DOT3_ARATH
ID DOT3_ARATH Reviewed; 607 AA.
AC Q9LFU0;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=BTB/POZ domain-containing protein DOT3;
DE AltName: Full=Protein DEFECTIVELY ORGANIZED TRIBUTARIES 3 {ECO:0000303|PubMed:18643975};
GN Name=DOT3 {ECO:0000303|PubMed:18643975}; OrderedLocusNames=At5g10250;
GN ORFNames=F18D22.20;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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 DOMAIN BTB.
RX PubMed=15749712; DOI=10.1074/jbc.m413247200;
RA Gingerich D.J., Gagne J.M., Salter D.W., Hellmann H., Estelle M., Ma L.,
RA Vierstra R.D.;
RT "Cullins 3a and 3b assemble with members of the broad
RT complex/tramtrack/bric-a-brac (BTB) protein family to form essential
RT ubiquitin-protein ligases (E3s) in Arabidopsis.";
RL J. Biol. Chem. 280:18810-18821(2005).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18643975; DOI=10.1111/j.1365-313x.2008.03595.x;
RA Petricka J.J., Clay N.K., Nelson T.M.;
RT "Vein patterning screens and the defectively organized tributaries mutants
RT in Arabidopsis thaliana.";
RL Plant J. 56:251-263(2008).
CC -!- FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin-
CC protein ligase complex (CUL3-RBX1-BTB) which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins (By similarity). Involved in leaf vasculature patterning
CC (PubMed:18643975). {ECO:0000250, ECO:0000269|PubMed:18643975}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- TISSUE SPECIFICITY: Expressed in emerging leaf primordia.
CC {ECO:0000269|PubMed:18643975}.
CC -!- DOMAIN: The BTB/POZ domain mediates the interaction with some component
CC of ubiquitin ligase complexes. {ECO:0000269|PubMed:15749712}.
CC -!- DISRUPTION PHENOTYPE: Defects in shoot and primary root growth and
CC aberrant parallel venation pattern in juvenile leaves.
CC {ECO:0000269|PubMed:18643975}.
CC -!- SIMILARITY: Belongs to the NPH3 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00982}.
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DR EMBL; AL360334; CAB96681.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91513.1; -; Genomic_DNA.
DR PIR; T50813; T50813.
DR RefSeq; NP_196587.1; NM_121063.2.
DR AlphaFoldDB; Q9LFU0; -.
DR SMR; Q9LFU0; -.
DR STRING; 3702.AT5G10250.1; -.
DR PaxDb; Q9LFU0; -.
DR PRIDE; Q9LFU0; -.
DR EnsemblPlants; AT5G10250.1; AT5G10250.1; AT5G10250.
DR GeneID; 830889; -.
DR Gramene; AT5G10250.1; AT5G10250.1; AT5G10250.
DR KEGG; ath:AT5G10250; -.
DR Araport; AT5G10250; -.
DR TAIR; locus:2145387; AT5G10250.
DR eggNOG; ENOG502QR2D; Eukaryota.
DR HOGENOM; CLU_005994_6_1_1; -.
DR InParanoid; Q9LFU0; -.
DR PhylomeDB; Q9LFU0; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LFU0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFU0; baseline and differential.
DR Genevisible; Q9LFU0; AT.
DR GO; GO:0010588; P:cotyledon vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:0010305; P:leaf vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IMP:TAIR.
DR GO; GO:0080022; P:primary root development; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0048367; P:shoot system development; IMP:TAIR.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR043454; NPH3/RPT2-like.
DR InterPro; IPR027356; NPH3_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR32370; PTHR32370; 1.
DR Pfam; PF03000; NPH3; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS51649; NPH3; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..607
FT /note="BTB/POZ domain-containing protein DOT3"
FT /id="PRO_0000409562"
FT DOMAIN 52..121
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 211..487
FT /note="NPH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00982"
FT REGION 498..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 511..563
FT /evidence="ECO:0000255"
FT COMPBIAS 573..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 428
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9FMF5"
SQ SEQUENCE 607 AA; 69973 MW; E5B70AF834C684DD CRC64;
MNSVSAAERL KSFGDAGPVC NKSIIFPSRV VTLANSFEKK DRSWYVKSQI PTDLSIQVND
ITFKAHKFPL ISKCGYISSI ELKPSTSENG YHLKLENFPG GADTFETILK FCYNLPLDLN
PLNVAPLRCA SEYLYMTEEF EAGNLISKTE AFITFVVLAS WRDTLTVLRS CTNLSPWAEN
LQIVRRCCDL LAWKACNDNN IPEDVVDRNE RCLYNDIATL DIDHFMRVIT TMKARRAKPQ
ITGKIIMKYA DNFLPVINDD LEGIKGYGLG KNELQFSVNR GRMEESNSLG CQEHKETIES
LVSVLPPQSG AVSCHFLLRM LKTSIVYSAS PALISDLEKR VGMALEDANV CDLLIPNFKN
EEQQERVRIF EFFLMHEQQQ VLGKPSISKL LDNYLAEIAK DPYLPITKFQ VLAEMLPENA
WKCHDGLYRA IDMFLKTHPS LSDHDRRRLC KTMNCEKLSL DACLHAAQND RLPLRTIVQI
NTQVLFSEQV KMRMMMQDKL PEKEEENSGG REDKRMSRDN EIIKTLKEEL ENVKKKMSEL
QSDYNELQQE YERLSSKQKS SHNWGLRWQK VKKSFQTKRE DEETRERTRR RSSTGQRTSF
RRRMSMS
