TTG1_ARATH
ID TTG1_ARATH Reviewed; 341 AA.
AC Q9XGN1; Q5PP66; Q9FT87;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein TRANSPARENT TESTA GLABRA 1;
GN Name=TTG1; OrderedLocusNames=At5g24520; ORFNames=K18P6_4, T31K7.8;
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], AND MUTANT TTG1-9.
RC STRAIN=cv. Columbia, cv. Landsberg erecta, cv. RLD, and cv. Wassilewskija;
RX PubMed=10402433; DOI=10.2307/3870753;
RA Walker A.R., Davison P.A., Bolognesi-Winfield A.C., James C.M.,
RA Srinivasan N., Blundell T.L., Esch J.J., Marks M.D., Gray J.C.;
RT "The TRANSPARENT TESTA GLABRA1 locus, which regulates trichome
RT differentiation and anthocyanin biosynthesis in Arabidopsis, encodes a WD40
RT repeat protein.";
RL Plant Cell 11:1337-1350(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT HLM.
RC STRAIN=cv. Est;
RA Bharti A.K., Khurana J.P.;
RT "Physiological and molecular characterization of transparent testa mutants
RT of Arabidopsis impaired in phenylpropanoid pathway.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND INTERACTION WITH GL3.
RX PubMed=11063707; DOI=10.1093/genetics/156.3.1349;
RA Payne C.T., Zhang F., Lloyd A.M.;
RT "GL3 encodes a bHLH protein that regulates trichome development in
RT arabidopsis through interaction with GL1 and TTG1.";
RL Genetics 156:1349-1362(2000).
RN [8]
RP FUNCTION.
RX PubMed=11585796; DOI=10.1242/dev.128.19.3697;
RA Lin Y., Schiefelbein J.;
RT "Embryonic control of epidermal cell patterning in the root and hypocotyl
RT of Arabidopsis.";
RL Development 128:3697-3705(2001).
RN [9]
RP INTERACTION WITH BHLH2.
RX PubMed=12917293; DOI=10.1242/dev.00681;
RA Zhang F., Gonzalez A., Zhao M., Payne C.T., Lloyd A.M.;
RT "A network of redundant bHLH proteins functions in all TTG1-dependent
RT pathways of Arabidopsis.";
RL Development 130:4859-4869(2003).
RN [10]
RP INTERACTION WITH GL3.
RX PubMed=14561633; DOI=10.1242/dev.00812;
RA Esch J.J., Chen M., Sanders M., Hillestad M., Ndkium S., Idelkope B.,
RA Neizer J., Marks M.D.;
RT "A contradictory GLABRA3 allele helps define gene interactions controlling
RT trichome development in Arabidopsis.";
RL Development 130:5885-5894(2003).
RN [11]
RP INTERACTION WITH GL3.
RX PubMed=15728674; DOI=10.1242/dev.01708;
RA Kirik V., Lee M.M., Wester K., Herrmann U., Zheng Z., Oppenheimer D.,
RA Schiefelbein J., Hulskamp M.;
RT "Functional diversification of MYB23 and GL1 genes in trichome
RT morphogenesis and initiation.";
RL Development 132:1477-1485(2005).
RN [12]
RP INTERACTION WITH CCT8.
RX PubMed=21868675; DOI=10.1126/science.1205727;
RA Xu X.M., Wang J., Xuan Z., Goldshmidt A., Borrill P.G., Hariharan N.,
RA Kim J.Y., Jackson D.;
RT "Chaperonins facilitate KNOTTED1 cell-to-cell trafficking and stem cell
RT function.";
RL Science 333:1141-1144(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: May regulate MYC transcription factors. Involved in epidermal
CC cell fate specification such as trichome and root hair development,
CC seed mucilage production, and anthocyanin biosynthesis by acting at the
CC dihydroflavonol-4-reductase (DFR) step. Together with GL1 and GL3,
CC promotes trichome formation. Activates the transcription of GL2.
CC {ECO:0000269|PubMed:11063707, ECO:0000269|PubMed:11585796}.
CC -!- SUBUNIT: Interacts directly with GL3 and BHLH2. Part of a complex made
CC of GL1, GL3 or BHLH2, and TTG1. Interacts with CCT8 (PubMed:21868675).
CC {ECO:0000269|PubMed:11063707, ECO:0000269|PubMed:12917293,
CC ECO:0000269|PubMed:14561633, ECO:0000269|PubMed:15728674,
CC ECO:0000269|PubMed:21868675}.
CC -!- INTERACTION:
CC Q9XGN1; Q9LKL2: APRR1; NbExp=4; IntAct=EBI-395803, EBI-618423;
CC Q9XGN1; C0SV91: At2g46670; NbExp=3; IntAct=EBI-395803, EBI-15192193;
CC Q9XGN1; Q9FIX5: BHLH92; NbExp=8; IntAct=EBI-395803, EBI-15199233;
CC Q9XGN1; Q9FN69: GL3; NbExp=3; IntAct=EBI-395803, EBI-533348;
CC Q9XGN1; Q8VZS3: HHO2; NbExp=3; IntAct=EBI-395803, EBI-4429217;
CC Q9XGN1; Q9LVS0: KUA1; NbExp=3; IntAct=EBI-395803, EBI-15200088;
CC Q9XGN1; Q9FDW1: MYB44; NbExp=3; IntAct=EBI-395803, EBI-15192813;
CC Q9XGN1; B5X4Z4: NAGS2; NbExp=3; IntAct=EBI-395803, EBI-15197867;
CC Q9XGN1; F4KGY6: RVE1; NbExp=4; IntAct=EBI-395803, EBI-15194459;
CC Q9XGN1; Q9FT81: TT8; NbExp=5; IntAct=EBI-395803, EBI-395790;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Roots, leaves, stems, meristems, flowers and flower
CC buds.
