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Database: UniProt
Entry: F4JUD2_ARATH
LinkDB: F4JUD2_ARATH
Original site: F4JUD2_ARATH 
ID   F4JUD2_ARATH            Unreviewed;       969 AA.
AC   F4JUD2;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Transcriptional corepressor LEUNIG {ECO:0000313|EMBL:AEE86077.1};
GN   Name=LUG {ECO:0000313|EMBL:AEE86077.1, ECO:0000313|TAIR:AT4G32551};
GN   Synonyms=LEUNIG {ECO:0000313|EMBL:AEE86077.1}, RON2
GN   {ECO:0000313|EMBL:AEE86077.1}, ROTUNDA 2
GN   {ECO:0000313|EMBL:AEE86077.1};
GN   OrderedLocusNames=At4g32551 {ECO:0000313|Araport:AT4G32551,
GN   ECO:0000313|EMBL:AEE86077.1};
GN   ORFNames=L23H3.30 {ECO:0000313|EMBL:AEE86077.1}, L23H3_30
GN   {ECO:0000313|EMBL:AEE86077.1};
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 {ECO:0000313|EMBL:AEE86077.1, ECO:0000313|Proteomes:UP000006548};
RN   [1] {ECO:0000313|EMBL:AEE86077.1, ECO:0000313|Proteomes:UP000006548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX   PubMed=10617198; DOI=10.1038/47134;
RG   EU;
RG   CSHL and WU Arabidopsis Sequencing Project;
RA   Mayer K., Schuller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Dusterhoft A., Stiekema W., Entian K.D., Terryn N., Harris B., Ansorge W.,
RA   Brandt P., Grivell L., Rieger M., Weichselgartner M., de Simone V.,
RA   Obermaier B., Mache R., Muller M., Kreis M., Delseny M., Puigdomenech P.,
RA   Watson M., Schmidtheini T., Reichert B., Portatelle D., Perez-Alonso M.,
RA   Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H.,
RA   Ridley P., Langham S.A., McCullagh B., Bilham L., Robben J.,
RA   Van der Schueren J., Grymonprez B., Chuang Y.J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E.,
RA   Brandt A., Peters S., van Staveren M., Dirske W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Kotter 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., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M.,
RA   Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M.,
RA   Benes V., Rechmann S., Borkova D., Blocker H., Scharfe M., Grimm M.,
RA   Lohnert T.H., Dose S., de Haan M., Maarse A., Schafer M., Muller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O.,
RA   Quigley F., Clabauld G., Mundlein A., Felber R., Schnabl S., Hiller R.,
RA   Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C.,
RA   Montfort 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., Sehkon 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., Nelson J.,
RA   Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J.,
RA   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., Hoffmann J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.,
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   [2] {ECO:0000313|Proteomes:UP000006548}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CP002687; AEE86077.1; -; Genomic_DNA.
DR   RefSeq; NP_001190891.1; NM_001203962.1.
DR   AlphaFoldDB; F4JUD2; -.
DR   SMR; F4JUD2; -.
DR   ProteomicsDB; 197680; -.
DR   EnsemblPlants; AT4G32551.2; AT4G32551.2; AT4G32551.
DR   GeneID; 829390; -.
DR   Gramene; AT4G32551.2; AT4G32551.2; AT4G32551.
DR   Araport; AT4G32551; -.
DR   TAIR; AT4G32551; LUG.
DR   OrthoDB; 1410379at2759; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JUD2; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:TAIR.
DR   GO; GO:0009908; P:flower development; IMP:TAIR.
DR   GO; GO:0080001; P:mucilage extrusion from seed coat; IMP:TAIR.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR006594; LisH.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR45093; TRANSCRIPTION ACTIVATOR MSS11; 1.
DR   PANTHER; PTHR45093:SF2; TRANSCRIPTION ACTIVATOR MSS11; 1.
DR   Pfam; PF08513; LisH; 1.
DR   Pfam; PF00400; WD40; 5.
DR   SMART; SM00667; LisH; 1.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50896; LISH; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE   1: Evidence at protein level;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F4JUD2,
KW   ECO:0007829|ProteomicsDB:F4JUD2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   REPEAT          685..726
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          727..762
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          770..812
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          852..877
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          937..969
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REGION          149..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          488..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        540..620
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   969 AA;  106520 MW;  9393F307E95636ED CRC64;
     MSQTNWEADK MLDVYIHDYL VKRDLKATAQ AFQAEGKVSS DPVAIDAPGG FLFEWWSVFW
     DIFIARTNEK HSEVAASYIE TQMIKAREQQ LQQSQHPQVS QQQQQQQQQQ IQMQQLLLQR
     AQQQQQQQQQ QHHHHQQQQQ QQQQQQQQQQ QQQQQHQNQP PSQQQQQQST PQHQQQPTPQ
     QQPQRRDGSH LANGSANGLV GNNSEPVMRQ NPGSGSSLAS KAYEERVKMP TQRESLDEAA
     MKRFGDNVGQ LLDPSHASIL KSAAASGQPA GQVLHSTSGG MSPQVQTRNQ QLPGSAVDIK
     SEINPVLTPR TAVPEGSLIG IPGRFAVLSV SFQLVKRVKC SISTSAHKNL LRINDWFPVS
     GSNQGSNNLT LKGWPLTGFD QLRSGLLQQQ KPFMQSQSFH QLNMLTPQHQ QQLMLAQQNL
     NSQSVSEENR RLKMLLNNRS MTLGKDGLGS SVGDVLPNVG SSLQPGGSLL PRGDTDMLLK
     LKMALLQQQQ QNQQQGGGNP PQPQPQPQPL NQLALTNPQP QSSNHSIHQQ EKLGGGGSIT
     MDGSISNSFR GNEQVLKNQS GRKRKQPVSS SGPANSSGTA NTAGPSPSSA PSTPSTHTPG
     DVISMPNLPH SGGSSKSMMM FGTEGTGTLT SPSNQLADMD RFVEDGSLDD NVESFLSQED
     GDQRDAVTRC MDVSKGFTFT EVNSVRASTT KVTCCHFSSD GKMLASAGHD KKAVLWYTDT
     MKPKTTLEEH TAMITDIRFS PSQLRLATSS FDKTVRVWDA DNKGYSLRTF MGHSSMVTSL
     DFHPIKDDLI CSCDNDNEIR YWSINNGSCT RVYKGGSTQI RFQPRVGKYL AASSANLVNV
     LDVETQAIRH SLQGHANPIN SVCWDPSGDF LASVSEDMVK VWTLGTGSEG ECVHELSCNG
     NKFQSCVFHP AYPSLLVIGC YQSLELWNMS ENKTMTLPAH EGLITSLAVS TATGLVASAS
     HDKLVKLWK
//
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