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Developmental protein eyes absent (EC 3.1.3.48) (Protein Clift)

 EYA_DROME               Reviewed;         766 AA.
Q05201; Q961V4; Q9VMC1;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
05-DEC-2018, entry version 166.
RecName: Full=Developmental protein eyes absent;
EC=3.1.3.48 {ECO:0000269|PubMed:14628052};
AltName: Full=Protein Clift;
Name=eya; Synonyms=cli; ORFNames=CG9554;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND
SUBCELLULAR LOCATION.
TISSUE=Head;
PubMed=8431945; DOI=10.1016/0092-8674(93)90115-7;
Bonini N.M., Leiserson W.M., Benzer S.;
"The eyes absent gene: genetic control of cell survival and
differentiation in the developing Drosophila eye.";
Cell 72:379-395(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=Berkeley; TISSUE=Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
INTERACTION WITH SO.
PubMed=9428512; DOI=10.1016/S0092-8674(00)80480-8;
Pignoni F., Hu B., Zavitz K.H., Xiao J., Garrity P.A., Zipursky S.L.;
"The eye-specification proteins So and Eya form a complex and regulate
multiple steps in Drosophila eye development.";
Cell 91:881-891(1997).
[6]
INTERACTION WITH DAC.
PubMed=9428513; DOI=10.1016/S0092-8674(00)80481-X;
Chen R., Amoui M., Zhang Z., Mardon G.;
"Dachshund and eyes absent proteins form a complex and function
synergistically to induce ectopic eye development in Drosophila.";
Cell 91:893-903(1997).
[7]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-499.
PubMed=14628052; DOI=10.1038/nature02093;
Rayapureddi J.P., Kattamuri C., Steinmetz B.D., Frankfort B.J.,
Ostrin E.J., Mardon G., Hegde R.S.;
"Eyes absent represents a class of protein tyrosine phosphatases.";
Nature 426:295-298(2003).
[8]
3D-STRUCTURE MODELING OF 493-766, FUNCTION, AND MUTAGENESIS OF
ASP-499; SER-676; LYS-705; ASP-730 AND GLU-734.
PubMed=14628053; DOI=10.1038/nature02097;
Tootle T.L., Silver S.J., Davies E.L., Newman V., Latek R.R.,
Mills I.A., Selengut J.D., Parlikar B.E., Rebay I.;
"The transcription factor Eyes absent is a protein tyrosine
phosphatase.";
Nature 426:299-302(2003).
-!- FUNCTION: Tyrosine phosphatase thought to play a role in
transcription regulation during organogenesis through its
intrinsic protein phosphatase activity (PubMed:14628052,
PubMed:14628053). The phosphatase activity was shown in vitro.
Appears to function together with So and Dac in eye development
(PubMed:9428512, PubMed:9428513). Required for the survival of eye
progenitor cells at a critical stage in morphogenesis
(PubMed:8431945). {ECO:0000269|PubMed:14628052,
ECO:0000269|PubMed:14628053, ECO:0000269|PubMed:8431945,
ECO:0000269|PubMed:9428512, ECO:0000269|PubMed:9428513}.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein]
+ phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136,
Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48;
Evidence={ECO:0000269|PubMed:14628052};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:O00167};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000250|UniProtKB:O00167};
-!- SUBUNIT: Interacts with Dac and So. {ECO:0000269|PubMed:9428512,
ECO:0000269|PubMed:9428513}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8431945}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=I, A;
IsoId=Q05201-1; Sequence=Displayed;
Name=2; Synonyms=II, B;
IsoId=Q05201-2; Sequence=VSP_001500;
-!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. EYA
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L08501; AAA28723.1; -; mRNA.
EMBL; L08502; AAA28310.1; -; mRNA.
EMBL; AE014134; AAF52400.1; -; Genomic_DNA.
EMBL; AE014134; AAN10587.1; -; Genomic_DNA.
EMBL; AY047539; AAK77271.1; -; mRNA.
PIR; A45174; A45174.
PIR; B45174; B45174.
