AIP2_ARATH
ID AIP2_ARATH Reviewed; 310 AA.
AC Q8RXD3; Q9M4B6;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=E3 ubiquitin-protein ligase AIP2;
DE EC=2.3.2.27 {ECO:0000269|PubMed:15644464};
DE AltName: Full=ABI3-interacting protein 2;
DE AltName: Full=RING-type E3 ubiquitin transferase AIP2 {ECO:0000305};
GN Name=AIP2; OrderedLocusNames=At5g20910; ORFNames=F22D1.80;
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 [MRNA], INTERACTION WITH ABI3, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta; TISSUE=Silique;
RX PubMed=10743655; DOI=10.1046/j.1365-313x.2000.00663.x;
RA Kurup S., Jones H.D., Holdsworth M.J.;
RT "Interactions of the developmental regulator ABI3 with proteins identified
RT from developing Arabidopsis seeds.";
RL Plant J. 21:143-155(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=15644464; DOI=10.1104/pp.104.052423;
RA Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J.;
RT "Functional analysis of the RING-type ubiquitin ligase family of
RT Arabidopsis.";
RL Plant Physiol. 137:13-30(2005).
RN [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION, INTERACTION WITH ABI3, SUBCELLULAR LOCATION, AUTOUBIQUITINATION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-230 AND CYS-231.
RX PubMed=15998807; DOI=10.1101/gad.1318705;
RA Zhang X., Garreton V., Chua N.H.;
RT "The AIP2 E3 ligase acts as a novel negative regulator of ABA signaling by
RT promoting ABI3 degradation.";
RL Genes Dev. 19:1532-1543(2005).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that acts as a negative regulator
CC of abscisic acid (ABA) signaling. Mediates ubiquitination and
CC subsequent proteasomal degradation of the transcription factor ABI3.
CC {ECO:0000269|PubMed:15644464, ECO:0000269|PubMed:15998807}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:15644464};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with ABI3 (via C-terminus).
CC {ECO:0000269|PubMed:10743655, ECO:0000269|PubMed:15998807}.
CC -!- INTERACTION:
CC Q8RXD3; Q01593: ABI3; NbExp=3; IntAct=EBI-2312425, EBI-1578892;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15998807}. Cytoplasm
CC {ECO:0000269|PubMed:15998807}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves and at lower levels in
CC flowers and seeds. {ECO:0000269|PubMed:10743655}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:15998807}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to abscisic acid (ABA).
CC {ECO:0000269|PubMed:15998807}.
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DR EMBL; AJ251087; CAB75509.1; -; mRNA.
DR EMBL; DQ059130; AAY57616.1; -; mRNA.
DR EMBL; AF296834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92903.1; -; Genomic_DNA.
DR EMBL; AY081329; AAL91218.1; -; mRNA.
DR EMBL; BT000238; AAN15557.1; -; mRNA.
DR RefSeq; NP_197591.1; NM_122099.4.
DR AlphaFoldDB; Q8RXD3; -.
DR SMR; Q8RXD3; -.
DR BioGRID; 17490; 1.
DR IntAct; Q8RXD3; 1.
DR STRING; 3702.AT5G20910.1; -.
DR PaxDb; Q8RXD3; -.
DR PRIDE; Q8RXD3; -.
DR ProteomicsDB; 244784; -.
DR EnsemblPlants; AT5G20910.1; AT5G20910.1; AT5G20910.
DR GeneID; 832215; -.
DR Gramene; AT5G20910.1; AT5G20910.1; AT5G20910.
DR KEGG; ath:AT5G20910; -.
DR Araport; AT5G20910; -.
DR TAIR; locus:2147152; AT5G20910.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_048503_0_0_1; -.
DR InParanoid; Q8RXD3; -.
DR OMA; YSVICRV; -.
DR OrthoDB; 1249953at2759; -.
DR PhylomeDB; Q8RXD3; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8RXD3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8RXD3; baseline and differential.
DR Genevisible; Q8RXD3; AT.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Coiled coil; Cytoplasm; Metal-binding;
KW Nucleus; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..310
FT /note="E3 ubiquitin-protein ligase AIP2"
FT /id="PRO_0000395844"
FT ZN_FING 230..271
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 285..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 276..306
FT /evidence="ECO:0000255"
FT COMPBIAS 285..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 230
FT /note="C->S: Loss of E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:15998807"
FT MUTAGEN 231
FT /note="C->S: Loss of E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:15998807"
FT CONFLICT 277
FT /note="D -> A (in Ref. 1; CAB75509)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 310 AA; 34807 MW; 47D3C96AF08D034E CRC64;
MDASSSPSPS EESLKLELDD LQKQLNKKLR FEASVCSIHN LLRDHYSSSS PSLRKQFYIV
VSRVATVLKT RYTATGFWVA GLSLFEEAER LVSDASEKKH LKSCVAQAKE QLSEVDNQPT
ESSQGYLFEG HLTVDREPPQ PQWLVQQNLM SAFASIVGGE SSNGPTENTI GETANLMQEL
INGLDMIIPD ILDDGGPPRA PPASKEVVEK LPVIIFTEEL LKKFGAEAEC CICKENLVIG
DKMQELPCKH TFHPPCLKPW LDEHNSCPIC RHELPTDDQK YENWKEREKE AEEERKGAEN
AVRGGEYMYV
