TCX2_ARATH
ID TCX2_ARATH Reviewed; 674 AA.
AC F4JIF5; O23333;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Protein tesmin/TSO1-like CXC 2;
DE Short=AtTCX2;
DE AltName: Full=Protein TSO1-like 2;
DE Short=Protein SOL2;
GN Name=TCX2; Synonyms=SOL2; OrderedLocusNames=At4g14770;
GN ORFNames=dl3425c, FCAALL.306;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 TISSUE SPECIFICITY.
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 [5]
RP GENE FAMILY, NOMENCLATURE, ZINC-BINDING, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
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 all the aerial
CC organs with highest expression in flowers.
CC {ECO:0000269|PubMed:10769245, ECO:0000269|PubMed:18057042}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the late stage of pollen development
CC in tricellular and mature pollen. {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=CAB10256.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78519.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z97337; CAB10256.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161539; CAB78519.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83496.1; -; Genomic_DNA.
DR PIR; F71410; F71410.
DR RefSeq; NP_193213.5; NM_117562.7.
DR AlphaFoldDB; F4JIF5; -.
DR SMR; F4JIF5; -.
DR BioGRID; 12429; 5.
DR IntAct; F4JIF5; 4.
DR STRING; 3702.AT4G14770.1; -.
DR iPTMnet; F4JIF5; -.
DR PaxDb; F4JIF5; -.
DR PRIDE; F4JIF5; -.
DR ProteomicsDB; 246411; -.
DR EnsemblPlants; AT4G14770.1; AT4G14770.1; AT4G14770.
DR GeneID; 827132; -.
DR Gramene; AT4G14770.1; AT4G14770.1; AT4G14770.
DR KEGG; ath:AT4G14770; -.
DR Araport; AT4G14770; -.
DR TAIR; locus:2130220; AT4G14770.
DR eggNOG; KOG1171; Eukaryota.
DR HOGENOM; CLU_012297_1_0_1; -.
DR InParanoid; F4JIF5; -.
DR OMA; DSSPIAC; -.
DR OrthoDB; 267145at2759; -.
DR PRO; PR:F4JIF5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JIF5; baseline and differential.
DR Genevisible; F4JIF5; 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:0006355; P:regulation of transcription, DNA-templated; TAS: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; 2.
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..674
FT /note="Protein tesmin/TSO1-like CXC 2"
FT /id="PRO_0000418167"
FT DOMAIN 373..498
FT /note="CRC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00971"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 674 AA; 74054 MW; B732E47E002A29FE CRC64;
MDTPQKSITQ IGTPISKSRF EDSPVFNYIN SLSPIRPVRS IPNPNQFSSL NFTSPPSVFT
SPHLTSSHKE SRFFKTHNSS SSDPTNSVES QEDESTSHEE VPAEGEDTKG LNIDDCMREE
ASVETNLDDS VASPCGGNTT DLSLVPYAPT RGEDGSCEDN GMELQKMHDN VQGKTETPDW
ESLIADASEL LIFDSPDASE AFRCFMMQRA SNSEARFRNG VEKQTMQHDS NKEPESANAI
PYEAVSLLHR GIRRRCLDFE MPGNKQTSSE NNTAACESSS RCVVPSIGLH LNAILMSSKD
CKTNVTQDYS CSANIQVGLQ RSISTLQDSL DQTENEIRED ADQDVPVEPA LQELNLSSPK
KKRVKLDSGE GESCKRCNCK KSKCLKLYCE CFAAGVYCIE PCSCIDCFNK PIHEDVVLAT
RKQIESRNPL AFAPKVIRNS DSVQETGDDA SKTPASARHK RGCNCKKSNC LKKYCECYQG
GVGCSINCRC EGCKNAFGRK DGSSIDMEAE QEEENETSEK SRTAKSQQNT EVLMRKDMSS
ALPTTPTPIY RPELVQLPFS SSKNRMPPPQ SLLGGGSSSG IFNSQYLRKP DISLSQSRIE
KSFETVAVDG AEQMPEILIH SPIPNIKSVS PNGKRVSPPH MESSSSGSIL GRRNGGRKLI
LQSIPSFPSL TPQH
