IBR5_ARATH
ID IBR5_ARATH Reviewed; 257 AA.
AC Q84JU4; Q3EC68; Q9SJB6;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Protein-tyrosine-phosphatase IBR5;
DE EC=3.1.3.48;
DE AltName: Full=Protein INDOLE-3-BUTYRIC ACID RESPONSE 5;
DE Short=Protein IBA RESPONSE 5;
DE AltName: Full=SKP1-interacting partner 33;
GN Name=IBR5; Synonyms=SKIP33; OrderedLocusNames=At2g04550; ORFNames=T1O3.4;
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), FUNCTION, DISRUPTION PHENOTYPE,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14630970; DOI=10.1105/tpc.017046;
RA Monroe-Augustus M., Zolman B.K., Bartel B.;
RT "IBR5, a dual-specificity phosphatase-like protein modulating auxin and
RT abscisic acid responsiveness in Arabidopsis.";
RL Plant Cell 15:2979-2991(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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] (ISOFORM 1).
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 INTERACTION WITH SKP1A/ASK1.
RX PubMed=12795696; DOI=10.1046/j.1365-313x.2003.01768.x;
RA Risseeuw E.P., Daskalchuk T.E., Banks T.W., Liu E., Cotelesage J.,
RA Hellmann H., Estelle M., Somers D.E., Crosby W.L.;
RT "Protein interaction analysis of SCF ubiquitin E3 ligase subunits from
RT Arabidopsis.";
RL Plant J. 34:753-767(2003).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18423007; DOI=10.1186/1471-2229-8-41;
RA Strader L.C., Monroe-Augustus M., Bartel B.;
RT "The IBR5 phosphatase promotes Arabidopsis auxin responses through a novel
RT mechanism distinct from TIR1-mediated repressor degradation.";
RL BMC Plant Biol. 8:41-41(2008).
RN [7]
RP FUNCTION.
RX PubMed=18832358; DOI=10.1534/genetics.108.091512;
RA Strader L.C., Monroe-Augustus M., Rogers K.C., Lin G.L., Bartel B.;
RT "Arabidopsis iba response5 suppressors separate responses to various
RT hormones.";
RL Genetics 180:2019-2031(2008).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MPK12.
RX PubMed=19000167; DOI=10.1111/j.1365-313x.2008.03741.x;
RA Lee J.S., Wang S., Sritubtim S., Chen J.-G., Ellis B.E.;
RT "Arabidopsis mitogen-activated protein kinase MPK12 interacts with the MAPK
RT phosphatase IBR5 and regulates auxin signaling.";
RL Plant J. 57:975-985(2009).
RN [9]
RP INTERACTION WITH MPK12.
RC STRAIN=cv. Columbia, and cv. Cvi-0;
RX PubMed=27923039; DOI=10.1371/journal.pbio.2000322;
RA Jakobson L., Vaahtera L., Toldsepp K., Nuhkat M., Wang C., Wang Y.S.,
RA Horak H., Valk E., Pechter P., Sindarovska Y., Tang J., Xiao C., Xu Y.,
RA Gerst Talas U., Garcia-Sosa A.T., Kangasjaervi S., Maran U., Remm M.,
RA Roelfsema M.R., Hu H., Kangasjaervi J., Loog M., Schroeder J.I.,
RA Kollist H., Brosche M.;
RT "Natural variation in Arabidopsis Cvi-0 accession reveals an important role
RT of MPK12 in guard cell CO2 signaling.";
RL PLoS Biol. 14:E2000322-E2000322(2016).
CC -!- FUNCTION: Required for the transduction of auxin and abscisic acid
CC (ABA) signaling pathways. Dephosphorylates and inactivates the MAP
CC kinase MPK12. {ECO:0000269|PubMed:14630970,
CC ECO:0000269|PubMed:18423007, ECO:0000269|PubMed:18832358,
CC ECO:0000269|PubMed:19000167}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBUNIT: Interacts with SKP1A/ASK1 and with MPK12.
CC {ECO:0000269|PubMed:12795696, ECO:0000269|PubMed:19000167,
CC ECO:0000269|PubMed:27923039}.
CC -!- INTERACTION:
CC Q84JU4; Q9LNT9: ASK4; NbExp=3; IntAct=EBI-604555, EBI-604085;
CC Q84JU4; Q9LTB8: CBL9; NbExp=4; IntAct=EBI-604555, EBI-637381;
CC Q84JU4; Q9ZR37: DSPTP1; NbExp=3; IntAct=EBI-604555, EBI-25512239;
CC Q84JU4; Q9LXT3: MBF1B; NbExp=3; IntAct=EBI-604555, EBI-15217346;
CC Q84JU4; Q8GYQ5: MPK12; NbExp=8; IntAct=EBI-604555, EBI-2128461;
CC Q84JU4; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-604555, EBI-15192297;
CC Q84JU4; Q93WV6: WRKY68; NbExp=3; IntAct=EBI-604555, EBI-25512440;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19000167}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q84JU4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q84JU4-2; Sequence=VSP_037361;
CC -!- TISSUE SPECIFICITY: Expressed in root tips and vasculature, cotyledons,
CC stems, leaves vasculature and hydathodes, flowers, siliques, and seeds.
