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SPL8_ARATH
ID   SPL8_ARATH              Reviewed;         333 AA.
AC   Q8GXL3; Q9S849;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Squamosa promoter-binding-like protein 8;
GN   Name=SPL8; OrderedLocusNames=At1g02065; ORFNames=T7I23.32;
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; 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=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   [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;
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   [5]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=12671094; DOI=10.1105/tpc.010678;
RA   Unte U.S., Sorensen A.-M., Pesaresi P., Gandikota M., Leister D.,
RA   Saedler H., Huijser P.;
RT   "SPL8, an SBP-box gene that affects pollen sac development in
RT   Arabidopsis.";
RL   Plant Cell 15:1009-1019(2003).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, REGION, AND
RP   MUTAGENESIS OF SER-233; SER-247 AND CYS-248.
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   [7]
RP   FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=17093870; DOI=10.1007/s11103-006-9099-6;
RA   Zhang Y., Schwarz S., Saedler H., Huijser P.;
RT   "SPL8, a local regulator in a subset of gibberellin-mediated developmental
RT   processes in Arabidopsis.";
RL   Plant Mol. Biol. 63:429-439(2007).
CC   -!- FUNCTION: Trans-acting factor that binds specifically to the consensus
CC       nucleotide sequence 5'-TNCGTACAA-3'. Binds specifically to the 5'-GTAC-
CC       3' core sequence. Involved in development and floral organogenesis.
CC       Required for ovule differentiation, pollen production, filament
CC       elongation, seed formation and siliques elongation. Also seems to play
CC       a role in the formation of trichomes on sepals. May positively modulate
CC       gibberellin (GA) signaling in flower. {ECO:0000269|PubMed:12671094,
CC       ECO:0000269|PubMed:16095614, ECO:0000269|PubMed:17093870}.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q8GXL3-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in shoot apical region and early floral
CC       tissues. Transcripts levels increase in developing pollen sacs, and
CC       decrease in later stage of anther development. Strongly expressed in
CC       the placental region of the carpels. {ECO:0000269|PubMed:12671094,
CC       ECO:0000269|PubMed:17093870}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during plant development. During pollen
CC       development, required for crosporogenesis that leads to archesporial
CC       formation and for the histogenesis of the microsporangia. During ovules
CC       development, involved in the transition to meiosis of the megaspore
CC       mother cells. {ECO:0000269|PubMed:10524240,
CC       ECO:0000269|PubMed:12671094}.
CC   -!- DOMAIN: The SBP-type zinc finger is required for the binding to DNA.
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DR   EMBL; AJ011641; CAB56593.1; -; Genomic_DNA.
DR   EMBL; AJ011642; CAB56594.1; -; mRNA.
DR   EMBL; U89959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002684; AEE27374.1; -; Genomic_DNA.
DR   EMBL; AK118174; BAC42797.1; -; mRNA.
DR   PIR; T52594; T52594.
DR   RefSeq; NP_683267.1; NM_148426.5. [Q8GXL3-1]
DR   AlphaFoldDB; Q8GXL3; -.
DR   SMR; Q8GXL3; -.
DR   BioGRID; 24510; 3.
DR   STRING; 3702.AT1G02065.1; -.
DR   iPTMnet; Q8GXL3; -.
DR   PaxDb; Q8GXL3; -.
DR   PRIDE; Q8GXL3; -.
DR   ProteomicsDB; 232489; -. [Q8GXL3-1]
DR   EnsemblPlants; AT1G02065.1; AT1G02065.1; AT1G02065. [Q8GXL3-1]
DR   GeneID; 839275; -.
DR   Gramene; AT1G02065.1; AT1G02065.1; AT1G02065. [Q8GXL3-1]
DR   KEGG; ath:AT1G02065; -.
DR   Araport; AT1G02065; -.
DR   TAIR; locus:504956101; AT1G02065.
DR   eggNOG; ENOG502QWHY; Eukaryota.
DR   HOGENOM; CLU_082879_0_0_1; -.
DR   InParanoid; Q8GXL3; -.
DR   OMA; DPRITNH; -.
DR   PhylomeDB; Q8GXL3; -.
DR   PRO; PR:Q8GXL3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8GXL3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:TAIR.
DR   GO; GO:0003677; F:DNA binding; ISS:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048653; P:anther development; IGI:TAIR.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0009554; P:megasporogenesis; IMP:TAIR.
DR   GO; GO:0009556; P:microsporogenesis; IMP: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   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW   DNA-binding; Flowering; Metal-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..333
FT                   /note="Squamosa promoter-binding-like protein 8"
FT                   /id="PRO_0000132729"
FT   ZN_FING         185..262
FT                   /note="SBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..269
FT                   /note="Sufficient and necessary for DNA binding"
FT   REGION          254..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          314..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           245..261
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        266..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         188
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT   BINDING         193
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="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT   BINDING         213
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
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   BINDING         232
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT   BINDING         236
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT   BINDING         248
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT   MUTAGEN         233
FT                   /note="S->A: Slight decrease in DNA binding efficiency."
FT                   /evidence="ECO:0000269|PubMed:16095614"
FT   MUTAGEN         247
FT                   /note="S->A: Slight decrease in DNA binding and nuclear
FT                   import efficiency."
FT                   /evidence="ECO:0000269|PubMed:16095614"
FT   MUTAGEN         247
FT                   /note="S->D: Complete loss of DNA binding. Slight increase
FT                   in nuclear import efficiency."
FT                   /evidence="ECO:0000269|PubMed:16095614"
FT   MUTAGEN         248
FT                   /note="C->A: Increase in nuclear import efficiency."
FT                   /evidence="ECO:0000269|PubMed:16095614"
FT   CONFLICT        63
FT                   /note="H -> Q (in Ref. 4; BAC42797)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        310
FT                   /note="Q -> R (in Ref. 4; BAC42797)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   333 AA;  36827 MW;  0182715A7A35D394 CRC64;
     MLDYEWDNPS SIVLSGDERN PDSDPTRSSF SFFDPISHYN NDHRHITISP PLLSSFSNQQ
     QQHHLTLYGQ TNSNNQFLHH HHHHHSLYGS TTTTTPYGAS DPIYHPHSSA PPASLFSYDQ
     TGPGSGSGSS YNFLIPKTEV DFTSNRIGLN LGGRTYFSAA DDDFVSRLYR RSRPGESGMA
     NSLSTPRCQA EGCNADLSHA KHYHRRHKVC EFHSKASTVV AAGLSQRFCQ QCSRFHLLSE
     FDNGKRSCRK RLADHNRRRR KCHQSASATQ DTGTGKTTPK SPNDSGVKAS SSPSSNAPPT
     ISLECFRQRQ FQTTASSSTS ASSSSNSMFF SSG
 
 
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