ID   SLN1_HORVU              Reviewed;         618 AA.
AC   Q8W127;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=DELLA protein SLN1;
DE   AltName: Full=Slender protein 1;
GN   Name=SLN1;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   MUTAGENESIS OF GLY-46.
RX   PubMed=12011349; DOI=10.1104/pp.010917;
RA   Chandler P.M., Marion-Poll A., Ellis M., Gubler F.;
RT   "Mutants at the Slender1 locus of barley cv Himalaya. Molecular and
RT   physiological characterization.";
RL   Plant Physiol. 129:181-190(2002).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DEGRADATION.
RX   PubMed=12011350; DOI=10.1104/pp.010918;
RA   Gubler F., Chandler P.M., White R.G., Llewellyn D.J., Jacobsen J.V.;
RT   "Gibberellin signaling in barley aleurone cells. Control of SLN1 and GAMYB
RT   expression.";
RL   Plant Physiol. 129:191-200(2002).
RN   [3]
RP   FUNCTION, PHOSPHORYLATION, AND PROBABLE UBIQUITINATION.
RX   PubMed=12468736; DOI=10.1105/tpc.006197;
RA   Fu X., Richards D.E., Ait-Ali T., Hynes L.W., Ougham H., Peng J.,
RA   Harberd N.P.;
RT   "Gibberellin-mediated proteasome-dependent degradation of the barley DELLA
RT   protein SLN1 repressor.";
RL   Plant Cell 14:3191-3200(2002).
CC   -!- FUNCTION: Probable transcriptional regulator that acts as a repressor
CC       of the gibberellin (GA) signaling pathway. Probably acts by
CC       participating in large multiprotein complexes that repress
CC       transcription of GA-inducible genes. Upon GA application, it is
CC       degraded by the proteasome, allowing the GA signaling pathway. Acts as
CC       a negative regulator of GAMYB gene expression.
CC       {ECO:0000269|PubMed:12011349, ECO:0000269|PubMed:12011350,
CC       ECO:0000269|PubMed:12468736}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12011350}.
CC   -!- TISSUE SPECIFICITY: Apparently restricted to regions where growth is
CC       occurring in the leaf blade. Localizes almost exclusively to the basal
CC       elongation zone (EZ) for the elongating blades of L1, L2 and L3. More
CC       detailed fractionation of the L3 blade shows that in cv. Himalaya, it
CC       is preferentially localized to the basal third of the EZ, but its
CC       presence can still be detected toward the end of the EZ (at protein
CC       level). {ECO:0000269|PubMed:12011349}.
CC   -!- DOMAIN: The DELLA motif is required for its GA-induced degradation.
CC       {ECO:0000305}.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:12468736}.
CC   -!- PTM: Ubiquitinated (Probable). Upon GA application it is ubiquitinated,
CC       leading to its subsequent degradation. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GRAS family. DELLA subfamily. {ECO:0000305}.
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DR   EMBL; AF460219; AAL66734.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8W127; -.
DR   SMR; Q8W127; -.
DR   PRIDE; Q8W127; -.
DR   EnsemblPlants; HORVU.MOREX.r2.4HG0280720.1; HORVU.MOREX.r2.4HG0280720.1.CDS.1; HORVU.MOREX.r2.4HG0280720.
DR   EnsemblPlants; HORVU.MOREX.r2.4HG0280720.1.mrna1; HORVU.MOREX.r2.4HG0280720.1.mrna1.cds1; HORVU.MOREX.r2.4HG0280720.1.
DR   Gramene; HORVU.MOREX.r2.4HG0280720.1; HORVU.MOREX.r2.4HG0280720.1.CDS.1; HORVU.MOREX.r2.4HG0280720.
DR   Gramene; HORVU.MOREX.r2.4HG0280720.1.mrna1; HORVU.MOREX.r2.4HG0280720.1.mrna1.cds1; HORVU.MOREX.r2.4HG0280720.1.
DR   ExpressionAtlas; Q8W127; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR   GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.1290; -; 1.
DR   InterPro; IPR038088; DELLA_N_sf.
DR   InterPro; IPR030006; TF_DELLA.
DR   InterPro; IPR021914; TF_DELLA_N.
DR   InterPro; IPR005202; TF_GRAS.
DR   PANTHER; PTHR31636; PTHR31636; 1.
DR   PANTHER; PTHR31636:SF47; PTHR31636:SF47; 1.
DR   Pfam; PF12041; DELLA; 1.
DR   Pfam; PF03514; GRAS; 1.
DR   PROSITE; PS50985; GRAS; 1.
PE   1: Evidence at protein level;
KW   Gibberellin signaling pathway; Nucleus; Phosphoprotein; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..618
FT                   /note="DELLA protein SLN1"
FT                   /id="PRO_0000132244"
FT   DOMAIN          221..614
FT                   /note="GRAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          106..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..284
FT                   /note="Leucine repeat I (LRI)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          303..368
FT                   /note="VHIID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          382..421
FT                   /note="Leucine repeat II (LRII)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          431..535
FT                   /note="PFYRE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          538..614
FT                   /note="SAW"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   MOTIF           39..43
FT                   /note="DELLA motif"
FT   MOTIF           235..239
FT                   /note="LxCxE motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   MOTIF           334..338
FT                   /note="VHIID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   COMPBIAS        174..195
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         46
FT                   /note="G->E: In sln1-d; dominant mutation that causes a
FT                   dwarf phenotype probably due to its inability to be
FT                   degraded."
FT                   /evidence="ECO:0000269|PubMed:12011349"
SQ   SEQUENCE   618 AA;  65206 MW;  5E862C8E8207E045 CRC64;
     MKREYQDGGG SGGGGDEMGS SRDKMMVSSS EAGEGEEVDE LLAALGYKVR ASDMADVAQK
     LEQLEMAMGM GGPAPDDGFA THLATDTVHY NPTDLSSWVE SMLSELNAPP PPLPPAPPQL
     NASTSSTVTG GGGYFDLPPS VDSSSSTYAL RPIISPPVAP ADLSADSVRD PKRMRTGGSS
     TSSSSSSSSS LGGGAARSSV VEAAPPVAAA AAAPALPVVV VDTQEAGIRL VHALLACAEA
     VQQENLSAAE ALVKQIPLLA ASQGGAMRKV AAYFGEALAR RVFRFRPQPD SSLLDAAFAD
     LLHAHFYESC PYLKFAHFTA NQAILEAFAG CRRVHVVDFG IKQGMQWPAL LQALALRPGG
     PPSFRLTGVG PPQPDETDAL QQVGWKLAQF AHTIRVDFQY RGLVAATLAD LEPFMLQPEG
     EEDPNEEPEV IAVNSVFEMH RLLAQPGALE KVLGTVRAVR PRIVTVVEQE ANHNSGSFLD
     RFTESLHYYS TMFDSLEGGS SGGPSEVSSG GAAPAAAAGT DQVMSEVYLG RQICNVVACE
     GTERTERHET LGQWRNRLGN AGFETVHLGS NAYKQASTLL ALFAGGDGYK VEEKEGCLTL
     GWHTRPLIAT SAWRLAAP