TGA1W_MAIZE
ID TGA1W_MAIZE Reviewed; 431 AA.
AC Q49I55;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Teosinte glume architecture 1 {ECO:0000303|PubMed:16079849};
GN Name=TGA1 {ECO:0000303|PubMed:16079849};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000312|EMBL:AAX83874.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, MUTAGENESIS OF LEU-5,
RP AND TISSUE SPECIFICITY.
RC STRAIN=cv. Wisconsin 22;
RX PubMed=16079849; DOI=10.1038/nature03863;
RA Wang H., Nussbaum-Wagler T., Li B., Zhao Q., Vigouroux Y., Faller M.,
RA Bomblies K., Lukens L., Doebley J.F.;
RT "The origin of the naked grains of maize.";
RL Nature 436:714-719(2005).
RN [2]
RP FUNCTION, SUBUNIT, AND DOMAIN.
RC STRAIN=cv. Wisconsin 22;
RX PubMed=25943393; DOI=10.1534/genetics.115.175752;
RA Wang H., Studer A.J., Zhao Q., Meeley R., Doebley J.F.;
RT "Evidence that the origin of naked kernels during Maize domestication was
RT caused by a single amino acid substitution in tga1.";
RL Genetics 200:965-974(2015).
CC -!- FUNCTION: SBP transcriptional regulator probably involved in the
CC domestication of maize (PubMed:16079849). Acts as a transcriptional
CC repressor binding to a 5'-GTAC-3' motif (PubMed:25943393). May repress
CC the growth of lateral branches in length and numbers (PubMed:25943393).
CC {ECO:0000269|PubMed:16079849, ECO:0000269|PubMed:25943393}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:25943393}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in immature ears and weakly in
CC husks. Found in the inflorescence meristem of the developing ear, in
CC the spikelet pair primordia, the glume primordia, the cupule forming
CC region and other floral organs. Not detected in other tissues.
CC {ECO:0000269|PubMed:16079849}.
CC -!- DOMAIN: The N-terminal domain is necessary for dimerization.
CC {ECO:0000269|PubMed:25943393}.
CC -!- MISCELLANEOUS: A single Lys to Asn substitution at position 6 is the
CC probable cause of the transition from the hardened fruitcase
CC surrounding the kernels in teosinte to the cob that bears naked grains
CC in maize. This substitution is not affecting the DNA binding site
CC specificity, but increases the stability of the homodimers
CC (PubMed:25943393). {ECO:0000269|PubMed:16079849,
CC ECO:0000269|PubMed:25943393}.
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DR EMBL; AY883560; AAX83873.1; -; mRNA.
DR EMBL; AY883563; AAX83874.1; -; Genomic_DNA.
DR EMBL; AY883561; AAX83874.1; JOINED; Genomic_DNA.
DR EMBL; AY883562; AAX83874.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q49I55; -.
DR SMR; Q49I55; -.
DR PRIDE; Q49I55; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q49I55; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..431
FT /note="Teosinte glume architecture 1"
FT /id="PRO_0000434103"
FT ZN_FING 101..178
FT /note="SBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT REGION 18..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 129
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="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 152
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 MUTAGEN 5
FT /note="L->F: In tga1-ems1; encased kernels."
FT /evidence="ECO:0000269|PubMed:16079849"
SQ SEQUENCE 431 AA; 45072 MW; 51577704EE4AA4C7 CRC64;
MDWDLNAAGA WDLAELEQDH AAAAPSSGGH AANAAAAGTG TESRPPAPGA AGAPAECSVD
LKLGGMGECE PGAARREREA AAGAAKRPRP AGPGGQQQQQ CPSCAVDGCR ADLGKCRDYH
RRHKVCEAHS KTPVVVVAGR EMRFCQQCSR FHLLAEFDAD KRSCRKRLDG HNRRRRKPQP
DTMASASFIA SQQGTRFSPF AHPRLEASWP PGVMKTEESP YHITHQIPLG SSSSSRQQHF
VALGAATPAY AKEGRRFPFL QEGEISFATG VVLEPPAAAP ACQPLLRTGA PSESSGAGGS
KMFSDQGLAR VLDSDCALSL LSAPANSSGI DVSRMVRPTE HVPMAQQPVV PGLQFGSASW
FPRPQASTGG SFVPFCPAAV EGEQQLNAVL GPNDSEVSMN YGGMFHVGGG SGGGEGSSDG
GTSSSMPFSW Q
