ID A0A1L8ELE2_XENLA Unreviewed; 554 AA.
AC A0A1L8ELE2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Eyes absent homolog {ECO:0000256|RuleBase:RU362036};
DE EC=3.1.3.48 {ECO:0000256|RuleBase:RU362036};
GN Name=eya2.S {ECO:0000313|RefSeq:XP_018093641.1,
GN ECO:0000313|RefSeq:XP_018093642.1,
GN ECO:0000313|Xenbase:XB-GENE-6487243};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|RefSeq:XP_018093641.1};
RN [1] {ECO:0000313|RefSeq:XP_018093641.1, ECO:0000313|RefSeq:XP_018093642.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018093641.1,
RC ECO:0000313|RefSeq:XP_018093642.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018093641.1,
RC ECO:0000313|RefSeq:XP_018093642.1};
RG RefSeq;
RL Submitted (APR-2022) 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_018093641.1; XM_018238152.2.
DR RefSeq; XP_018093642.1; XM_018238153.2.
DR STRING; 8355.A0A1L8ELE2; -.
DR PaxDb; 8355-A0A1L8ELE2; -.
DR GeneID; 108702587; -.
DR KEGG; xla:108702587; -.
DR AGR; Xenbase:XB-GENE-6487243; -.
DR CTD; 108702587; -.
DR Xenbase; XB-GENE-6487243; eya2.S.
DR OMA; ESHPGEY; -.
DR OrthoDB; 452222at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 108702587; Expressed in internal ear and 9 other cell types or tissues.
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:UP000186698};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU362036}.
FT REGION 11..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 290
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR628472-1"
FT ACT_SITE 292
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR628472-1"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR628472-2"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR628472-2"
FT BINDING 518
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR628472-2"
SQ SEQUENCE 554 AA; 60889 MW; 8B82BD75D682A37D CRC64;
MIDLLISQSL SVSSGSSEDL KFDLSDSLPE SPDDIADKSK KVSSRESFPH SGNSKESQQF
TPEGNYSRQY PHIVSPPSVP GMAAYGQTQY SAGIQQTAAY STYPPPGQSY GIPSYSIKTE
DSLSHSPGQS GFLTYGSSFS TSSPGQAPYT YQVHGPSGIY QGANGLANAG AFGSVHQEYS
SYPGFSQGQY PQYYSSSYNS PYVPTNSISP TALSTAAYSI HESSQHISNQ STESLSGEYN
AHNGPSTPIK DAENDRQHRG SDAKLRGRSK RSNDPSPAVD NEIERVFVWD LDETIIIFHS
LLTGTFATRY GKDTTTAVRV GLMMEEMIFN LADTHLFFND LEECDQIHID DVSSDDNGQD
LSTYNFSSDG FHSSAAGANL CLGSGVHGGV DWMRKLAFRY RRVKEMYSTY KNNVGGLIGA
PKRETWLQLR AEMEAVTDLW LTHALKALNL IHSRPNCVNV LVTTTQLIPA IAKVLLYGLG
TVFPIENIYS ATKTGKECCF ERIMQRFGRK AVYVVIGDGV EEEQAAKKHN MPFWRISCHA
DLEALRHALD LEYL
//
