TGA1B_MAIZE
ID TGA1B_MAIZE Reviewed; 432 AA.
AC Q49I57; G5D585;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Teosinte glume architecture 1 {ECO:0000303|PubMed:16079849};
GN Name=TGA1 {ECO:0000303|PubMed:16079849};
GN ORFNames=GRMZM2G101511 {ECO:0000305},
GN ZEAMMB73_922217 {ECO:0000312|EMBL:AFW61574.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. B73;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Maize Genome Sequencing Project;
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 314-432.
RX PubMed=21954998; DOI=10.1111/j.1469-8137.2011.03908.x;
RA Preston J.C., Wang H., Kursel L., Doebley J., Kellogg E.A.;
RT "The role of teosinte glume architecture (tga1) in coordinated regulation
RT and evolution of grass glumes and inflorescence axes.";
RL New Phytol. 193:204-215(2012).
CC -!- FUNCTION: SBP transcriptional regulator probably involved in the
CC domestication of maize. Acts as a transcriptional repressor binding to
CC a 5'-GTAC-3' motif. May repress the growth of lateral branches in
CC length and numbers. {ECO:0000250|UniProtKB:Q49I55}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000250|UniProtKB:Q49I55}.
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:0000250|UniProtKB:Q49I55}.
CC -!- DOMAIN: The N-terminal domain is necessary for dimerization.
CC {ECO:0000250|UniProtKB:Q49I55}.
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 {ECO:0000250|UniProtKB:Q49I55}.
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DR EMBL; AY883559; AAX83872.1; -; Genomic_DNA.
DR EMBL; CM000780; AFW61574.1; -; Genomic_DNA.
DR EMBL; JN560749; AEP96351.1; -; Genomic_DNA.
DR RefSeq; XP_008678396.1; XM_008680174.1.
DR AlphaFoldDB; Q49I57; -.
DR SMR; Q49I57; -.
DR STRING; 4577.GRMZM2G101511_P02; -.
DR EnsemblPlants; Zm00001eb175150_T003; Zm00001eb175150_P003; Zm00001eb175150.
DR GeneID; 103653213; -.
DR Gramene; Zm00001eb175150_T003; Zm00001eb175150_P003; Zm00001eb175150.
DR eggNOG; ENOG502QRGA; Eukaryota.
DR HOGENOM; CLU_042475_0_0_1; -.
DR OMA; WPRIARS; -.
DR OrthoDB; 916847at2759; -.
DR Proteomes; UP000007305; Chromosome 4.
DR ExpressionAtlas; Q49I57; 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 3: Inferred from homology;
KW Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..432
FT /note="Teosinte glume architecture 1"
FT /id="PRO_0000434102"
FT ZN_FING 102..179
FT /note="SBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT REGION 20..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 409..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
SQ SEQUENCE 432 AA; 45168 MW; 3DDB98892D58B971 CRC64;
MDWDLNAAGA WDLAELERDH AAAAPSSGGH AANAAAAGTG TESRPPAPGA AGAPAECSVD
LKLGGMGECE PGAARREREA AAGAAKRPRP AGPGGQQQQQ QCPSCAVDGC RADLGKCRDY
HRRHKVCEAH SKTPVVVVAG REMRFCQQCS RFHLLAEFDA DKRSCRKRLD GHNRRRRKPQ
PDTMASASFI ASQQGTRFSP FAHPRLEASW PPGVMKTEES PYHITHQIPL GSSSSSRQQH
FVALGAATPA YAKEGRRFPF LQEGEISFAT GVVLEPPAAA PACQPLLRTG APSESSGAGG
SKMFSDQGLA RVLDSDCALS LLSAPANSSG IDVSRMVRPT EHVPMAQQPV VPGLQFGSAS
WFPRPQASTG GSFVPSCPAA VEGEQQLNAV LGPNDSEVSM NYGGMFHVGG GSGGGEGSSD
GGTSSSMPFS WQ
