EYA_DROME
ID EYA_DROME Reviewed; 766 AA.
AC Q05201; Q961V4; Q9VMC1;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Developmental protein eyes absent;
DE EC=3.1.3.48 {ECO:0000269|PubMed:14628052};
DE AltName: Full=Protein Clift;
GN Name=eya; Synonyms=cli; ORFNames=CG9554;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Head;
RX PubMed=8431945; DOI=10.1016/0092-8674(93)90115-7;
RA Bonini N.M., Leiserson W.M., Benzer S.;
RT "The eyes absent gene: genetic control of cell survival and differentiation
RT in the developing Drosophila eye.";
RL Cell 72:379-395(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP INTERACTION WITH SO.
RX PubMed=9428512; DOI=10.1016/s0092-8674(00)80480-8;
RA Pignoni F., Hu B., Zavitz K.H., Xiao J., Garrity P.A., Zipursky S.L.;
RT "The eye-specification proteins So and Eya form a complex and regulate
RT multiple steps in Drosophila eye development.";
RL Cell 91:881-891(1997).
RN [6]
RP INTERACTION WITH DAC.
RX PubMed=9428513; DOI=10.1016/s0092-8674(00)80481-x;
RA Chen R., Amoui M., Zhang Z., Mardon G.;
RT "Dachshund and eyes absent proteins form a complex and function
RT synergistically to induce ectopic eye development in Drosophila.";
RL Cell 91:893-903(1997).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-499.
RX PubMed=14628052; DOI=10.1038/nature02093;
RA Rayapureddi J.P., Kattamuri C., Steinmetz B.D., Frankfort B.J.,
RA Ostrin E.J., Mardon G., Hegde R.S.;
RT "Eyes absent represents a class of protein tyrosine phosphatases.";
RL Nature 426:295-298(2003).
RN [8]
RP 3D-STRUCTURE MODELING OF 493-766, FUNCTION, AND MUTAGENESIS OF ASP-499;
RP SER-676; LYS-705; ASP-730 AND GLU-734.
RX PubMed=14628053; DOI=10.1038/nature02097;
RA Tootle T.L., Silver S.J., Davies E.L., Newman V., Latek R.R., Mills I.A.,
RA Selengut J.D., Parlikar B.E., Rebay I.;
RT "The transcription factor Eyes absent is a protein tyrosine phosphatase.";
RL Nature 426:299-302(2003).
CC -!- FUNCTION: Tyrosine phosphatase thought to play a role in transcription
CC regulation during organogenesis through its intrinsic protein
CC phosphatase activity (PubMed:14628052, PubMed:14628053). The
CC phosphatase activity was shown in vitro. Appears to function together
CC with So and Dac in eye development (PubMed:9428512, PubMed:9428513).
CC Required for the survival of eye progenitor cells at a critical stage
CC in morphogenesis (PubMed:8431945). {ECO:0000269|PubMed:14628052,
CC ECO:0000269|PubMed:14628053, ECO:0000269|PubMed:8431945,
CC ECO:0000269|PubMed:9428512, ECO:0000269|PubMed:9428513}.
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:0000269|PubMed:14628052};
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 Dac and So. {ECO:0000269|PubMed:9428512,
CC ECO:0000269|PubMed:9428513}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8431945}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=I, A;
CC IsoId=Q05201-1; Sequence=Displayed;
CC Name=2; Synonyms=II, B;
CC IsoId=Q05201-2; Sequence=VSP_001500;
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. EYA family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L08501; AAA28723.1; -; mRNA.
DR EMBL; L08502; AAA28310.1; -; mRNA.
DR EMBL; AE014134; AAF52400.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10587.1; -; Genomic_DNA.
DR EMBL; AY047539; AAK77271.1; -; mRNA.
DR PIR; A45174; A45174.
DR PIR; B45174; B45174.
DR RefSeq; NP_523492.1; NM_078768.4. [Q05201-2]
DR RefSeq; NP_723188.1; NM_164693.2. [Q05201-1]
DR AlphaFoldDB; Q05201; -.
DR SMR; Q05201; -.
DR BioGRID; 60071; 37.
DR DIP; DIP-19253N; -.
DR IntAct; Q05201; 2.
DR STRING; 7227.FBpp0078964; -.
DR PaxDb; Q05201; -.
