ID   EYA2_BOVIN              Reviewed;         537 AA.
AC   Q58DB6;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   04-NOV-2026, entry version 121.
DE   RecName: Full=Protein phosphatase EYA2 {ECO:0000305};
DE            EC=3.1.3.48 {ECO:0000250|UniProtKB:O00167};
DE   AltName: Full=Eyes absent homolog 2;
GN   Name=EYA2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Functions both as protein phosphatase and as transcriptional
CC       coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5.
CC       Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX
CC       (H2AXY142ph) and promotes efficient DNA repair via the recruitment of
CC       DNA repair complexes containing MDC1. 'Tyr-142' phosphorylation of
CC       histone H2AX plays a central role in DNA repair and acts as a mark that
CC       distinguishes between apoptotic and repair responses to genotoxic
CC       stress. Its function as histone phosphatase may contribute to its
CC       function in transcription regulation during organogenesis. Plays an
CC       important role in hypaxial muscle development together with SIX1 and
CC       DACH2; in this it is functionally redundant with EYA1.
CC       {ECO:0000250|UniProtKB:O00167}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978; EC=3.1.3.48;
CC         Evidence={ECO:0000250|UniProtKB:O00167};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:O00167};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:O00167};
CC   -!- SUBUNIT: Interacts with DACH2 and SIX1, and probably with SIX2, SIX4
CC       and SIX5. Interacts with CAPN8 (By similarity). Interacts with GNAZ and
CC       GNAI2; this precludes interaction with SIX1 (By similarity).
CC       {ECO:0000250, ECO:0000250|UniProtKB:O00167}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O00167}. Nucleus
CC       {ECO:0000250|UniProtKB:O00167}. Note=Retained in the cytoplasm via
CC       interaction with GNAZ and GNAI2. Interaction with SIX1, SIX2, SIX4 or
CC       SIX5 is required for translocation to the nucleus.
CC       {ECO:0000250|UniProtKB:O00167}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. EYA family.
CC       {ECO:0000305}.
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DR   EMBL; BT021681; AAX46528.1; -; mRNA.
DR   RefSeq; NP_001030541.1; NM_001035464.1.
DR   RefSeq; XP_010809833.1; XM_010811531.4.
DR   RefSeq; XP_010809834.1; XM_010811532.4.
DR   AlphaFoldDB; Q58DB6; -.
DR   SMR; Q58DB6; -.
DR   FunCoup; Q58DB6; 49.
DR   STRING; 9913.ENSBTAP00000017737; -.
DR   GlyGen; Q58DB6; 1 site.
DR   PaxDb; 9913-ENSBTAP00000017737; -.
DR   Ensembl; ENSBTAT00000152574.1; ENSBTAP00000104554.1; ENSBTAG00000013336.6.
DR   GeneID; 615264; -.
DR   KEGG; bta:615264; -.
DR   CTD; 2139; -.
DR   VEuPathDB; HostDB:ENSBTAG00000013336; -.
DR   VGNC; VGNC:28671; EYA2.
DR   eggNOG; KOG3107; Eukaryota.
DR   GeneTree; ENSGT00950000182978; -.
DR   HOGENOM; CLU_021184_2_0_1; -.
DR   InParanoid; Q58DB6; -.
DR   OMA; AAYTNMQ; -.
DR   OrthoDB; 167668at2759; -.
DR   Reactome; R-BTA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Proteomes; UP000009136; Chromosome 13.
DR   Bgee; ENSBTAG00000013336; Expressed in oviduct epithelium and 85 other cell types or tissues.
DR   ExpressionAtlas; Q58DB6; baseline.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0140793; F:histone H2AXY142 phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0045739; P:positive regulation of DNA repair; IBA:GO_Central.
DR   CDD; cd02601; HAD_Eya; 1.
DR   FunFam; 3.40.50.12350:FF:000001; Eyes absent homolog; 1.
DR   Gene3D; 3.40.50.12350; -; 1.
DR   InterPro; IPR028472; EYA.
DR   InterPro; IPR006545; EYA_dom.
DR   InterPro; IPR042577; EYA_dom_metazoan.
DR   InterPro; IPR038102; EYA_dom_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   NCBIfam; TIGR01658; EYA-cons_domain; 1.
DR   PANTHER; PTHR10190; EYES ABSENT; 1.
DR   PANTHER; PTHR10190:SF7; EYES ABSENT HOMOLOG 2; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   2: Evidence at transcript level;
KW   Activator; Chromatin regulator; Cytoplasm; Developmental protein;
KW   DNA damage; DNA repair; Hydrolase; Magnesium; Metal-binding; Nucleus;
KW   Protein phosphatase; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..537
FT                   /note="Protein phosphatase EYA2"
FT                   /id="PRO_0000244420"
FT   REGION          210..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        273
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O00167"
FT   ACT_SITE        275
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O00167"
FT   BINDING         273
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O00167"
FT   BINDING         275
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O00167"
FT   BINDING         501
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O00167"
SQ   SEQUENCE   537 AA;  58807 MW;  081635FDF8BEE2DF CRC64;
     MLELLVSASL TVNSDRPGKL KPSRADADVW TLSDREGITT SARSVSQLFA RPCPRVPPGQ
     PPSAMAAYSQ TQYSAGIQQA TPYTAYPPPA QAYGIPSYSI KTEDSLNHSP GQSGFLSYGS
     SFSTPASGQS PYTYQMHGTA GIYQGANGLT NAAGFGTVHQ DYPSYPGFPQ SQYSQYYSSS
     YNPPYVPASS ICPSPLSTST YVLQEASHNI PSQSSESLGG EYNTHNGPST PAKEGDTDRP
     PRASDGKLRG RSKRSSDPSP AGDNEIERVF VWDLDETIII FHSLLTGTFA SRYGKDTTAS
     VRIGLMMEEM IFNLADTHLF FNDLEDCDQI HVDDVSSDDN GQDLSTYNFS ADGFHSSAPG
     ANLCLGSGVH GGVDWMRKLA FRYRRVKEMY NTYKNNVGGL IGAPKRETWL QLRAELEALT
     DLWLTHSLKA LNLINSRPNC VNVLVTTTQL IPALAKVLLY GLGSVFPIEN IYSATKTGKE
     SCFERIMQRF GRKAVYIVIG DGVEEEQGAK KHNMPFWRIS CHADLEALRH ALELEYL
//