EYA1_CHICK
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 03-AUG-2022, entry version 101.
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.ENSGALP00000025135; -.
DR PaxDb; Q9YHA0; -.
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; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0140793; F:histone tyrosine phosphatase activity (H2-Y142 specific); ISS:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; IEA:InterPro.
DR Gene3D; 3.40.50.12350; -; 1.
DR InterPro; IPR028478; EYA4.
DR InterPro; IPR038102; EYA_dom_sf.
DR InterPro; IPR028472; EYA_fam.
DR PANTHER; PTHR10190; PTHR10190; 1.
DR PANTHER; PTHR10190:SF17; PTHR10190:SF17; 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