DR EnsemblMetazoa; FBtr0079334; FBpp0078963; FBgn0000320. [Q05201-2]
DR EnsemblMetazoa; FBtr0079335; FBpp0078964; FBgn0000320. [Q05201-1]
DR GeneID; 33916; -.
DR KEGG; dme:Dmel_CG9554; -.
DR CTD; 33916; -.
DR FlyBase; FBgn0000320; eya.
DR VEuPathDB; VectorBase:FBgn0000320; -.
DR eggNOG; KOG3107; Eukaryota.
DR GeneTree; ENSGT00950000182978; -.
DR InParanoid; Q05201; -.
DR OMA; NVNPSSC; -.
DR PhylomeDB; Q05201; -.
DR Reactome; R-DME-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR SignaLink; Q05201; -.
DR BioGRID-ORCS; 33916; 0 hits in 3 CRISPR screens.
DR ChiTaRS; eya; fly.
DR GenomeRNAi; 33916; -.
DR PRO; PR:Q05201; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000320; Expressed in eye disc (Drosophila) and 58 other tissues.
DR ExpressionAtlas; Q05201; baseline and differential.
DR Genevisible; Q05201; DM.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IMP:FlyBase.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:FlyBase.
DR GO; GO:0030946; F:protein tyrosine phosphatase activity, metal-dependent; IDA:FlyBase.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:FlyBase.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IGI:FlyBase.
DR GO; GO:0001746; P:Bolwig's organ morphogenesis; IMP:FlyBase.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0042675; P:compound eye cone cell differentiation; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0042051; P:compound eye photoreceptor development; IMP:FlyBase.
DR GO; GO:0007455; P:eye-antennal disc morphogenesis; IMP:UniProtKB.
DR GO; GO:0008406; P:gonad development; IMP:FlyBase.
DR GO; GO:0045087; P:innate immune response; IGI:FlyBase.
DR GO; GO:0001744; P:insect visual primordium formation; IMP:FlyBase.
DR GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
DR GO; GO:0008584; P:male gonad development; IMP:FlyBase.
DR GO; GO:0007498; P:mesoderm development; IMP:FlyBase.
DR GO; GO:0009996; P:negative regulation of cell fate specification; IMP:FlyBase.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
DR GO; GO:0070285; P:pigment cell development; IMP:FlyBase.
DR GO; GO:0045739; P:positive regulation of DNA repair; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:FlyBase.
DR GO; GO:0009416; P:response to light stimulus; IMP:FlyBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR GO; GO:0007419; P:ventral cord development; IGI:FlyBase.
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 PANTHER; PTHR10190; PTHR10190; 1.
DR TIGRFAMs; TIGR01658; EYA-cons_domain; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Developmental protein; Hydrolase;
KW Magnesium; Metal-binding; Nucleus; Protein phosphatase; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..766
FT /note="Developmental protein eyes absent"
FT /id="PRO_0000218655"
FT REGION 22..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 499
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT ACT_SITE 501
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT BINDING 499
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"
FT BINDING 730
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT VAR_SEQ 1..23
FT /note="MVTLMPYNYAAPRCGLIDKMIEP -> MLYNVPCYQNFSTLDYY (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:8431945"
FT /id="VSP_001500"
FT MUTAGEN 499
FT /note="D->N: Highly reduced ectopic eye induction and
FT diminishes degree of ommatidial restoration in eyeless
FT phenotype rescue assay."
FT /evidence="ECO:0000269|PubMed:14628052,
FT ECO:0000269|PubMed:14628053"
FT MUTAGEN 676
FT /note="S->A: Highly reduced ectopic eye induction and
FT diminishes degree of ommatidial restoration in eyeless
FT phenotype rescue assay."
FT /evidence="ECO:0000269|PubMed:14628053"
FT MUTAGEN 705
FT /note="K->Q: Highly reduced ectopic eye induction and
FT diminishes degree of ommatidial restoration in eyeless
FT phenotype rescue assay."
FT /evidence="ECO:0000269|PubMed:14628053"
FT MUTAGEN 730
FT /note="D->N: Highly reduced ectopic eye induction."
FT /evidence="ECO:0000269|PubMed:14628053"
FT MUTAGEN 734
FT /note="E->Q: Highly reduced ectopic eye induction."
FT /evidence="ECO:0000269|PubMed:14628053"
SQ 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
