ARIA_ARATH
ID ARIA_ARATH Reviewed; 710 AA.
AC B9DHT4; Q56ZQ9;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=ARM REPEAT PROTEIN INTERACTING WITH ABF2;
DE Short=ARIA;
GN Name=ARIA; OrderedLocusNames=At5g19330; ORFNames=F7K24.80;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-710.
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 596-710.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, INTERACTION WITH ABF2, DISRUPTION PHENOTYPE, INDUCTION, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15516505; DOI=10.1104/pp.104.049189;
RA Kim S., Choi H.I., Ryu H.J., Park J.H., Kim M.D., Kim S.Y.;
RT "ARIA, an Arabidopsis arm repeat protein interacting with a transcriptional
RT regulator of abscisic acid-responsive gene expression, is a novel abscisic
RT acid signaling component.";
RL Plant Physiol. 136:3639-3648(2004).
RN [7]
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 [8]
RP INTERACTION WITH DUF7/AIP1.
RX PubMed=26538092; DOI=10.1186/s12870-015-0641-z;
RA Brasil J.N., Cabral L.M., Eloy N.B., Primo L.M., Barroso-Neto I.L.,
RA Grangeiro L.P., Gonzalez N., Inze D., Ferreira P.C., Hemerly A.S.;
RT "AIP1 is a novel Agenet/Tudor domain protein from Arabidopsis that
RT interacts with regulators of DNA replication, transcription and chromatin
RT remodeling.";
RL BMC Plant Biol. 15:270-270(2015).
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). Acts as a positive regulator of ABA response
CC via the modulation of the transcriptional activity of ABF2, a
CC transcription factor which controls ABA-dependent gene expression via
CC the G-box-type ABA-responsive elements. Negative regulator of seed
CC germination and young seedling growth. {ECO:0000250,
CC ECO:0000269|PubMed:15516505}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with ABF2 (PubMed:15516505). Interacts with
CC DUF7/AIP1 (PubMed:26538092). {ECO:0000269|PubMed:15516505,
CC ECO:0000269|PubMed:26538092}.
CC -!- INTERACTION:
CC B9DHT4; Q9C5W9: ARF18; NbExp=3; IntAct=EBI-15192195, EBI-3946783;
CC B9DHT4; F4IEB6: At1g32700; NbExp=3; IntAct=EBI-15192195, EBI-15198265;
CC B9DHT4; C0SV91: At2g46670; NbExp=3; IntAct=EBI-15192195, EBI-15192193;
CC B9DHT4; Q38826: IAA8; NbExp=3; IntAct=EBI-15192195, EBI-632200;
CC B9DHT4; F4IPE3: SGR5; NbExp=3; IntAct=EBI-15192195, EBI-15192881;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15516505}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=B9DHT4-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Detected in embryos and most of the vegetative and
CC reproductive organs. {ECO:0000269|PubMed:15516505}.
CC -!- INDUCTION: Up-regulated by abscisic acid (ABA) and high salt.
CC {ECO:0000269|PubMed:15516505}.
CC -!- DOMAIN: The BTB/POZ domain mediates the interaction with some component
CC of ubiquitin ligase complexes. {ECO:0000269|PubMed:15749712}.
CC -!- DISRUPTION PHENOTYPE: Abscisic acid (ABA) and glucose insensitivities.
CC More efficient germination and postgermination growth.
CC {ECO:0000269|PubMed:15516505}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AY058878; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF296837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92686.1; -; Genomic_DNA.
DR EMBL; AY058878; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK317640; BAH20301.1; -; mRNA.
DR EMBL; AK220904; BAD94337.1; -; mRNA.
DR RefSeq; NP_850852.1; NM_180521.3. [B9DHT4-1]
DR AlphaFoldDB; B9DHT4; -.
DR SMR; B9DHT4; -.
DR BioGRID; 17329; 23.
DR IntAct; B9DHT4; 22.
DR STRING; 3702.AT5G19330.1; -.
