ID TCX6_ARATH Reviewed; 571 AA. AC Q9SL70; F4IUE5; Q8GUZ0; Q8GUZ1; Q8GUZ2; DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 02-SEP-2026, entry version 140. DE RecName: Full=Protein tesmin/TSO1-like CXC 6; DE Short=AtTCX6; GN Name=TCX6; OrderedLocusNames=At2g20110; ORFNames=T2G17.9; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."; RL Nature 402:761-768(1999). RN [2] 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 [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RT "Community-consensus reference genome of Arabidopsis thaliana Col-0."; RL Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-571 (ISOFORMS 1; 2 AND 3). RC STRAIN=cv. Columbia; RX PubMed=12481096; DOI=10.1104/pp.010207; RA Xiao Y.-L., Malik M., Whitelaw C.A., Town C.D.; RT "Cloning and sequencing of cDNAs for hypothetical genes from chromosome 2 RT of Arabidopsis."; RL Plant Physiol. 130:2118-2128(2002). RN [6] 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). CC -!- FUNCTION: Plays a role in development of both male and female CC reproductive tissues. {ECO:0000250}. CC -!- INTERACTION: CC Q9SL70; Q9LM76: PUB44; NbExp=3; IntAct=EBI-1238421, EBI-4466572; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9SL70-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9SL70-2; Sequence=VSP_044004; CC Name=3; CC IsoId=Q9SL70-3; Sequence=VSP_044003; CC -!- TISSUE SPECIFICITY: Ubiquitous but expressed mostly in flowers. CC {ECO:0000269|PubMed:18057042}. CC -!- DOMAIN: The cysteine-rich domain CRC binds zinc in vitro. CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice CC site. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing donor splice CC site. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the lin-54 family. {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; AC006081; AAD24386.1; -; Genomic_DNA. DR EMBL; CP002685; AEC06966.1; -; Genomic_DNA. DR EMBL; CP002685; AEC06967.1; -; Genomic_DNA. DR EMBL; OZ408684; CAO7035623.1; -; Genomic_DNA. DR EMBL; AB493556; BAH30394.1; -; mRNA. DR EMBL; AY163773; AAN85197.1; -; mRNA. DR EMBL; AY163774; AAN85198.1; -; mRNA. DR EMBL; AY163775; AAN85199.1; -; mRNA. DR PIR; B84585; B84585. DR RefSeq; NP_179601.1; NM_127569.3. [Q9SL70-1] DR RefSeq; NP_849995.1; NM_179664.2. [Q9SL70-2] DR AlphaFoldDB; Q9SL70; -. DR SMR; Q9SL70; -. DR BioGRID; 1884; 11. DR FunCoup; Q9SL70; 28. DR IntAct; Q9SL70; 9. DR STRING; 3702.Q9SL70; -. DR iPTMnet; Q9SL70; -. DR PaxDb; 3702-Q9SL70; -. DR ProteomicsDB; 234379; -. [Q9SL70-1] DR GeneID; 816530; -. DR KEGG; ath:AT2G20110; -. DR Araport; AT2G20110; -. DR TAIR; AT2G20110; -. DR eggNOG; KOG1171; Eukaryota. DR InParanoid; Q9SL70; -. DR PhylomeDB; Q9SL70; -. DR PRO; PR:Q9SL70; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; Q9SL70; baseline and differential. DR GO; GO:0005634; C:nucleus; ISM:TAIR. DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR InterPro; IPR005172; CRC. DR InterPro; IPR028307; Lin-54_fam. DR InterPro; IPR033467; Tesmin/TSO1-like_CXC. DR PANTHER; PTHR12446:SF34; PROTEIN LIN-54 HOMOLOG; 1. DR PANTHER; PTHR12446; TESMIN/TSO1-RELATED; 1. DR Pfam; PF03638; TCR; 2. DR SMART; SM01114; CXC; 2. DR PROSITE; PS51634; CRC; 1. PE 1: Evidence at protein level; KW Alternative splicing; Developmental protein; Metal-binding; Nucleus; KW Reference proteome; Zinc. FT CHAIN 1..571 FT /note="Protein tesmin/TSO1-like CXC 6" FT /id="PRO_0000418171" FT DOMAIN 117..241 FT /note="CRC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00971" FT REGION 1..52 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 92..119 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 293..325 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 370..411 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 507..571 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 7..16 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 293..319 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 373..388 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 508..539 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 540..557 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 331..334 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12481096" FT /id="VSP_044003" FT VAR_SEQ 475 FT /note="K -> KVFCLFVA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12481096" FT /id="VSP_044004" FT CONFLICT 520 FT /note="N -> T (in Ref. 5; AAN85197/AAN85198/AAN85199)" FT /evidence="ECO:0000305" SQ SEQUENCE 571 AA; 61313 MW; 36701C5FA62B3B89 CRC64; MGEGEEGDKF PPKTDEVTQE SMKSARQLDF TGGSSDVEHS HSNQASSMAA ASIPSPIVTV TRPIITSQAP PTVATPIPPP PQSQGIILHV PIRHPRPESP NSMPRPAGET RDGTPQKKKQ CNCKHSRCLK LYCECFASGT YCDGCNCVNC FNNVENEPAR RQAVESTLER NPNAFRPKIA ASPHGGRDNR EEVGDVVMLA RHNKGCHCKK SGCLKKYCEC FQANILCSEN CKCLDCKNFE GSEVRQSLFH GEHSHNLAYL QHANAAITGA IGSSGFASAP PPKRRKGQEI FFNQGTKDSS THRLGQANNG RTTSSQTGSR AGGNASLGPS KVVYKSLLAN IIKPMDVKAL CSVLVAVAGE AAKTLTEKRL ANQKETSVAS SVQDQGHVNN KAEKSGLEDS NADGSKGRSL SPETLALMCD ERDTMLMVAA SPNCSVEPTS QLPNGQDQVY AEQEKVVLTK FRDCLNRIIS CGEVKESNCS MSRMDLDTPV QTTVRIDPVV QQAPVANGVS QTAKQPSQLN TTTPNTSSQT ANGVSQTAKQ PSQLTTTTTT PNTSSQTHLH KTPALSEKKD L //