10.1186/s12870-016-0830-4;
RA Gielen H., Remans T., Vangronsveld J., Cuypers A.;
RT "Toxicity responses of Cu and Cd: the involvement of miRNAs and the
RT transcription factor SPL7.";
RL BMC Plant Biol. 16:145-145(2016).
RN [12]
RP STRUCTURE BY NMR OF 135-220, AND ZINC-BINDING SITES CYS-138; CYS-143;
RP CYS-160; CYS-163; CYS-179; CYS-182; HIS-186 AND CYS-198.
RX PubMed=15001351; DOI=10.1016/j.jmb.2004.01.015;
RA Yamasaki K., Kigawa T., Inoue M., Tateno M., Yamasaki T., Yabuki T.,
RA Aoki M., Seki E., Matsuda T., Nunokawa E., Ishizuka Y., Terada T.,
RA Shirouzu M., Osanai T., Tanaka A., Seki M., Shinozaki K., Yokoyama S.;
RT "A novel zinc-binding motif revealed by solution structures of DNA-binding
RT domains of Arabidopsis SBP-family transcription factors.";
RL J. Mol. Biol. 337:49-63(2004).
CC -!- FUNCTION: Transcription factor that participates in reprogramming
CC global gene expression during copper deficiency in order to improve the
CC metal uptake and prioritize its distribution to copper proteins of
CC major importance (Probable). Binds directly to 5'-GTAC-3' motifs in the
CC microRNA (miRNA) promoter of the stress-responsive miRNAs miR398b and
CC miR398c to activate their transcription. During copper deficiency,
CC activates the copper transporters COPT1 and COPT2, and the copper
CC chaperone CCH, directly or indirectly via miRNAs. Required for the
CC expression of the miRNAs miR397, miR408 and miR857 (PubMed:19122104).
CC Acts coordinately with HY5 to regulate miR408 and its target genes in
CC response to changes in light and copper conditions (PubMed:25516599).
CC Activates miR857 and its target genes in response to low copper
CC conditions (PubMed:26511915). Involved in cadmium stress response by
CC regulating miR397a, miR398b, miR398c and miR857 (PubMed:27352843).
CC Required for iron homeostasis during copper deficiency
CC (PubMed:22374396). {ECO:0000269|PubMed:19122104,
CC ECO:0000269|PubMed:22374396, ECO:0000269|PubMed:25516599,
CC ECO:0000269|PubMed:26511915, ECO:0000269|PubMed:27352843}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15001351};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:15001351};
CC -!- SUBUNIT: Homodimer (PubMed:25207797). Interacts with KIN17
CC (PubMed:24335506). Interacts with HY5 (PubMed:25516599).
CC {ECO:0000269|PubMed:24335506, ECO:0000269|PubMed:25207797,
CC ECO:0000269|PubMed:25516599}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:24335506}.
CC Note=Nuclear localization with a speckled distribution pattern.
CC {ECO:0000269|PubMed:24335506}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8S9G8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8S9G8-2; Sequence=VSP_013984;
CC -!- TISSUE SPECIFICITY: Expressed in roots rosette leaves, cauline leaves,
CC stems, flowers and siliques. {ECO:0000269|PubMed:24335506}.
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 {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Retarded growth and hypersensitivity to copper
CC deprivation. {ECO:0000269|PubMed:24335506}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL77751.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ011611; CAB56573.1; -; mRNA.
DR EMBL; AJ011612; CAB56574.1; -; mRNA.
DR EMBL; AJ011613; CAB56575.1; -; Genomic_DNA.
DR EMBL; AC068655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92617.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92618.1; -; Genomic_DNA.
DR EMBL; AF367355; AAK32941.1; -; mRNA.
DR EMBL; AY063815; AAL36171.1; -; mRNA.
DR EMBL; AY078050; AAL77751.1; ALT_INIT; mRNA.
DR PIR; T52605; T52605.
DR PIR; T52606; T52606.
DR RefSeq; NP_197384.1; NM_121888.3. [Q8S9G8-1]
DR RefSeq; NP_850850.1; NM_180519.1. [Q8S9G8-2]
DR PDB; 1UL5; NMR; -; A=135-220.
DR PDBsum; 1UL5; -.
DR AlphaFoldDB; Q8S9G8; -.
DR SMR; Q8S9G8; -.
DR BioGRID; 17277; 3.
DR IntAct; Q8S9G8; 1.
DR STRING; 3702.AT5G18830.3; -.
DR PaxDb; Q8S9G8; -.
DR ProteomicsDB; 228397; -. [Q8S9G8-1]
DR EnsemblPlants; AT5G18830.1; AT5G18830.1; AT5G18830. [Q8S9G8-1]
DR EnsemblPlants; AT5G18830.2; AT5G18830.2; AT5G18830. [Q8S9G8-2]
DR GeneID; 832001; -.