CC {ECO:0000269|PubMed:14630970}.
CC -!- DEVELOPMENTAL STAGE: During flower development, detected in sepals,
CC anther filaments, and carpels. During germination, levels decline
CC slightly two days after imbibition. {ECO:0000269|PubMed:14630970}.
CC -!- DISRUPTION PHENOTYPE: Impaired responses to phytohormones such as
CC indole-3-butyric acid, indole-3-acetic acid (auxin), synthetic auxins,
CC auxin transport inhibitors, and abscisic acid (ABA). Plants exhibit
CC long roots and short hypocotyls when grown in the light, with aberrant
CC vascular patterning, increased leaf serration, and reduced accumulation
CC of auxin-inducible genes. {ECO:0000269|PubMed:14630970,
CC ECO:0000269|PubMed:18423007}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25825.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BT004283; AAO42283.1; -; mRNA.
DR EMBL; AC006951; AAD25825.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC05845.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05846.1; -; Genomic_DNA.
DR EMBL; BT005609; AAO64029.1; -; mRNA.
DR EMBL; AY337455; AAR04550.1; -; mRNA.
DR PIR; G84458; G84458.
DR RefSeq; NP_178534.2; NM_126486.6. [Q84JU4-1]
DR RefSeq; NP_973418.2; NM_201689.3. [Q84JU4-2]
DR AlphaFoldDB; Q84JU4; -.
DR SMR; Q84JU4; -.
DR BioGRID; 398; 10.
DR IntAct; Q84JU4; 10.
DR STRING; 3702.AT2G04550.1; -.
DR PaxDb; Q84JU4; -.
DR PRIDE; Q84JU4; -.
DR ProteomicsDB; 248567; -. [Q84JU4-1]
DR EnsemblPlants; AT2G04550.1; AT2G04550.1; AT2G04550. [Q84JU4-1]
DR EnsemblPlants; AT2G04550.3; AT2G04550.3; AT2G04550. [Q84JU4-2]
DR GeneID; 814997; -.
DR Gramene; AT2G04550.1; AT2G04550.1; AT2G04550. [Q84JU4-1]
DR Gramene; AT2G04550.3; AT2G04550.3; AT2G04550. [Q84JU4-2]
DR KEGG; ath:AT2G04550; -.
DR Araport; AT2G04550; -.
DR TAIR; locus:2058344; AT2G04550.
DR eggNOG; KOG1716; Eukaryota.
DR HOGENOM; CLU_053611_0_0_1; -.
DR InParanoid; Q84JU4; -.
DR OMA; YCMSGRS; -.
DR PhylomeDB; Q84JU4; -.
DR PRO; PR:Q84JU4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q84JU4; baseline and differential.
DR Genevisible; Q84JU4; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0033549; F:MAP kinase phosphatase activity; IDA:TAIR.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IC:TAIR.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:TAIR.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0046620; P:regulation of organ growth; IMP:TAIR.
DR GO; GO:0061388; P:regulation of rate of cell growth; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR044212; IBR5-like.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR47244; PTHR47244; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing;
KW Auxin signaling pathway; Hydrolase; Nucleus; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..257
FT /note="Protein-tyrosine-phosphatase IBR5"
FT /id="PRO_0000375243"
FT DOMAIN 49..185
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 235..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 129
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT VAR_SEQ 171..257
FT /note="EFYQQLQEFEQGIFGSEMMSAMNINDAPTFGFGFPKIDNQAQAPVFNNAPTS
FT SIFSSPASSIPPQEFTFGATPPKPTTGGDIAMDGS -> VLPTTAGV (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037361"
SQ SEQUENCE 257 AA; 28690 MW; 68CFA8A26DC933DF CRC64;
MRKRERENPC SICGHYHKYE EGEVCGVCGH CMPVSSDTVA PQQVHVSAFP SEILPEFLYL
GSYDNASRSE LLKTQGISRV LNTVPMCQNL YRNSFTYHGL DNEKVLQFDD AIKFLDQCEK
DKARVLVHCM SGKSRSPAVV VAYLMKRKGW RLAESHQWVK QRRPSTDISP EFYQQLQEFE
QGIFGSEMMS AMNINDAPTF GFGFPKIDNQ AQAPVFNNAP TSSIFSSPAS SIPPQEFTFG
ATPPKPTTGG DIAMDGS