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DR EMBL; AJ133743; CAB45372.1; -; Genomic_DNA.
DR EMBL; AJ251522; CAC10523.1; -; Genomic_DNA.
DR EMBL; AJ251523; CAC10524.1; -; Genomic_DNA.
DR EMBL; AB010068; BAB11204.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93319.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93320.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93321.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69758.1; -; Genomic_DNA.
DR EMBL; BT020231; AAV74225.1; -; mRNA.
DR EMBL; BT020513; AAW39014.1; -; mRNA.
DR EMBL; AK227211; BAE99249.1; -; mRNA.
DR RefSeq; NP_001318637.1; NM_001343878.1.
DR RefSeq; NP_197840.1; NM_122360.2.
DR RefSeq; NP_851069.1; NM_180738.3.
DR RefSeq; NP_851070.1; NM_180739.2.
DR AlphaFoldDB; Q9XGN1; -.
DR SMR; Q9XGN1; -.
DR BioGRID; 17798; 37.
DR IntAct; Q9XGN1; 29.
DR STRING; 3702.AT5G24520.1; -.
DR iPTMnet; Q9XGN1; -.
DR PaxDb; Q9XGN1; -.
DR PRIDE; Q9XGN1; -.
DR ProteomicsDB; 232363; -.
DR EnsemblPlants; AT5G24520.1; AT5G24520.1; AT5G24520.
DR EnsemblPlants; AT5G24520.2; AT5G24520.2; AT5G24520.
DR EnsemblPlants; AT5G24520.3; AT5G24520.3; AT5G24520.
DR EnsemblPlants; AT5G24520.4; AT5G24520.4; AT5G24520.
DR GeneID; 832523; -.
DR Gramene; AT5G24520.1; AT5G24520.1; AT5G24520.
DR Gramene; AT5G24520.2; AT5G24520.2; AT5G24520.
DR Gramene; AT5G24520.3; AT5G24520.3; AT5G24520.
DR Gramene; AT5G24520.4; AT5G24520.4; AT5G24520.
DR KEGG; ath:AT5G24520; -.
DR Araport; AT5G24520; -.
DR TAIR; locus:2153914; AT5G24520.
DR eggNOG; KOG0290; Eukaryota.
DR HOGENOM; CLU_013694_0_0_1; -.
DR InParanoid; Q9XGN1; -.
DR OMA; NEDWMAI; -.
DR OrthoDB; 750776at2759; -.
DR PhylomeDB; Q9XGN1; -.
DR PRO; PR:Q9XGN1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9XGN1; baseline and differential.
DR Genevisible; Q9XGN1; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0045165; P:cell fate commitment; IMP:TAIR.
DR GO; GO:0009957; P:epidermal cell fate specification; IMP:TAIR.
DR GO; GO:0032880; P:regulation of protein localization; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR GO; GO:0009723; P:response to ethylene; IEP:TAIR.
DR GO; GO:0010026; P:trichome differentiation; IMP:TAIR.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR045159; DCAF7-like.
DR InterPro; IPR031104; TTG1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19919; PTHR19919; 1.
DR PANTHER; PTHR19919:SF10; PTHR19919:SF10; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Developmental protein; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..341
FT /note="Protein TRANSPARENT TESTA GLABRA 1"
FT /id="PRO_0000051307"
FT REPEAT 74..118
FT /note="WD 1"
FT REPEAT 130..170
FT /note="WD 2"
FT REPEAT 173..211
FT /note="WD 3"
FT REPEAT 262..302
FT /note="WD 4"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 101
FT /note="S->F: In hlm."
FT MUTAGEN 282
FT /note="S->F: In ttg1-9; glabra and loss of seed
FT pigmentation."
SQ SEQUENCE 341 AA; 37892 MW; B247738AE41FEE38 CRC64;
MDNSAPDSLS RSETAVTYDS PYPLYAMAFS SLRSSSGHRI AVGSFLEDYN NRIDILSFDS
DSMTVKPLPN LSFEHPYPPT KLMFSPPSLR RPSSGDLLAS SGDFLRLWEI NEDSSTVEPI
SVLNNSKTSE FCAPLTSFDW NDVEPKRLGT CSIDTTCTIW DIEKSVVETQ LIAHDKEVHD
IAWGEARVFA SVSADGSVRI FDLRDKEHST IIYESPQPDT PLLRLAWNKQ DLRYMATILM
DSNKVVILDI RSPTMPVAEL ERHQASVNAI AWAPQSCKHI CSGGDDTQAL IWELPTVAGP
NGIDPMSVYS AGSEINQLQW SSSQPDWIGI AFANKMQLLR V
