ID A0A087WRG6_MOUSE Unreviewed; 118 AA. AC A0A087WRG6; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 24-JAN-2024, entry version 49. DE RecName: Full=Eyes absent homolog {ECO:0000256|RuleBase:RU362036}; DE EC=3.1.3.48 {ECO:0000256|RuleBase:RU362036}; DE Flags: Fragment; GN Name=Eya1 {ECO:0000313|Ensembl:ENSMUSP00000140619.2, GN ECO:0000313|MGI:MGI:109344}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000140619.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000140619.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000140619.2, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0000313|Ensembl:ENSMUSP00000140619.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000140619.2}; RG Ensembl; RL Submitted (JUL-2023) to UniProtKB. 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:0000256|RuleBase:RU362036}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR628472-2, CC ECO:0000256|RuleBase:RU362036}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR628472-2, CC ECO:0000256|RuleBase:RU362036}; CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. EYA family. CC {ECO:0000256|ARBA:ARBA00010501, ECO:0000256|RuleBase:RU362036}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR ProteomicsDB; 373294; -. DR Antibodypedia; 25098; 255 antibodies from 31 providers. DR Ensembl; ENSMUST00000189526.2; ENSMUSP00000140619.2; ENSMUSG00000025932.15. DR AGR; MGI:109344; -. DR MGI; MGI:109344; Eya1. DR VEuPathDB; HostDB:ENSMUSG00000025932; -. DR GeneTree; ENSGT00950000182978; -. DR HOGENOM; CLU_2090298_0_0_1; -. DR ChiTaRS; Eya1; mouse. DR Proteomes; UP000000589; Chromosome 1. DR Bgee; ENSMUSG00000025932; Expressed in epithelium of cochlear duct and 246 other cell types or tissues. DR ExpressionAtlas; A0A087WRG6; baseline and differential. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.12350; -; 1. DR InterPro; IPR038102; EYA_dom_sf. DR InterPro; IPR028472; EYA_fam. DR PANTHER; PTHR10190; EYES ABSENT; 1. DR PANTHER; PTHR10190:SF11; EYES ABSENT HOMOLOG 1; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362036}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR628472-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR628472-2, KW ECO:0000256|RuleBase:RU362036}; KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912, KW ECO:0000256|RuleBase:RU362036}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Transcription {ECO:0000256|RuleBase:RU362036}; KW Transcription regulation {ECO:0000256|RuleBase:RU362036}. FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 33 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR628472-1" FT ACT_SITE 35 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR628472-1" FT BINDING 33 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR628472-2" FT BINDING 35 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR628472-2" FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSMUSP00000140619.2" SQ SEQUENCE 118 AA; 13388 MW; 785E0E60C6942BAD CRC64; XRGSDGKSRG RGRRNNNPSP PPDSDLERVF IWDLDETIIV FHSLLTGSYA NRYGRDPPTS VSLGLRMEEM IFNLADTHLF FNDLEQNAPY LMEEPKSLGK SQRATELKCG LFNICPVF //