EYA2_BOVIN
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 03-AUG-2022, entry version 103.
DE RecName: Full=Eyes absent homolog 2;
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:O00167};
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=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: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_010811531.2.
DR RefSeq; XP_010809834.1; XM_010811532.2.
DR AlphaFoldDB; Q58DB6; -.
DR SMR; Q58DB6; -.
DR STRING; 9913.ENSBTAP00000017737; -.
DR PaxDb; Q58DB6; -.
DR Ensembl; ENSBTAT00000017737; ENSBTAP00000017737; ENSBTAG00000013336.
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; HTQGYSV; -.
DR OrthoDB; 1030296at2759; -.
DR TreeFam; TF319337; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000013336; Expressed in oviduct epithelium and 85 other tissues.
DR ExpressionAtlas; Q58DB6; baseline.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0140793; F:histone tyrosine phosphatase activity (H2-Y142 specific); ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:Ensembl.
DR GO; GO:0014706; P:striated muscle tissue development; IEA:Ensembl.
DR CDD; cd02601; HAD_Eya; 1.
DR Gene3D; 3.40.50.12350; -; 1.
DR InterPro; IPR028473; EYA2.
DR InterPro; IPR006545; EYA_dom.
DR InterPro; IPR042577; EYA_dom_metazoan.
DR InterPro; IPR038102; EYA_dom_sf.
DR InterPro; IPR028472; EYA_fam.
DR InterPro; IPR036412; HAD-like_sf.
DR PANTHER; PTHR10190; PTHR10190; 1.
DR PANTHER; PTHR10190:SF7; PTHR10190:SF7; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01658; EYA-cons_domain; 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="Eyes absent homolog 2"
FT /id="PRO_0000244420"
FT REGION 210..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..261
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