RefSeq; NP_523492.1; NM_078768.4. [Q05201-2]
RefSeq; NP_723188.1; NM_164693.2. [Q05201-1]
UniGene; Dm.5293; -.
ProteinModelPortal; Q05201; -.
SMR; Q05201; -.
BioGrid; 60071; 30.
DIP; DIP-19253N; -.
IntAct; Q05201; 2.
STRING; 7227.FBpp0078964; -.
PaxDb; Q05201; -.
PRIDE; Q05201; -.
EnsemblMetazoa; FBtr0079334; FBpp0078963; FBgn0000320. [Q05201-2]
EnsemblMetazoa; FBtr0079335; FBpp0078964; FBgn0000320. [Q05201-1]
GeneID; 33916; -.
KEGG; dme:Dmel_CG9554; -.
CTD; 33916; -.
FlyBase; FBgn0000320; eya.
eggNOG; KOG3107; Eukaryota.
eggNOG; ENOG410XT12; LUCA.
GeneTree; ENSGT00940000156367; -.
InParanoid; Q05201; -.
KO; K15616; -.
OrthoDB; EOG091G04YD; -.
PhylomeDB; Q05201; -.
Reactome; R-DME-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
ChiTaRS; eya; fly.
GenomeRNAi; 33916; -.
PRO; PR:Q05201; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0000320; Expressed in 54 organ(s), highest expression level in eye disc (Drosophila).
ExpressionAtlas; Q05201; baseline and differential.
Genevisible; Q05201; DM.
GO; GO:0005829; C:cytosol; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IMP:FlyBase.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:FlyBase.
GO; GO:0030946; F:protein tyrosine phosphatase activity, metal-dependent; IDA:FlyBase.
GO; GO:0003713; F:transcription coactivator activity; IMP:FlyBase.
GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
GO; GO:0007411; P:axon guidance; IGI:FlyBase.
GO; GO:0001746; P:Bolwig's organ morphogenesis; IMP:FlyBase.
GO; GO:0042675; P:compound eye cone cell differentiation; IMP:FlyBase.
GO; GO:0048749; P:compound eye development; IMP:FlyBase.
GO; GO:0042051; P:compound eye photoreceptor development; IMP:FlyBase.
GO; GO:0007455; P:eye-antennal disc morphogenesis; IMP:UniProtKB.
GO; GO:0008406; P:gonad development; IMP:FlyBase.
GO; GO:0016576; P:histone dephosphorylation; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IGI:FlyBase.
GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
GO; GO:0008584; P:male gonad development; IMP:FlyBase.
GO; GO:0007498; P:mesoderm development; IMP:FlyBase.
GO; GO:0009996; P:negative regulation of cell fate specification; IMP:FlyBase.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
GO; GO:0001744; P:optic lobe placode formation; IMP:FlyBase.
GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
GO; GO:0070285; P:pigment cell development; IMP:FlyBase.
GO; GO:0007280; P:pole cell migration; TAS:FlyBase.
GO; GO:0045739; P:positive regulation of DNA repair; IBA:GO_Central.
GO; GO:0010628; P:positive regulation of gene expression; IMP:FlyBase.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
GO; GO:0006470; P:protein dephosphorylation; IDA:FlyBase.
GO; GO:0009416; P:response to light stimulus; IMP:FlyBase.
GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
GO; GO:0006351; P:transcription, DNA-templated; TAS:FlyBase.
GO; GO:0007419; P:ventral cord development; IGI:FlyBase.
CDD; cd02601; HAD_Eya; 1.
Gene3D; 3.40.50.12350; -; 1.
InterPro; IPR006545; EYA_dom.
InterPro; IPR038102; EYA_dom_sf.
InterPro; IPR028472; EYA_fam.
PANTHER; PTHR10190; PTHR10190; 1.
TIGRFAMs; TIGR01658; EYA-cons_domain; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome;
Developmental protein; Hydrolase; Magnesium; Metal-binding; Nucleus;
Protein phosphatase; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 766 Developmental protein eyes absent.
/FTId=PRO_0000218655.
