TCX3_ARATH
ID TCX3_ARATH Reviewed; 609 AA.
AC Q8L548; Q9LUI5; Q9M679;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protein tesmin/TSO1-like CXC 3;
DE Short=AtTCX3;
DE AltName: Full=Protein TSO1-like 1;
DE Short=Protein SOL1;
GN Name=TCX3; Synonyms=SOL1; OrderedLocusNames=At3g22760; ORFNames=MWI23.13;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10769245; DOI=10.1242/dev.127.10.2219;
RA Hauser B.A., He J.Q., Park S.O., Gasser C.S.;
RT "TSO1 is a novel protein that modulates cytokinesis and cell expansion in
RT Arabidopsis.";
RL Development 127:2219-2226(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY, NOMENCLATURE, ZINC-BINDING, AND TISSUE SPECIFICITY.
RX PubMed=18057042; DOI=10.1093/jxb/erm215;
RA Andersen S.U., Algreen-Petersen R.G., Hoedl M., Jurkiewicz A.,
RA Cvitanich C., Braunschweig U., Schauser L., Oh S.A., Twell D., Jensen E.O.;
RT "The conserved cysteine-rich domain of a tesmin/TSO1-like protein binds
RT zinc in vitro and TSO1 is required for both male and female fertility in
RT Arabidopsis thaliana.";
RL J. Exp. Bot. 58:3657-3670(2007).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=22072982; DOI=10.1371/journal.pgen.1002352;
RA Sijacic P., Wang W., Liu Z.;
RT "Recessive antimorphic alleles overcome functionally redundant loci to
RT reveal TSO1 function in Arabidopsis flowers and meristems.";
RL PLoS Genet. 7:E1002352-E1002352(2011).
CC -!- FUNCTION: Plays a role in development of both male and female
CC reproductive tissues. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous but expressed mostly in flowers and at
CC significant levels in leaves. Detected with highest levels in
CC developing ovules and microspores, and in petals.
CC {ECO:0000269|PubMed:10769245, ECO:0000269|PubMed:18057042}.
CC -!- DOMAIN: The cysteine-rich domain CRC binds zinc in vitro.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:22072982}.
CC -!- SIMILARITY: Belongs to the lin-54 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01251.1; Type=Erroneous gene model prediction; Evidence={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; AF205142; AAF69125.1; -; mRNA.
DR EMBL; AB022223; BAB01251.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76674.1; -; Genomic_DNA.
DR EMBL; AY099653; AAM20504.1; -; mRNA.
DR EMBL; AY128837; AAM91237.1; -; mRNA.
DR RefSeq; NP_566717.1; NM_113175.2.
DR AlphaFoldDB; Q8L548; -.
DR SMR; Q8L548; -.
DR STRING; 3702.AT3G22760.1; -.
DR PaxDb; Q8L548; -.
DR PRIDE; Q8L548; -.
DR EnsemblPlants; AT3G22760.1; AT3G22760.1; AT3G22760.
DR GeneID; 821847; -.
DR Gramene; AT3G22760.1; AT3G22760.1; AT3G22760.
DR KEGG; ath:AT3G22760; -.
DR Araport; AT3G22760; -.
DR TAIR; locus:2094344; AT3G22760.
DR eggNOG; KOG1171; Eukaryota.
DR HOGENOM; CLU_012297_1_0_1; -.
DR InParanoid; Q8L548; -.
DR OMA; NDGACEY; -.
DR OrthoDB; 267145at2759; -.
DR PhylomeDB; Q8L548; -.
DR PRO; PR:Q8L548; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8L548; baseline and differential.
DR Genevisible; Q8L548; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0010375; P:stomatal complex patterning; IGI:TAIR.
DR GO; GO:0010440; P:stomatal lineage progression; IGI:TAIR.
DR InterPro; IPR005172; CRC.
DR InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR InterPro; IPR044522; TSO1-like.
DR PANTHER; PTHR46159; PTHR46159; 1.
DR Pfam; PF03638; TCR; 2.
DR SMART; SM01114; CXC; 2.
DR PROSITE; PS51634; CRC; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Metal-binding; Nucleus; Reference proteome; Zinc.
FT CHAIN 1..609
FT /note="Protein tesmin/TSO1-like CXC 3"
FT /id="PRO_0000418168"
FT DOMAIN 326..451
FT /note="CRC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00971"
FT REGION 69..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 109
FT /note="T -> L (in Ref. 1; AAF69125)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="G -> E (in Ref. 1; AAF69125)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 609 AA; 66654 MW; 1E29C3E3451F941B CRC64;
MDTPEKSETQ IGTPVSKLKV EDSPVFSYIC NLSPIKTIKP IPITCPLSSL NYASPPSVFT
SPHAVSHKES RFRSQKDVSA SKEVGEEEAL VGSEPEQSYK NDCNTPRVTN DVKDNGCGKD
LQVMMDNVKK KSDTPDWETL IAATTELIYG SPRESEAFSC LLKKTSNSEA RLRGSITATS
VAVTNTDVVN NESESVDALS ILHRGVRRRC LDFEVKGNNQ QTLGESSSSC VVPSIGLHLN
TIAMSSKDKN VANEYSFSGN IKVGVQSSLT PVLHSQHDIV RENESGKDSG QIIEVVPKSL
ASVDLTPISP KKKRRKSEQS GEGDSSCKRC NCKKSKCLKL YCECFAAGFY CIEPCSCINC
FNKPIHKDVV LATRKQIESR NPLAFAPKVI RNSDSIIEVG EDASKTPASA RHKRGCNCKK
SNCLKKYCEC YQGGVGCSIN CRCEGCKNAF GRKDGSLFEQ DEENETSGTP GTKKTQQNVE
LFKPAAPPST PIPFRQPLAQ LPISSNNRLL PPQSHFHHGA IGSSSSGIYN IRKPDMSLLS
HSRIETITED IDDMSENLIH SPITTLSPNS KRVSLSHLDS PESTPWRRNG GGRNLIRSFP
TFPSLTPHH