DR Gramene; AT5G18830.1; AT5G18830.1; AT5G18830. [Q8S9G8-1]
DR Gramene; AT5G18830.2; AT5G18830.2; AT5G18830. [Q8S9G8-2]
DR KEGG; ath:AT5G18830; -.
DR Araport; AT5G18830; -.
DR eggNOG; ENOG502QUTN; Eukaryota.
DR InParanoid; Q8S9G8; -.
DR OMA; WGDDSIG; -.
DR PhylomeDB; Q8S9G8; -.
DR EvolutionaryTrace; Q8S9G8; -.
DR PRO; PR:Q8S9G8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8S9G8; baseline and differential.
DR Genevisible; Q8S9G8; AT.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0035874; P:cellular response to copper ion starvation; IMP:UniProtKB.
DR GO; GO:0048638; P:regulation of developmental growth; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
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; 2.
DR Pfam; PF03110; SBP; 1.
DR SUPFAM; SSF103612; SSF103612; 1.
DR PROSITE; PS51141; ZF_SBP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Stress response; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..801
FT /note="Squamosa promoter-binding-like protein 7"
FT /id="PRO_0000132728"
FT ZN_FING 135..212
FT /note="SBP-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 195..211
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 235..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470,
FT ECO:0000269|PubMed:15001351, ECO:0007744|PDB:1UL5"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470,
FT ECO:0000269|PubMed:15001351, ECO:0007744|PDB:1UL5"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470,
FT ECO:0000269|PubMed:15001351, ECO:0007744|PDB:1UL5"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470,
FT ECO:0000269|PubMed:15001351, ECO:0007744|PDB:1UL5"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470,
FT ECO:0000269|PubMed:15001351, ECO:0007744|PDB:1UL5"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470,
FT ECO:0000269|PubMed:15001351, ECO:0007744|PDB:1UL5"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470,
FT ECO:0000269|PubMed:15001351, ECO:0007744|PDB:1UL5"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470,
FT ECO:0000269|PubMed:15001351, ECO:0007744|PDB:1UL5"
FT VAR_SEQ 675..700
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_013984"
FT CONFLICT 165
FT /note="T -> N (in Ref. 1; CAB56573)"
FT /evidence="ECO:0000305"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:1UL5"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1UL5"
FT HELIX 161..166
FT /evidence="ECO:0007829|PDB:1UL5"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:1UL5"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:1UL5"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:1UL5"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:1UL5"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:1UL5"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1UL5"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:1UL5"
SQ SEQUENCE 801 AA; 89617 MW; E69BE9C57670090D CRC64;
MSSLSQSPPP PEMDIQPPAL VNDDPSTYSS ALWDWGDLLD FAADERLLVD QIHFPPVLSP
PLPPLIPTQT PAESELDPSP EESGSGSDRV RKRDPRLICS NFIEGMLPCS CPELDQKLED
AELPKKKRVR GGSGVARCQV PDCEADISEL KGYHKRHRVC LRCATASFVV LDGENKRYCQ
QCGKFHLLPD FDEGKRSCRR KLERHNNRRK RKPVDKGGVA AEQQQVLSQN DNSVIDVEDG
KDITCSSDQR AEEEPSLIFE DRHITTQGSV PFTRSINADN FVSVTGSGEA QPDEGMNDTK
FERSPSNGDN KSAYSTVCPT GRISFKLYDW NPAEFPRRLR HQIFQWLANM PVELEGYIRP
GCTILTVFIA MPEIMWAKLS KDPVAYLDEF ILKPGKMLFG RGSMTVYLNN MIFRLIKGGT
TLKRVDVKLE SPKLQFVYPT CFEAGKPIEL VVCGQNLLQP KCRFLVSFSG KYLPHNYSVV
PAPDQDGKRS CNNKFYKINI VNSDPSLFGP AFVEVENESG LSNFIPLIIG DAAVCSEMKL
IEQKFNATLF PEGQEVTACS SLTCCCRDFG ERQSTFSGLL LDIAWSVKVP SAERTEQPVN
RCQIKRYNRV LNYLIQNNSA SILGNVLHNL ETLVKKMEPD SLVHCTCDCD VRLLHENMDL
ASDIHRKHQS PIESKVNPPS SGCCCVSSQK DIPSRILNFN KDPEAGLDCK ERIQADCSPD
SGGKETDPLL NKEVVMNVND IGDWPRKSCI KTHSALAFRS RQTMFLIATF AVCFAVCAVL
YHPNKVTQLA VAIRMRLVHK I
