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Q05201 (EYA_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Developmental protein eyes absent

EC=3.1.3.48
Alternative name(s):
Protein Clift
Gene names
Name:eya
Synonyms:cli
ORF Names:CG9554
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length766 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Thought to play a role in transcription regulation during organogenesis through its intrinsic protein phosphatase activity. The phosphatase activity was shown in vitro. Appears to function together with So and Dac in eye development. Required for the survival of eye progenitor cells at a critical stage in morphogenesis.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.7

Cofactor

Binds 1 Mg2+ ion per subunit By similarity.

Subunit structure

Interacts with Dac and So. Ref.5 Ref.6

Subcellular location

Nucleus.

Sequence similarities

Belongs to the HAD-like hydrolase superfamily. EYA family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandMagnesium
Metal-binding
   Molecular functionActivator
Developmental protein
Hydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBolwig's organ morphogenesis

Inferred from mutant phenotype PubMed 10704398. Source: FlyBase

axon guidance

Inferred from genetic interaction PubMed 19217428. Source: FlyBase

compound eye development

Inferred from mutant phenotype Ref.7PubMed 19217428. Source: FlyBase

compound eye photoreceptor development

Inferred from mutant phenotype PubMed 15242803. Source: FlyBase

eye-antennal disc morphogenesis

Inferred from mutant phenotype Ref.1. Source: UniProtKB

gonad development

Inferred from mutant phenotype PubMed 21377458. Source: FlyBase

innate immune response

Inferred from genetic interaction PubMed 22916150. Source: FlyBase

larval somatic muscle development

Inferred from mutant phenotype PubMed 19217429. Source: FlyBase

male gonad development

Inferred from mutant phenotype PubMed 12919673. Source: FlyBase

mesoderm development

Inferred from mutant phenotype PubMed 16171793. Source: FlyBase

negative regulation of cell fate specification

Inferred from mutant phenotype PubMed 12403709. Source: FlyBase

optic lobe placode formation

Inferred from mutant phenotype PubMed 10357938. Source: FlyBase

ovarian follicle cell development

Inferred from mutant phenotype PubMed 15944190. Source: FlyBase

peptidyl-tyrosine dephosphorylation

Inferred from direct assay Ref.7Ref.8. Source: GOC

photoreceptor cell axon guidance

Inferred from mutant phenotype PubMed 19217428. Source: FlyBase

pole cell migration

Traceable author statement PubMed 9637912. Source: FlyBase

positive regulation of gene expression

Inferred from mutant phenotype PubMed 20580700. Source: FlyBase

positive regulation of transcription from RNA polymerase II promoter

Inferred from physical interaction PubMed 16125693. Source: FlyBase

protein dephosphorylation

Inferred from direct assay Ref.7Ref.8. Source: FlyBase

response to light stimulus

Inferred from mutant phenotype PubMed 17307880. Source: FlyBase

salivary gland morphogenesis

Inferred from mutant phenotype PubMed 16171793. Source: FlyBase

spermatogenesis

Inferred from mutant phenotype PubMed 12781687. Source: FlyBase

transcription, DNA-templated

Traceable author statement PubMed 10821764. Source: FlyBase

ventral cord development

Inferred from genetic interaction PubMed 19217428. Source: FlyBase

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 19217428. Source: FlyBase

nucleus

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoprotein phosphatase activity

Inferred from mutant phenotype PubMed 22916150. Source: FlyBase

protein tyrosine phosphatase activity

Inferred from direct assay Ref.8. Source: FlyBase

protein tyrosine phosphatase activity, metal-dependent

Inferred from direct assay Ref.7. Source: FlyBase

transcription factor binding

Inferred from physical interaction PubMed 16125693. Source: FlyBase

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q05201-1)

Also known as: I; A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q05201-2)

Also known as: II; B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MVTLMPYNYAAPRCGLIDKMIEP → MLYNVPCYQNFSTLDYY

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 766766Developmental protein eyes absent
PRO_0000218655

Regions

Compositional bias46 – 5712Poly-Gln
Compositional bias60 – 689Poly-Gln
Compositional bias92 – 10817Poly-Gly
Compositional bias253 – 2608Poly-Ala
Compositional bias268 – 2714Poly-Tyr
Compositional bias305 – 3117Poly-Ala
Compositional bias428 – 4347Poly-Ala

Sites

Active site4991Nucleophile By similarity
Active site5011Proton donor By similarity
Metal binding4991Magnesium By similarity
Metal binding5011Magnesium By similarity
Metal binding7301Magnesium By similarity

Natural variations

Alternative sequence1 – 2323MVTLM…KMIEP → MLYNVPCYQNFSTLDYY in isoform 2.
VSP_001500

Experimental info

Mutagenesis4991D → N: Highly reduced ectopic eye induction and diminishes degree of ommatidial restoration in eyeless phenotype rescue assay. Ref.7 Ref.8
Mutagenesis6761S → A: Highly reduced ectopic eye induction and diminishes degree of ommatidial restoration in eyeless phenotype rescue assay. Ref.8
Mutagenesis7051K → Q: Highly reduced ectopic eye induction and diminishes degree of ommatidial restoration in eyeless phenotype rescue assay. Ref.8
Mutagenesis7301D → N: Highly reduced ectopic eye induction. Ref.8
Mutagenesis7341E → Q: Highly reduced ectopic eye induction. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (I) (A) [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 3581C26AB1811E74

FASTA76680,657
        10         20         30         40         50         60 
MVTLMPYNYA APRCGLIDKM IEPKVKRPKT DHTDTHERNR LCNLSQQQQQ QQPQQQQTHQ 