COMPBIAS 46 57 Poly-Gln.
COMPBIAS 60 68 Poly-Gln.
COMPBIAS 92 108 Poly-Gly.
COMPBIAS 253 260 Poly-Ala.
COMPBIAS 268 271 Poly-Tyr.
COMPBIAS 305 311 Poly-Ala.
COMPBIAS 428 434 Poly-Ala.
ACT_SITE 499 499 Nucleophile.
{ECO:0000250|UniProtKB:O00167}.
ACT_SITE 501 501 Proton donor.
{ECO:0000250|UniProtKB:O00167}.
METAL 499 499 Magnesium.
{ECO:0000250|UniProtKB:O00167}.
METAL 501 501 Magnesium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:O00167}.
METAL 730 730 Magnesium.
{ECO:0000250|UniProtKB:O00167}.
VAR_SEQ 1 23 MVTLMPYNYAAPRCGLIDKMIEP -> MLYNVPCYQNFSTL
DYY (in isoform 2).
{ECO:0000303|PubMed:12537569,
ECO:0000303|PubMed:8431945}.
/FTId=VSP_001500.
MUTAGEN 499 499 D->N: Highly reduced ectopic eye
induction and diminishes degree of
ommatidial restoration in eyeless
phenotype rescue assay.
{ECO:0000269|PubMed:14628052,
ECO:0000269|PubMed:14628053}.
MUTAGEN 676 676 S->A: Highly reduced ectopic eye
induction and diminishes degree of
ommatidial restoration in eyeless
phenotype rescue assay.
{ECO:0000269|PubMed:14628053}.
MUTAGEN 705 705 K->Q: Highly reduced ectopic eye
induction and diminishes degree of
ommatidial restoration in eyeless
phenotype rescue assay.
{ECO:0000269|PubMed:14628053}.
MUTAGEN 730 730 D->N: Highly reduced ectopic eye
induction. {ECO:0000269|PubMed:14628053}.
MUTAGEN 734 734 E->Q: Highly reduced ectopic eye
induction. {ECO:0000269|PubMed:14628053}.
SEQUENCE 766 AA; 80657 MW; 3581C26AB1811E74 CRC64;
MVTLMPYNYA APRCGLIDKM IEPKVKRPKT DHTDTHERNR LCNLSQQQQQ QQPQQQQTHQ
QQQQQQQQSH QQSHSSTVLA SNGPSSAGAG MGVGVGGGGG SGGGVGGGVG QCSPLGLPPQ
SQPLQPTIGS LASLSGHYSN GNANPNVNSS SCSLATASSF AQSAGSSFST YQQAGGTSGG
VSGEDGVVGG ATVMSHWTHD GTGSSAAVKS ESRSPGQVHA SLDNGSVAGS NLYGCSSASN
PLDGGAVAVN SSAVAAAAAA VYDGKHDYYY YNSMQQYTPP PFYSGYGTPY AAATAARQAK
MEPGAAAAAA AYLTPSYAAS GNNNSQLYSS PYAGYNNFGQ QDYGGYYNEQ YGNYYSPANY
SPYAVSSPSS SASHGHGFHV AASSNLSESP TDTHSTTPVH QTTHSPHSPL PISPSTGSGI
GPLGNVSAAA AAAALNSSGG SSVGTAGSGG VATSKTTPTG KTGRARGRRH QQPSPTRSTA
SDTGNSEAVK PPERVFVWDL DETLIIFHTL LSGSYANRYT KDHSSLMTIA FRMEEMVFNM
ADTHFFFNEI EECDQVHIDD VSSDDNGQDL SAYNFATDGF HTNTPPGAPP NLCLPTGVRG
GVDWMRKLAF RYRKIKDIYN SYRGNVGTLL GPGKREAWLQ IRSEIEVATD NWATLALKCL
SMISQRENCV NVLVTSTQLA PALAKVLLFG LGGIFNIENI YSAHKIGHET CYERIVTRFG
RKSTYVVIGD GNEEETAAKA MNFPFWRISA HSDIRALYTA LDMGFL


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