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GAI_GOSHI
ID   GAI_GOSHI               Reviewed;         537 AA.
AC   Q84TQ7; Q4ZIN2;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=DELLA protein GAI;
DE   AltName: Full=GhGAI;
DE   AltName: Full=Gibberellic acid-insensitive mutant protein;
GN   Name=GAI;
OS   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fiber;
RA   Luo M., Xiao Y., Hou L., Luo X., Li D., Zhang Z., Pei Y.;
RT   "Molecular cloning and expression analysis of a gene (GhGAI) from cotton
RT   (Gossypium hirsutum L.).";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Liao W.B., Cui B.M., Wei H.B., Yu X.L., Li J.H., Peng M.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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 represses
CC       transcription of GA-inducible genes. Upon GA application, it is
CC       degraded by the proteasome, allowing the GA signaling pathway (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The DELLA motif is required for its GA-induced degradation.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated. Upon GA application it is ubiquitinated, leading to
CC       its subsequent degradation (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GRAS family. DELLA subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY28970.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY208992; AAO62757.1; -; mRNA.
DR   EMBL; DQ006269; AAY28970.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; Q84TQ7; -.
DR   SMR; Q84TQ7; -.
DR   Proteomes; UP000189702; Genome assembly.
DR   GO; GO:0005634; C:nucleus; IDA:AgBase.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR   GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IDA:AgBase.
DR   GO; GO:0042538; P:hyperosmotic salinity response; IBA:GO_Central.
DR   GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0009938; P:negative regulation of gibberellic acid mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0010187; P:negative regulation of seed germination; IBA:GO_Central.
DR   GO; GO:2000273; P:positive regulation of signaling receptor activity; IDA:AgBase.
DR   GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IBA:GO_Central.
DR   GO; GO:2000033; P:regulation of seed dormancy process; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:AgBase.
DR   GO; GO:0009737; P:response to abscisic acid; IBA:GO_Central.
DR   GO; GO:0009723; P:response to ethylene; IBA:GO_Central.
DR   GO; GO:0009739; P:response to gibberellin; IDA:AgBase.
DR   GO; GO:0009863; P:salicylic acid mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0090378; P:seed trichome elongation; IDA:AgBase.
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   2: Evidence at transcript level;
KW   Gibberellin signaling pathway; Nucleus; Phosphoprotein; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..537
FT                   /note="DELLA protein GAI"
FT                   /id="PRO_0000132243"
FT   DOMAIN          162..533
FT                   /note="GRAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..223
FT                   /note="Leucine repeat I (LRI)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          241..306
FT                   /note="VHIID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          320..352
FT                   /note="Leucine repeat II (LRII)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          364..454
FT                   /note="PFYRE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          457..533
FT                   /note="SAW"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   MOTIF           37..41
FT                   /note="DELLA motif"
FT   MOTIF           272..276
FT                   /note="VHIID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   MOTIF           372..376
FT                   /note="LXXLL motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   CONFLICT        125
FT                   /note="A -> T (in Ref. 2; AAY28970)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="I -> N (in Ref. 2; AAY28970)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        167
FT                   /note="A -> T (in Ref. 2; AAY28970)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        242..243
FT                   /note="IP -> MH (in Ref. 2; AAY28970)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        265
FT                   /note="A -> T (in Ref. 2; AAY28970)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        270
FT                   /note="S -> N (in Ref. 2; AAY28970)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        314
FT                   /note="N -> D (in Ref. 2; AAY28970)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        327
FT                   /note="Q -> E (in Ref. 2; AAY28970)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339
FT                   /note="R -> P (in Ref. 2; AAY28970)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        437
FT                   /note="A -> P (in Ref. 2; AAY28970)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        482
FT                   /note="V -> F (in Ref. 2; AAY28970)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   537 AA;  58902 MW;  B9E01DE4761A62E1 CRC64;
     MKRDHQEISG SGSNPAESSS IKGKLWEEDP DAGGMDDELL AVLGYKVRSS DMADVAQKLE
     MLEKVMGTAQ EDGISQLGDT VHFNPSDLSG WVQNLLIEFN GSTTTPDPNF NDDSEYDLRA
     IPGVAAYPPV KSDPGLEITR KRAKTESSSS SSSTTTRPVV LIDSQEAGVR LVHTLMACAE
     AVQQDNLKLA DALVKHIGLL ASSQTGAMRK VATYFAEALA RRIYRIFPPD SLDPSYNDKL
     QIPFYETCPY LKFAHFTANQ AILEAFSMAS RVHVIDFGLK QGMQWPALMQ ALALRPGGPP
     AFRLTGIGPP QPDNTDALQQ VGWKLAQLAE RIGIEFEFRG FVANSLADLE PEMLDIRPPE
     IEVVAVNAVF ELHPLLARPG GIEKVVSSIK AMKPKIVTVV EQEANHNGPV FLDRFTEALH
     YYSTLFDSLE GSGVAPASQD LAMSELYLGR QICNVVACEG MDRVERHEPL TQWRTRMETA
     GVSPVHLGSN AYKQASMLLA LFASGDGYRV EENNGCLMLG WHTRPLIAHL GLATRWY
 
 
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