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Database: UniProt
Entry: A0A1S2ZYY4_ERIEU
LinkDB: A0A1S2ZYY4_ERIEU
Original site: A0A1S2ZYY4_ERIEU 
ID   A0A1S2ZYY4_ERIEU        Unreviewed;       478 AA.
AC   A0A1S2ZYY4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Eyes absent homolog {ECO:0000256|RuleBase:RU362036};
DE            EC=3.1.3.48 {ECO:0000256|RuleBase:RU362036};
GN   Name=EYA2 {ECO:0000313|RefSeq:XP_007526780.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007526780.1};
RN   [1] {ECO:0000313|RefSeq:XP_007526780.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001490,
CC         ECO:0000256|RuleBase:RU362036};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR628472-2,
CC         ECO:0000256|RuleBase:RU362036};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR628472-2,
CC       ECO:0000256|RuleBase:RU362036};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. EYA family.
CC       {ECO:0000256|ARBA:ARBA00010501, ECO:0000256|RuleBase:RU362036}.
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DR   RefSeq; XP_007526780.1; XM_007526718.2.
DR   AlphaFoldDB; A0A1S2ZYY4; -.
DR   CTD; 2139; -.
DR   OrthoDB; 452222at2759; -.
DR   Proteomes; UP000079721; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd02601; HAD_Eya; 1.
DR   Gene3D; 3.40.50.12350; -; 1.
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   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   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362036};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR628472-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR628472-2}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW   ECO:0000256|RuleBase:RU362036};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU362036}.
FT   REGION          153..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        214
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628472-1"
FT   ACT_SITE        216
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628472-1"
FT   BINDING         214
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628472-2"
FT   BINDING         216
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628472-2"
FT   BINDING         442
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR628472-2"
SQ   SEQUENCE   478 AA;  52636 MW;  2547BE8307CCE8AD CRC64;
     MAAYGQTQYS AGLQQAASYA TYPPPAQAYG IPSYSIKTED SLNHSPGQSG FLSYGSSFST
     PPTGQSPYTY QMHGQSFKTS MGIYQGANGL ANAAGFGGVH QDYPSYSGFP QSQYSQYYSS
     SYNPPYVPAS SICPSPLSTS TYVLQEASHN IPNQSSESLV GEYNTHNGPP TPAKEGDSDR
     PHRASDGKLR GRSKRSSDPS PAGDNEIERV FVWDLDETII IFHSLLTGTF ASRYGKDTTT
     SVRIGLMMEE MIFNLADTHL FFNDLEDCDQ IHVDDVSSDD NGQDLSTYNF SADGFHSAAP
     GANLCLGSGV HGGVDWMRKL AFRYRRVKEM YNTYKNNVGG LIGAPKRETW LQLRAELEAL
     TDLWLTHSLK ALNLINSRPN CVNVLVTTTQ LIPALAKVLL YGLGSVFPIE NIYSATKTGK
     ESCFERIMQR FGRKAVYIVI GDGVEEEQGA KKHNMPFWRI SCHADLEALR HALELEYL
//
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