ID H2ZYU8_LATCH Unreviewed; 579 AA.
AC H2ZYU8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
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|Ensembl:ENSLACP00000002569.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000002569.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000002569.1}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; AFYH01112086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01112087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01112088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01112089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01112090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01112091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01112092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01112093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H2ZYU8; -.
DR STRING; 7897.ENSLACP00000002569; -.
DR Ensembl; ENSLACT00000002589.1; ENSLACP00000002569.1; ENSLACG00000002294.1.
DR eggNOG; KOG3107; Eukaryota.
DR GeneTree; ENSGT00950000182978; -.
DR HOGENOM; CLU_021184_2_1_1; -.
DR InParanoid; H2ZYU8; -.
DR OMA; ESHPGEY; -.
DR TreeFam; TF319337; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000002294; Expressed in mesonephros and 1 other cell type or tissue.
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 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.
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:UP000008672};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU362036}.
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 315
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR628472-1"
FT ACT_SITE 317
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR628472-1"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR628472-2"
FT BINDING 317
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR628472-2"
FT BINDING 543
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR628472-2"
SQ SEQUENCE 579 AA; 64206 MW; A41F1436C8496BAB CRC64;
KEMLDLVTPH SGTTSGECPG NSKLNFLHIH STTPNGTEDK SKQVKSSEAV SAPLSTTAED
SGAEFGWKNN FPSRRKHAFN EKQNYHSKLY RSYPHIVSTP FFQSMAAYGQ AQYSAGIQQA
AAYTAYPPPG QAYGIPSYSI KTEDSLSHSP GQSGIFSYSS NFSPSPAGQA PYSYQMHGSN
ITSGIYQESN GLASPAGFST THQEYSLYPS FSQGQYPQYY SSHYSSPYVT GNISPSALST
TTHQLQEQSY SVTNHSTESL AGDYNTHSSP PTPIKDAESD RQRRGSDGKL RGRSKRSNAP
AHLLENEIER VFIWDLDETI IVFHSLLTGT FASRYGKDAT ISVSLGLRME EMIFNLADTH
LFFNDLEDCD QVHIDDVSSD DNGQDLSKYN FADDGFHNTA TGVNLCLGSG VHGGVDWMRK
LAFRYRRVKE IYSTYKNNIG GLIGPAKREV WLQLRAEMEA LTDLWLTHAL KALNLIHSRP
NSVNVLVSTT QIIPALAKVL LYGLGTVFPI ENIYSAIKAG KDSCFERIMQ RFGRKAVYVV
VGDGVEEEQA ARKHSMPFWR ISSHQDLEAL RHALELEYL
//
