TCX6_ARATH
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 03-AUG-2022, entry version 125.
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 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 [4]
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 [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).
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}.
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DR EMBL; AC006081; AAD24386.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06966.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06967.1; -; 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 IntAct; Q9SL70; 9.
DR STRING; 3702.AT2G20110.2; -.
DR iPTMnet; Q9SL70; -.
DR PaxDb; Q9SL70; -.
DR PRIDE; Q9SL70; -.
DR ProteomicsDB; 234379; -. [Q9SL70-1]
DR EnsemblPlants; AT2G20110.1; AT2G20110.1; AT2G20110. [Q9SL70-1]
DR EnsemblPlants; AT2G20110.2; AT2G20110.2; AT2G20110. [Q9SL70-2]
DR GeneID; 816530; -.
DR Gramene; AT2G20110.1; AT2G20110.1; AT2G20110. [Q9SL70-1]
DR Gramene; AT2G20110.2; AT2G20110.2; AT2G20110. [Q9SL70-2]
DR KEGG; ath:AT2G20110; -.
DR Araport; AT2G20110; -.
DR TAIR; locus:2061683; AT2G20110.
DR eggNOG; KOG1171; Eukaryota.
DR InParanoid; Q9SL70; -.
DR OrthoDB; 704611at2759; -.
DR PhylomeDB; Q9SL70; -.
DR PRO; PR:Q9SL70; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SL70; baseline and differential.
DR Genevisible; Q9SL70; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR005172; CRC.
DR InterPro; IPR028307; Lin-54_fam.
DR InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR PANTHER; PTHR12446; PTHR12446; 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 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..561
FT /note="Polar residues"
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. 4; 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
