ID A0A8I6AMN9_RAT Unreviewed; 572 AA. AC A0A8I6AMN9; DT 25-MAY-2022, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 1. DT 24-JUL-2024, entry version 13. DE RecName: Full=Eyes absent homolog {ECO:0000256|RuleBase:RU362036}; DE EC=3.1.3.48 {ECO:0000256|RuleBase:RU362036}; GN Name=Eya3 {ECO:0000313|Ensembl:ENSRNOP00000095246.1, GN ECO:0000313|RGD:1309932}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000095246.1, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000095246.1, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000095246.1, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000095246.1} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000095246.1}; RG Ensembl; RL Submitted (APR-2024) 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|ARBA:ARBA00001490, CC 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. 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 RefSeq; XP_006239086.1; XM_006239024.3. DR RefSeq; XP_006239087.1; XM_006239025.3. DR RefSeq; XP_006239088.1; XM_006239026.2. DR PhosphoSitePlus; A0A8I6AMN9; -. DR Ensembl; ENSRNOT00000097388.1; ENSRNOP00000095246.1; ENSRNOG00000010396.8. DR GeneID; 313027; -. DR AGR; RGD:1309932; -. DR CTD; 2140; -. DR RGD; 1309932; Eya3. DR GeneTree; ENSGT00950000182978; -. DR Proteomes; UP000002494; Chromosome 5. DR GO; GO:0005634; C:nucleus; ISO:RGD. DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD. DR GO; GO:0003682; F:chromatin binding; ISO:RGD. DR GO; GO:0140793; F:histone H2AXY142 phosphatase activity; ISO:RGD. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:RGD. DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISO:RGD. DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central. DR GO; GO:0006302; P:double-strand break repair; ISO:RGD. DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central. DR GO; GO:0045739; P:positive regulation of DNA repair; ISO:RGD. DR GO; GO:0010212; P:response to ionizing radiation; ISO:RGD. DR CDD; cd02601; HAD_Eya; 1. DR Gene3D; 3.40.50.12350; -; 1. DR InterPro; IPR006545; EYA_dom. DR InterPro; IPR042577; EYA_dom_metazoan. DR InterPro; IPR038102; EYA_dom_sf. DR InterPro; IPR028472; EYA_fam. DR NCBIfam; TIGR01658; EYA-cons_domain; 1. DR PANTHER; PTHR10190; EYES ABSENT; 1. DR PANTHER; PTHR10190:SF5; EYES ABSENT HOMOLOG 3; 1. DR Pfam; PF00702; Hydrolase; 1. DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1. DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1. PE 1: Evidence at protein level; KW Activator {ECO:0000256|ARBA:ARBA00023159}; 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|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR628472-2}; Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912, KW ECO:0000256|RuleBase:RU362036}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A8I6AMN9}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Transcription {ECO:0000256|ARBA:ARBA00023163}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, KW ECO:0000256|RuleBase:RU362036}. FT REGION 1..47 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 238..295 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..17 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 20..47 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 252..271 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 272..295 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 308 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR628472-1" FT ACT_SITE 310 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR628472-1" FT BINDING 308 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR628472-2" FT BINDING 310 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR628472-2" FT BINDING 536 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR628472-2" SQ SEQUENCE 572 AA; 62590 MW; 8593C7470334D4FB CRC64; MEEEQDLPER PVKKAKMQEP GEQTLSQVNN PDTSDQKPET ASLASNLSMS EEIMTCTDYI PRSSNDYTSQ MYSAKPYAHI LSVPVSETTY PGQTQYQTLQ QSQPYAVYPQ ATQTYGLPPF GALWPGMKPE SGLIQTPSPS QHSVLTCTTG LTTSQPSPAH YSYPIPASST NASLISTSSA IANIPAAAVA SISNQDYPTY TILGQNQYQA CYPSSSFGVT GQTNSDTENT ALAATTYQTE KPGAMGPAPA TQRLPSDSST SPPLSQTTPN KDADDQARKN MTVKNRGKRK ADASSSQDSE LERVFLWDLD ETIIIFHSLL TGSYAQKYGK DPTVVIGSGL TMEEMIFEVA DTHLFFNDLE ECDQVHVEDV ASDDNGQDLS NYSFSTDGFS GSGGSGSHGS SVGVQGGVDW MRKLAFRYRK VREIYDKHKS NVGGLLSPQR KEALQRLRAE IEVLTDSWLG TALKSLLLIQ SRKNCVNVLI TTTQLVPALA KVLLYGLGEI FPIENIYSAT KIGKESCFER IVSRFGKKVT YVVIGDGRDE EIAAKQHNMP FWRITNHGDL VSLHQALELD FL //