EYA_ARATH
ID EYA_ARATH Reviewed; 307 AA.
AC O82162; Q8LAU3; Q93W85;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Eyes absent homolog {ECO:0000303|PubMed:15641802};
DE Short=AtEYA {ECO:0000303|PubMed:15641802};
DE EC=3.1.3.48 {ECO:0000269|PubMed:18759246};
GN Name=EYA {ECO:0000303|PubMed:15641802};
GN OrderedLocusNames=At2g35320 {ECO:0000312|Araport:AT2G35320};
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=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 [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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVE SITE, AND MUTAGENESIS OF 1-MET--ASP-15; ASP-25; ASP-27; THR-29;
RP THR-197; GLY-252; ASP-253 AND GLU-257.
RX PubMed=15641802; DOI=10.1021/bi0481794;
RA Rayapureddi J.P., Kattamuri C., Chan F.H., Hegde R.S.;
RT "Characterization of a plant, tyrosine-specific phosphatase of the aspartyl
RT class.";
RL Biochemistry 44:751-758(2005).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18759246; DOI=10.1002/cbic.200800224;
RA Musharraf A., Markschies N., Teichmann K., Pankratz S., Landgraf K.,
RA Englert C., Imhof D.;
RT "Eyes absent proteins: characterization of substrate specificity and
RT phosphatase activity of mutants associated with branchial, otic and renal
RT anomalies.";
RL ChemBioChem 9:2285-2294(2008).
CC -!- FUNCTION: Possesses phosphatase activity toward para-nitrophenyl
CC phosphate (pNPP) in vitro (PubMed:15641802). Possesses phosphatase
CC activity toward several phosphotyrosine-containing peptides in vitro,
CC with low peptide substrate specificity (PubMed:18759246).
CC {ECO:0000269|PubMed:15641802, ECO:0000269|PubMed:18759246}.
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;
CC Evidence={ECO:0000269|PubMed:18759246};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15641802};
CC Note=Possesses phosphatase activity in presence of Mn(2+), Co(2+),
CC Ni(2+) or Zn(2+). No phosphatase activity in presence Ca(2+).
CC {ECO:0000269|PubMed:15641802};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:15641802}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.73 mM for para-nitrophenyl phosphate (at pH 5.5);
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:15641802};
CC -!- INTERACTION:
CC O82162; Q9SJM4: GPL3; NbExp=3; IntAct=EBI-25523010, EBI-15199331;
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. EYA family.
CC {ECO:0000305}.
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DR EMBL; AC004667; AAC61806.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09093.1; -; Genomic_DNA.
DR EMBL; AF410332; AAK95318.1; -; mRNA.
DR EMBL; AY054555; AAK96746.1; -; mRNA.
DR EMBL; AY064618; AAL47332.1; -; mRNA.
DR EMBL; AY149930; AAN31084.1; -; mRNA.
DR EMBL; AY087608; AAM65149.1; -; mRNA.
DR PIR; B84767; B84767.
DR RefSeq; NP_565803.1; NM_129084.3.
DR AlphaFoldDB; O82162; -.
DR SMR; O82162; -.
DR IntAct; O82162; 1.
DR STRING; 3702.AT2G35320.1; -.
DR PaxDb; O82162; -.
DR PRIDE; O82162; -.
DR ProteomicsDB; 221821; -.
DR EnsemblPlants; AT2G35320.1; AT2G35320.1; AT2G35320.
DR GeneID; 818099; -.
DR Gramene; AT2G35320.1; AT2G35320.1; AT2G35320.
DR KEGG; ath:AT2G35320; -.
DR Araport; AT2G35320; -.
DR TAIR; locus:2063414; AT2G35320.
DR eggNOG; KOG3107; Eukaryota.
DR HOGENOM; CLU_051936_0_0_1; -.
DR InParanoid; O82162; -.
DR OMA; NVQFCVI; -.
DR OrthoDB; 1030296at2759; -.
DR PhylomeDB; O82162; -.
DR PRO; PR:O82162; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82162; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0030946; F:protein tyrosine phosphatase activity, metal-dependent; IDA:UniProtKB.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045739; P:positive regulation of DNA repair; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; TAS:TAIR.
DR Gene3D; 3.40.50.12350; -; 1.
DR InterPro; IPR006545; EYA_dom.
DR InterPro; IPR038102; EYA_dom_sf.
DR InterPro; IPR028472; EYA_fam.
DR InterPro; IPR036412; HAD-like_sf.
DR PANTHER; PTHR10190; PTHR10190; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01658; EYA-cons_domain; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..307
FT /note="Eyes absent homolog"
FT /id="PRO_0000443993"
FT REGION 1..15
FT /note="Necessary for optimum phosphatase activity"
FT /evidence="ECO:0000269|PubMed:15641802"
FT ACT_SITE 25
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:15641802"
FT ACT_SITE 27
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:15641802"
FT BINDING 25
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:15641802"
FT BINDING 27
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:15641802"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:15641802"
FT MUTAGEN 1..15
FT /note="Missing: Reduces phosphatase activity 2-fold."
FT /evidence="ECO:0000269|PubMed:15641802"
FT MUTAGEN 25
FT /note="D->C,E,N: Abolishes phosphatase activity."
FT /evidence="ECO:0000269|PubMed:15641802"
FT MUTAGEN 27
FT /note="D->A,N: Reduces phosphatase activity 30-fold."
FT /evidence="ECO:0000269|PubMed:15641802"
FT MUTAGEN 29
FT /note="T->A: Reduces phosphatase activity 45-fold."
FT /evidence="ECO:0000269|PubMed:15641802"
FT MUTAGEN 197
FT /note="T->A: Reduces phosphatase activity 55-fold."
FT /evidence="ECO:0000269|PubMed:15641802"
FT MUTAGEN 252
FT /note="G->A: Reduces phosphatase activity 30-fold."
FT /evidence="ECO:0000269|PubMed:15641802"
FT MUTAGEN 253
FT /note="D->N: Reduces phosphatase activity 25-fold."
FT /evidence="ECO:0000269|PubMed:15641802"
FT MUTAGEN 257
FT /note="E->Q: Reduces phosphatase activity 45-fold."
FT /evidence="ECO:0000269|PubMed:15641802"
FT CONFLICT 87
FT /note="D -> E (in Ref. 4; AAM65149)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="P -> Q (in Ref. 4; AAM65149)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 35258 MW; 44BF0B612D473668 CRC64;
MNNDTSKKLG TLVSDDGPVN VYVWDMDETL ILLRSLLNGT YAESFNGSKD VKRGVEIGRM
WEKHILKICD DFFFYEQVEE CNEPFLDSLR QYDDGKDLSR YEFKQDDFST PTDDLNKRKL
AYRHRAVAER YEKGLCPFID SESMSGLDEL YNVTDEYTDR WLSSARAFLE QCSCVEESSD
GTSAIEQSSQ DIHILVTSGA LIPSLVKCLL FRLDTFLRHE NVYSSIDVGK LQCFKWIKER
FNHPKFRFCA IGDGWEECAA AQALQWPFVK IDLQPDSSHR FPGLTPKTVS YYFAAVYGNS
DADSSKE
