AIRP1_ARATH
ID AIRP1_ARATH Reviewed; 153 AA.
AC Q93ZF6; O81741;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 154.
DE RecName: Full=E3 ubiquitin-protein ligase AIRP1 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:15644464, ECO:0000269|PubMed:20884812};
DE AltName: Full=Protein ABA INSENSITIVE RING PROTEIN 1 {ECO:0000303|PubMed:20884812};
DE Short=AtAIRP1 {ECO:0000303|PubMed:20884812};
DE AltName: Full=RING-type E3 ubiquitin transferase AIRP1 {ECO:0000305};
GN Name=AIRP1 {ECO:0000303|PubMed:20884812};
GN OrderedLocusNames=At4g23450 {ECO:0000312|Araport:AT4G23450};
GN ORFNames=F16G20.150 {ECO:0000312|EMBL:CAA20466.1};
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], FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND
RP MUTAGENESIS OF CYS-122; HIS-124 AND HIS-127.
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter 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.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort 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., Sekhon 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.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., 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., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
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 [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].
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, INDUCTION, DOMAIN,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-127.
RX PubMed=20884812; DOI=10.1104/pp.110.164749;
RA Ryu M.Y., Cho S.K., Kim W.T.;
RT "The Arabidopsis C3H2C3-type RING E3 ubiquitin ligase AtAIRP1 is a positive
RT regulator of an abscisic acid-dependent response to drought stress.";
RL Plant Physiol. 154:1983-1997(2010).
CC -!- FUNCTION: Possesses E3 ubiquitin-protein ligase activity in vitro when
CC associated with the E2 enzyme UBC8 in vitro (PubMed:20884812,
CC PubMed:15644464). Plays combinatory roles with AIRP2 in the positive
CC regulation of the abscisic acid-mediated drought stress response
CC (PubMed:20884812). {ECO:0000269|PubMed:15644464,
CC ECO:0000269|PubMed:20884812}.
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 ECO:0000269|PubMed:20884812};
CC -!- INTERACTION:
CC Q93ZF6; Q9SVD7: UEV1D; NbExp=3; IntAct=EBI-4465263, EBI-3386882;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20884812}.
CC -!- INDUCTION: Induced by salt stress, cold stress, drought stress and
CC abscisic acid (ABA). {ECO:0000269|PubMed:20884812}.
CC -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000305|PubMed:15644464, ECO:0000305|PubMed:20884812}.
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:20884812}.
CC -!- MISCELLANEOUS: Plants over-expressing AIRP1 exhibit tolerance to severe
CC drought stress. {ECO:0000269|PubMed:20884812}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA20466.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79300.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ059123; AAY57609.1; -; mRNA.
DR EMBL; AL031326; CAA20466.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161559; CAB79300.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84758.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM68051.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM68052.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM68053.1; -; Genomic_DNA.
DR EMBL; AY057571; AAL09810.1; -; mRNA.
DR EMBL; AY093984; AAM16245.1; -; mRNA.
DR PIR; T05383; T05383.
DR RefSeq; NP_001329832.1; NM_001341615.1.
DR RefSeq; NP_001329833.1; NM_001341616.1.
DR RefSeq; NP_001329834.1; NM_001341614.1.
DR RefSeq; NP_567682.1; NM_118474.4.
DR AlphaFoldDB; Q93ZF6; -.
DR SMR; Q93ZF6; -.
DR IntAct; Q93ZF6; 2.
DR STRING; 3702.AT4G23450.3; -.
DR ProteomicsDB; 244671; -.
DR EnsemblPlants; AT4G23450.1; AT4G23450.1; AT4G23450.
DR EnsemblPlants; AT4G23450.4; AT4G23450.4; AT4G23450.
DR EnsemblPlants; AT4G23450.5; AT4G23450.5; AT4G23450.
DR EnsemblPlants; AT4G23450.6; AT4G23450.6; AT4G23450.
DR GeneID; 828444; -.
DR Gramene; AT4G23450.1; AT4G23450.1; AT4G23450.
DR Gramene; AT4G23450.4; AT4G23450.4; AT4G23450.
DR Gramene; AT4G23450.5; AT4G23450.5; AT4G23450.
DR Gramene; AT4G23450.6; AT4G23450.6; AT4G23450.
DR KEGG; ath:AT4G23450; -.
DR Araport; AT4G23450; -.
DR PhylomeDB; Q93ZF6; -.
DR BRENDA; 2.3.2.27; 399.
DR PRO; PR:Q93ZF6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q93ZF6; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0010729; P:positive regulation of hydrogen peroxide biosynthetic process; IMP:UniProtKB.
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 Cytoplasm; Metal-binding; Reference proteome; Stress response; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..153
FT /note="E3 ubiquitin-protein ligase AIRP1"
FT /id="PRO_0000443383"
FT ZN_FING 104..145
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MUTAGEN 122
FT /note="C->A: Strongly reduces E3 ubiquitin-protein ligase
FT activity; when associated with A-124 and A-127."
FT /evidence="ECO:0000269|PubMed:15644464"
FT MUTAGEN 124
FT /note="H->A: Strongly reduces E3 ubiquitin-protein ligase
FT activity; when associated with A-122 and A-127."
FT /evidence="ECO:0000269|PubMed:15644464"
FT MUTAGEN 127
FT /note="H->A: Strongly reduces E3 ubiquitin-protein ligase
FT activity; when associated with A-122 and A-124."
FT /evidence="ECO:0000269|PubMed:15644464"
FT MUTAGEN 127
FT /note="H->Y: Strongly reduces E3 ubiquitin-protein ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:20884812"
SQ SEQUENCE 153 AA; 16940 MW; CDB0EF84CEFC2049 CRC64;
MGCCCCLPSI PESSRTIDEH LPLSRATPSS LSNAYSSPLS PPIPLAITNI NLQTSPPKLP
RTQGNSSEAS PGLTQVVPEK KTWHVDDLTD FELKKQYREA IDECPICLEE YEIDNPKLLT
KCGHDFHLAC ILAWMERSEA CPVCDKELVL TES