DR TCDB; 8.A.160.1.3; the catenin (catenin) family.
DR iPTMnet; B9DHT4; -.
DR PaxDb; B9DHT4; -.
DR PRIDE; B9DHT4; -.
DR ProteomicsDB; 240972; -. [B9DHT4-1]
DR EnsemblPlants; AT5G19330.1; AT5G19330.1; AT5G19330. [B9DHT4-1]
DR GeneID; 832053; -.
DR Gramene; AT5G19330.1; AT5G19330.1; AT5G19330. [B9DHT4-1]
DR KEGG; ath:AT5G19330; -.
DR Araport; AT5G19330; -.
DR TAIR; locus:2150295; AT5G19330.
DR eggNOG; KOG0167; Eukaryota.
DR HOGENOM; CLU_392026_0_0_1; -.
DR InParanoid; B9DHT4; -.
DR OMA; LLYMMRV; -.
DR PhylomeDB; B9DHT4; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:B9DHT4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; B9DHT4; baseline and differential.
DR Genevisible; B9DHT4; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0010187; P:negative regulation of seed germination; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR Gene3D; 1.25.10.10; -; 2.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR044282; ABAP1/ARIA.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR46710; PTHR46710; 1.
DR Pfam; PF00514; Arm; 3.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM00185; ARM; 9.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50176; ARM_REPEAT; 5.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..710
FT /note="ARM REPEAT PROTEIN INTERACTING WITH ABF2"
FT /id="PRO_0000405806"
FT REPEAT 85..127
FT /note="ARM 1"
FT REPEAT 138..185
FT /note="ARM 2"
FT REPEAT 188..227
FT /note="ARM 3"
FT REPEAT 230..269
FT /note="ARM 4"
FT REPEAT 272..311
FT /note="ARM 5"
FT REPEAT 314..353
FT /note="ARM 6"
FT REPEAT 355..394
FT /note="ARM 7"
FT REPEAT 429..468
FT /note="ARM 8"
FT REPEAT 470..509
FT /note="ARM 9"
FT DOMAIN 541..608
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 531
FT /note="G -> E (in Ref. 3; AY058878)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 710 AA; 78186 MW; E331C22DF2BD98CB CRC64;
MDQQPERREG RSFPERKGQK RKLEEGAAAV EDREISAVST DGGQALLSEV AAQVSVLNSA
FSWQESDRAA AKRATQVLAE LAKNEDLVNV IVDGGAVPAL MTHLQAPPYN DGDLAEKPYE
HEVEKGSAFA LGLLAIKPEY QKLIVDKGAL PHLVNLLKRN KDGSSSRAVN SVIRRAADAI
TNLAHENSSI KTRVRVEGGI PPLVELLEFS DSKVQRAAAG ALRTLAFKND DNKNQIVECN
ALPTLILMLG SEDAAIHYEA VGVIGNLVHS SPHIKKEVLT AGALQPVIGL LSSCCPESQR
EAALLLGQFA STDSDCKVHI VQRGAVRPLI EMLQSPDVQL KEMSAFALGR LAQDAHNQAG
IAHSGGLGPL LKLLDSRNGS LQHNAAFALY GLADNEDNVS DFIRVGGIQK LQDGEFIVQA
TKDCVSKTLK RLEEKIHGRV LRHLLYLMRI SEKSIQRRVA LALAHLCSPE DQRTIFIDDN
GLELLLGLLG SLNTKQQLDG AAALYKLANK SMALSPVDAA PPSPTQRVYL GEQYVNNATL
SDVTFLVEGR TFYAHRICLL ASSDAFRAMF DGGYREKDAR DIEIPNIKWE VFELMMRFIY
TGSVDITNEI SKDLLRAADQ YLLEGLKRLC EYTIAQDITL ESIGDMYELS EAFHAMSLRQ
ACIMFILEHF DKLSSMPWQN ELVQRTIPEI REYFCRALTK STTNLQSLRL
