EYA3_CHICK
ID EYA3_CHICK Reviewed; 119 AA.
AC Q9YH99;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Eyes absent homolog 3;
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:P97480};
DE Flags: Fragment;
GN Name=EYA3;
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: Tyrosine phosphatase that specifically dephosphorylates 'Tyr-
CC 142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone
CC 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. Promotes efficient DNA repair by dephosphorylating H2AX,
CC promoting the recruitment of DNA repair complexes containing MDC1 (By
CC similarity). Its function as histone phosphatase probably explains its
CC role in transcription regulation during organogenesis. May be involved
CC in development of the eye (By similarity).
CC {ECO:0000250|UniProtKB:P97480, ECO:0000250|UniProtKB:Q99504}.
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:P97480};
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:P97480}. Nucleus
CC {ECO:0000250|UniProtKB:P97480}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. EYA family.
CC {ECO:0000305}.
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DR EMBL; AJ008003; CAA07823.1; -; mRNA.
DR AlphaFoldDB; Q9YH99; -.
DR SMR; Q9YH99; -.
DR STRING; 9031.ENSGALP00000001125; -.
DR PaxDb; Q9YH99; -.
DR VEuPathDB; HostDB:geneid_395717; -.
DR eggNOG; KOG3107; Eukaryota.
DR HOGENOM; CLU_021184_2_1_1; -.
DR InParanoid; Q9YH99; -.
DR OrthoDB; 1030296at2759; -.
DR PhylomeDB; Q9YH99; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IEA:InterPro.
DR GO; GO:0140793; F:histone tyrosine phosphatase activity (H2-Y142 specific); ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
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:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR Gene3D; 3.40.50.12350; -; 1.
DR InterPro; IPR028479; EYA3.
DR InterPro; IPR038102; EYA_dom_sf.
DR InterPro; IPR028472; EYA_fam.
DR PANTHER; PTHR10190; PTHR10190; 1.
DR PANTHER; PTHR10190:SF5; PTHR10190:SF5; 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..>119
FT /note="Eyes absent homolog 3"
FT /id="PRO_0000218650"
FT NON_TER 1
FT NON_TER 119
SQ SEQUENCE 119 AA; 13704 MW; E062E2FE4A2C62F8 CRC64;
RKLAFRYRRV REIYDKYKTN VGGLLSPQKR EALQRLRTDI EVLTDSWLET ALKSLLLIQS
RKNCVNILIT TTQLVPALAK VLLYGLGEVF PIENIYSATK IGKESCFERI VSRFGKKVT
