ID   EYA1_CHICK              Reviewed;         119 AA.
AC   Q9YHA0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   24-JAN-2024, entry version 107.
DE   RecName: Full=Eyes absent homolog 1;
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
DE   Flags: Fragment;
GN   Name=EYA1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   PubMed=9887327; DOI=10.1093/hmg/8.1.11;
RA   Borsani G., DeGrandi A., Ballabio A., Bulfone A., Bernard L., Banfi S.,
RA   Gattuso C., Mariani M., Dixon M., Donnai D., Metcalfe K., Winter R.,
RA   Robertson M., Axton R., Brown A., van Heyningen V., Hanson I.;
RT   "EYA4, a novel vertebrate gene related to Drosophila eyes absent.";
RL   Hum. Mol. Genet. 8:11-23(1999).
CC   -!- FUNCTION: Functions both as protein phosphatase and as transcriptional
CC       coactivator for SIX1, and probably also for other transcription factors
CC       of this family. Tyrosine phosphatase that dephosphorylates 'Tyr-142' of
CC       histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the
CC       recruitment of DNA repair complexes containing MDC1. 'Tyr-142'
CC       phosphorylation of histone H2AX plays a central role in DNA repair and
CC       acts as a mark that distinguishes between apoptotic and repair
CC       responses to genotoxic stress. Its function as histone phosphatase may
CC       contribute to its function in transcription regulation during
CC       organogenesis. Has also phosphatase activity with proteins
CC       phosphorylated on Ser and Thr residues (in vitro). Required for normal
CC       embryonic development of the skeleton, kidneys and ears (By
CC       similarity). {ECO:0000250|UniProtKB:P97767,
CC       ECO:0000250|UniProtKB:Q99502}.
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:0000250|UniProtKB:Q99502};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000250|UniProtKB:Q99502};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC         Evidence={ECO:0000250|UniProtKB:Q99502};
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99502}. Nucleus
CC       {ECO:0000250|UniProtKB:Q99502}. Note=Localizes at sites of DNA damage
CC       at double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q99502}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. EYA family.
CC       {ECO:0000305}.
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DR   EMBL; AJ008002; CAA07822.1; -; mRNA.
DR   AlphaFoldDB; Q9YHA0; -.
DR   SMR; Q9YHA0; -.
DR   STRING; 9031.ENSGALP00000051963; -.
DR   PaxDb; 9031-ENSGALP00000025135; -.
DR   VEuPathDB; HostDB:geneid_395718; -.
DR   eggNOG; KOG3107; Eukaryota.
DR   HOGENOM; CLU_021184_2_1_1; -.
DR   InParanoid; Q9YHA0; -.
DR   PhylomeDB; Q9YHA0; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0140793; F:histone H2AXY142 phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR   GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR   GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR   GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Activator; Chromatin regulator; Cytoplasm; Developmental protein;
KW   DNA damage; DNA repair; Hydrolase; Magnesium; Nucleus; Protein phosphatase;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           <1..>119
FT                   /note="Eyes absent homolog 1"
FT                   /id="PRO_0000218645"
FT   NON_TER         1
FT   NON_TER         119
SQ   SEQUENCE   119 AA;  13549 MW;  DD24DF364AD166E6 CRC64;
     RKLAFRYRRV KEIYNTYKNN VGGLLGPAKR EAWLQLRAEI EALTDSWLTL ALKALTLIHS
     RTNCVNILVT TTQLIPALAK VLLYGLGVVF PIENIYSATK IGKESCFERI IQRFGRKVV
//