TT1_ARATH
ID TT1_ARATH Reviewed; 303 AA.
AC Q8VWG3; C0SUZ2; Q8VWL1;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein TRANSPARENT TESTA 1;
DE AltName: Full=TTL1;
DE AltName: Full=WIP-domain protein 1 {ECO:0000303|PubMed:20541552};
DE AltName: Full=Zinc finger protein TT1;
GN Name=TT1 {ECO:0000303|PubMed:11782451};
GN Synonyms=WIP1 {ECO:0000303|PubMed:20541552}; OrderedLocusNames=At1g34790;
GN ORFNames=F11O6.15;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=11782451; DOI=10.1101/gad.212702;
RA Sagasser M., Lu G.-H., Hahlbrock K., Weisshaar B.;
RT "A. thaliana TRANSPARENT TESTA 1 is involved in seed coat development and
RT defines the WIP subfamily of plant zinc finger proteins.";
RL Genes Dev. 16:138-149(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND ZINC-FINGER.
RX PubMed=20541552; DOI=10.1016/j.febslet.2010.06.007;
RA Appelhagen I., Huep G., Lu G.H., Strompen G., Weisshaar B., Sagasser M.;
RT "Weird fingers: functional analysis of WIP domain proteins.";
RL FEBS Lett. 584:3116-3122(2010).
RN [6]
RP FUNCTION, SUBUNIT, INTERACTION WITH MYB75; TT2 AND TT16, SUBCELLULAR
RP LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND DISRUPTION PHENOTYPE.
RX PubMed=21477081; DOI=10.1111/j.1365-313x.2011.04603.x;
RA Appelhagen I., Lu G.H., Huep G., Schmelzer E., Weisshaar B., Sagasser M.;
RT "TRANSPARENT TESTA1 interacts with R2R3-MYB factors and affects early and
RT late steps of flavonoid biosynthesis in the endothelium of Arabidopsis
RT thaliana seeds.";
RL Plant J. 67:406-419(2011).
CC -!- FUNCTION: May act as a transcriptional regulator involved in the
CC differentiation of young endothelium. Altered differentiation results
CC in incompetence for pigments synthesis and the lack of condensed
CC tannins in the seed coat (PubMed:21477081). Plays a role in the
CC regulatory network controlling flavonoid accumulation in endothelium
CC cells during seed development (PubMed:21477081).
CC {ECO:0000269|PubMed:11782451, ECO:0000269|PubMed:21477081}.
CC -!- SUBUNIT: Can form homodimers. Interacts with MYB75, TT2 and TT16.
CC {ECO:0000269|PubMed:21477081}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11782451,
CC ECO:0000269|PubMed:20541552, ECO:0000269|PubMed:21477081}.
CC -!- TISSUE SPECIFICITY: Restricted to the endothelium, the innermost cell
CC layer of the seed coat and detected to a lesser extent in the other
CC cell layers of the testa. {ECO:0000269|PubMed:11782451}.
CC -!- DEVELOPMENTAL STAGE: Developing ovules and young seeds.
CC {ECO:0000269|PubMed:11782451}.
CC -!- DISRUPTION PHENOTYPE: Lack of flavanoid pigment accumulation in the
CC seed coat endothelium (transparent testa phenotype).
CC {ECO:0000269|PubMed:21477081}.
CC -!- SIMILARITY: Belongs to the WIP C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF190298; AAL66406.1; -; mRNA.
DR EMBL; AF190297; AAL66405.1; -; Genomic_DNA.
DR EMBL; AJ318491; CAC86393.1; -; mRNA.
DR EMBL; AF190299; AAL66407.1; -; Genomic_DNA.
DR EMBL; AC018460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE31740.1; -; Genomic_DNA.
DR EMBL; AB493495; BAH30333.1; -; mRNA.
DR RefSeq; NP_174737.2; NM_103201.3.
DR AlphaFoldDB; Q8VWG3; -.
DR BioGRID; 25618; 4.
DR STRING; 3702.AT1G34790.1; -.
DR PaxDb; Q8VWG3; -.
DR PRIDE; Q8VWG3; -.
DR EnsemblPlants; AT1G34790.1; AT1G34790.1; AT1G34790.
DR GeneID; 840386; -.
DR Gramene; AT1G34790.1; AT1G34790.1; AT1G34790.
DR KEGG; ath:AT1G34790; -.
DR Araport; AT1G34790; -.
DR TAIR; locus:2008386; AT1G34790.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_052255_0_1_1; -.
DR InParanoid; Q8VWG3; -.
DR OMA; KAYWIPT; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8VWG3; -.
DR PRO; PR:Q8VWG3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VWG3; baseline.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IMP:TAIR.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR029789; TT1-like.
DR InterPro; IPR043584; WIP1/2/3/4/5/6.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45878; PTHR45878; 1.
DR PANTHER; PTHR45878:SF17; PTHR45878:SF17; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..303
FT /note="Protein TRANSPARENT TESTA 1"
FT /id="PRO_0000047840"
FT ZN_FING 145..167
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 192..224
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000303|PubMed:20541552"
FT ZN_FING 229..251
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000303|PubMed:20541552"
FT ZN_FING 255..280
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000303|PubMed:20541552"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 66..84
FT /evidence="ECO:0000255"
FT MOTIF 221..224
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:21477081"
FT MOTIF 264..267
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:21477081"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..82
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 201
FT /note="H -> N (in strain: cv. Landsberg erecta)"
FT VARIANT 301
FT /note="L -> F (in strain: cv. Landsberg erecta)"
SQ SEQUENCE 303 AA; 34512 MW; CC1A47D942B83A3B CRC64;
MESPPLYEIS SSSSSEKPRH HFQSLDLFPN LNQNSCINNT LIEPLPLIDR INLNSNLDLN
PNPLYAEEGE QEEEEEEEED REVDVDLHIG LPGFGKPSND AKQLKKRNGK EIATYDAGKG
IENELSGKAY WIPAPEQILI GFTHFSCHVC FKTFNRYNNL QMHMWGHGSQ YRKGPESLKG
TQPRAMLGIP CYCCVEGCRN HIDHPRSKPL KDFRTLQTHY KRKHGHKPFS CRLCGKLLAV
KGDWRTHEKN CGKRWVCVCG SDFKHKRSLK DHVKAFGSGH GPYPTGLFEE QASNSSVSET
LFF
