AIRP2_ARATH
ID AIRP2_ARATH Reviewed; 242 AA.
AC Q9M022; Q93WE1;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=E3 ubiquitin-protein ligase AIRP2 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:21969385};
DE AltName: Full=Protein ABA INSENSITIVE RING PROTEIN 2 {ECO:0000303|PubMed:21969385};
DE Short=AtAIRP2 {ECO:0000303|PubMed:21969385};
DE AltName: Full=RING-type E3 ubiquitin transferase AIRP2 {ECO:0000305};
GN Name=AIRP2 {ECO:0000303|PubMed:21969385};
GN OrderedLocusNames=At5g01520 {ECO:0000312|Araport:AT5G01520};
GN ORFNames=F7A7_40 {ECO:0000312|EMBL:CAB82268.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [2]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INDUCTION, DOMAIN, MUTAGENESIS OF HIS-163, AND DISRUPTION PHENOTYPE.
RX PubMed=21969385; DOI=10.1104/pp.111.185595;
RA Cho S.K., Ryu M.Y., Seo D.H., Kang B.G., Kim W.T.;
RT "The Arabidopsis RING E3 ubiquitin ligase AtAIRP2 plays combinatory roles
RT with AtAIRP1 in abscisic acid-mediated drought stress responses.";
RL Plant Physiol. 157:2240-2257(2011).
RN [6]
RP FUNCTION, AND INTERACTION WITH ATP1/SDIRIP1.
RX PubMed=28626006; DOI=10.1104/pp.17.00467;
RA Oh T.R., Kim J.H., Cho S.K., Ryu M.Y., Yang S.W., Kim W.T.;
RT "AtAIRP2 E3 ligase affects ABA and high-salinity responses by stimulating
RT its ATP1/SDIRIP1 substrate turnover.";
RL Plant Physiol. 174:2515-2531(2017).
CC -!- FUNCTION: Possesses E3 ubiquitin-protein ligase activity in vitro when
CC associated with the E2 enzyme UBC8 in vitro (PubMed:21969385,
CC PubMed:28626006). Plays combinatory roles with AIRP1 in the positive
CC regulation of the abscisic acid-mediated drought stress response
CC (PubMed:21969385). Plays a positive role in abscisic acid- and high
CC salinity-regulated seed germination through the ubiquitin-proteasome-
CC dependent down-regulation of ATP1/SDIRIP1 (PubMed:28626006).
CC {ECO:0000269|PubMed:21969385, ECO:0000269|PubMed:28626006}.
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:21969385};
CC -!- SUBUNIT: Interacts with ATP1/SDIRIP1. {ECO:0000269|PubMed:28626006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21969385}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9M022-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M022-2; Sequence=VSP_059339;
CC -!- TISSUE SPECIFICITY: Expressed in germinating seeds, flower organs and
CC siliques. {ECO:0000269|PubMed:21969385}.
CC -!- INDUCTION: Induced by salt stress, cold stress, drought stress and
CC abscisic acid (ABA). {ECO:0000269|PubMed:21969385}.
CC -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000305|PubMed:21969385}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant seeds are insensitive to germination inhibition
CC by abscisic acid (ABA). {ECO:0000269|PubMed:21969385}.
CC -!- MISCELLANEOUS: Plants over-expressing AIRP2 exhibit tolerance to severe
CC drought stress. {ECO:0000269|PubMed:21969385}.
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DR EMBL; DQ059129; AAY57615.1; -; mRNA.
DR EMBL; AL161946; CAB82268.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90355.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90356.1; -; Genomic_DNA.
DR EMBL; AF370144; AAK43959.1; -; mRNA.
DR EMBL; AY050835; AAK92770.1; -; mRNA.
DR EMBL; AY056355; AAL07241.1; -; mRNA.
DR EMBL; AY091165; AAM14104.1; -; mRNA.
DR PIR; T48173; T48173.
DR RefSeq; NP_195772.1; NM_120230.2. [Q9M022-1]
DR RefSeq; NP_974721.1; NM_202992.1. [Q9M022-2]
DR AlphaFoldDB; Q9M022; -.
DR SMR; Q9M022; -.
DR STRING; 3702.AT5G01520.1; -.
DR PaxDb; Q9M022; -.
DR PRIDE; Q9M022; -.
DR ProteomicsDB; 244870; -. [Q9M022-1]
DR EnsemblPlants; AT5G01520.1; AT5G01520.1; AT5G01520. [Q9M022-1]
DR EnsemblPlants; AT5G01520.2; AT5G01520.2; AT5G01520. [Q9M022-2]
DR GeneID; 831747; -.
DR Gramene; AT5G01520.1; AT5G01520.1; AT5G01520. [Q9M022-1]
DR Gramene; AT5G01520.2; AT5G01520.2; AT5G01520. [Q9M022-2]
DR KEGG; ath:AT5G01520; -.
DR Araport; AT5G01520; -.
DR TAIR; locus:2149750; AT5G01520.
DR eggNOG; KOG1039; Eukaryota.
DR HOGENOM; CLU_059830_3_0_1; -.
DR InParanoid; Q9M022; -.
DR OMA; MYIHERK; -.
DR PhylomeDB; Q9M022; -.
DR PRO; PR:Q9M022; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9M022; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:TAIR.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Metal-binding; Reference proteome;
KW Stress response; Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..242
FT /note="E3 ubiquitin-protein ligase AIRP2"
FT /id="PRO_0000443384"
FT ZN_FING 146..184
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT VAR_SEQ 173..242
FT /note="Missing (in isoform 2)"
FT /id="VSP_059339"
FT MUTAGEN 163
FT /note="H->A: Abolishes E3 ubiquitin-protein ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:21969385"
SQ SEQUENCE 242 AA; 28049 MW; 417C8C244A36C981 CRC64;
MRKSFKDSLK ALEADIQFAN TLASEYPEEY DGGYVQMRLS YSPAAHLFLF LLQWTDCHFA
GALGLLRILI YKAYVDGKTT MSLHERKTSI REFYDVLFPS LLQLHGGITD VEERKQKEIC
DKRYRKKDRT DKGKMSEIDL EREEECGICL EIRNKVVLPT CNHSMCINCY RNWRARSQSC
PFCRGSLKRV NSGDLWIYTC SAEIADLPAI YKENLKRLLI YIDKLPLVTS DPNLVPYAPL
PR