        70         80         90        100        110        120 
QQQQQQQQSH QQSHSSTVLA SNGPSSAGAG MGVGVGGGGG SGGGVGGGVG QCSPLGLPPQ 

       130        140        150        160        170        180 
SQPLQPTIGS LASLSGHYSN GNANPNVNSS SCSLATASSF AQSAGSSFST YQQAGGTSGG 

       190        200        210        220        230        240 
VSGEDGVVGG ATVMSHWTHD GTGSSAAVKS ESRSPGQVHA SLDNGSVAGS NLYGCSSASN 

       250        260        270        280        290        300 
PLDGGAVAVN SSAVAAAAAA VYDGKHDYYY YNSMQQYTPP PFYSGYGTPY AAATAARQAK 

       310        320        330        340        350        360 
MEPGAAAAAA AYLTPSYAAS GNNNSQLYSS PYAGYNNFGQ QDYGGYYNEQ YGNYYSPANY 

       370        380        390        400        410        420 
SPYAVSSPSS SASHGHGFHV AASSNLSESP TDTHSTTPVH QTTHSPHSPL PISPSTGSGI 

       430        440        450        460        470        480 
GPLGNVSAAA AAAALNSSGG SSVGTAGSGG VATSKTTPTG KTGRARGRRH QQPSPTRSTA 

       490        500        510        520        530        540 
SDTGNSEAVK PPERVFVWDL DETLIIFHTL LSGSYANRYT KDHSSLMTIA FRMEEMVFNM 

       550        560        570        580        590        600 
ADTHFFFNEI EECDQVHIDD VSSDDNGQDL SAYNFATDGF HTNTPPGAPP NLCLPTGVRG 

       610        620        630        640        650        660 
GVDWMRKLAF RYRKIKDIYN SYRGNVGTLL GPGKREAWLQ IRSEIEVATD NWATLALKCL 

       670        680        690        700        710        720 
SMISQRENCV NVLVTSTQLA PALAKVLLFG LGGIFNIENI YSAHKIGHET CYERIVTRFG 

       730        740        750        760 
RKSTYVVIGD GNEEETAAKA MNFPFWRISA HSDIRALYTA LDMGFL 

« Hide

Isoform 2 (II) (B) [UniParc].

Checksum: 7BCC45472692B844
Show »

FASTA76080,164

References

« Hide 'large scale' references
[1]"The eyes absent gene: genetic control of cell survival and differentiation in the developing Drosophila eye."
Bonini N.M., Leiserson W.M., Benzer S.
Cell 72:379-395(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Head.
[2]"The genome sequence of Drosophila melanogaster."
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. expand/collapse author list , 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.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
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.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: Berkeley.
Tissue: Head.
[5]"The eye-specification proteins So and Eya form a complex and regulate multiple steps in Drosophila eye development."
Pignoni F., Hu B., Zavitz K.H., Xiao J., Garrity P.A., Zipursky S.L.
Cell 91:881-891(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SO.
[6]"Dachshund and eyes absent proteins form a complex and function synergistically to induce ectopic eye development in Drosophila."
Chen R., Amoui M., Zhang Z., Mardon G.
Cell 91:893-903(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAC.
[7]"Eyes absent represents a class of protein tyrosine phosphatases."
Rayapureddi J.P., Kattamuri C., Steinmetz B.D., Frankfort B.J., Ostrin E.J., Mardon G., Hegde R.S.
Nature 426:295-298(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-499.
[8]"The transcription factor Eyes absent is a protein tyrosine phosphatase."
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.
Nature 426:299-302(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 493-766, MUTAGENESIS OF ASP-499; SER-676; LYS-705; ASP-730 AND GLU-734.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L08501 mRNA. Translation: AAA28723.1.
L08502 mRNA. Translation: AAA28310.1.
AE014134 Genomic DNA. Translation: AAF52400.1.
AE014134 Genomic DNA. Translation: AAN10587.1.
AY047539 mRNA. Translation: AAK77271.1.
PIRA45174.
B45174.
RefSeqNP_523492.1. NM_078768.3.
NP_723188.1. NM_164693.2.
UniGeneDm.5293.

3D structure databases

ProteinModelPortalQ05201.
SMRQ05201. Positions 493-766.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid60071. 18 interactions.
DIPDIP-19253N.
IntActQ05201. 2 interactions.

Proteomic databases

PRIDEQ05201.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0079335; FBpp0078964; FBgn0000320. [Q05201-1]
GeneID33916.
KEGGdme:Dmel_CG9554.

Organism-specific databases

CTD33916.
FlyBaseFBgn0000320. eya.

Phylogenomic databases

eggNOGNOG297494.
GeneTreeENSGT00390000008860.
InParanoidQ05201.
KOK15616.
OMAYNSMQQY.
OrthoDBEOG7DNNTZ.
PhylomeDBQ05201.

Gene expression databases

BgeeQ05201.

Family and domain databases

InterProIPR028480. Develop_EYA.
IPR006545. EYA_dom.
IPR028472. EYA_fam.
[Graphical view]
PANTHERPTHR10190. PTHR10190. 1 hit.
PTHR10190:SF12. PTHR10190:SF12. 1 hit.
TIGRFAMsTIGR01658. EYA-cons_domain. 1 hit.
ProtoNetSearch...

Other

ChiTaRSeya. drosophila.
GenomeRNAi33916.
NextBio785901.

Entry information

Entry nameEYA_DROME
AccessionPrimary (citable) accession number: Q05201
Secondary accession number(s): Q961V4, Q9VMC1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase