EYA1_CAEEL
ID EYA1_CAEEL Reviewed; 503 AA.
AC O17670; Q564S5;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Eyes absent homolog 1 {ECO:0000255|RuleBase:RU362036, ECO:0000303|PubMed:25108328};
DE EC=3.1.3.48 {ECO:0000255|RuleBase:RU362036};
GN Name=eya-1 {ECO:0000303|PubMed:16154558, ECO:0000312|WormBase:C49A1.4a};
GN ORFNames=C49A1.4 {ECO:0000312|WormBase:C49A1.4a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16154558; DOI=10.1016/j.ydbio.2005.08.011;
RA Furuya M., Qadota H., Chisholm A.D., Sugimoto A.;
RT "The C. elegans eyes absent ortholog EYA-1 is required for tissue
RT differentiation and plays partially redundant roles with PAX-6.";
RL Dev. Biol. 286:452-463(2005).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CEH-34, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=19427847; DOI=10.1016/j.ydbio.2009.05.538;
RA Amin N.M., Lim S.E., Shi H., Chan T.L., Liu J.;
RT "A conserved Six-Eya cassette acts downstream of Wnt signaling to direct
RT non-myogenic versus myogenic fates in the C. elegans postembryonic
RT mesoderm.";
RL Dev. Biol. 331:350-360(2009).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CEH-34, AND DEVELOPMENTAL STAGE.
RX PubMed=20713707; DOI=10.1073/pnas.1010023107;
RA Hirose T., Galvin B.D., Horvitz H.R.;
RT "Six and Eya promote apoptosis through direct transcriptional activation of
RT the proapoptotic BH3-only gene egl-1 in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:15479-15484(2010).
RN [5] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25108328; DOI=10.1134/s0006297914070074;
RA Wang B.Y., Xu X.S., Cui Y.X., Wang H., Liu G., Zhao Z.J., Ma J.F., Fu X.Q.;
RT "Caenorhabditis elegans eyes absent ortholog EYA-1 is required for stress
RT resistance.";
RL Biochemistry (Mosc.) 79:653-662(2014).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=30890567; DOI=10.1242/dev.168153;
RA Brandt J.P., Rossillo M., Du Z., Ichikawa D., Barnes K., Chen A., Noyes M.,
RA Bao Z., Ringstad N.;
RT "Lineage context switches the function of a C. elegans Pax6 homolog in
RT determining a neuronal fate.";
RL Development 146:0-0(2019).
CC -!- FUNCTION: Tyrosine protein phosphatase (By similarity). Acts probably
CC as a transcription regulator in the embryonic and postembryonic
CC development of several tissues including pharynx, vulva and gonads
CC (PubMed:16154558). Required for the development of anterior tissues
CC during late embryogenesis (PubMed:16154558). Together with ceh-34,
CC required to specify the coelomocyte fate in embryonic and postembryonic
CC precursors (PubMed:19427847). In the anterior part of the embryo,
CC prevents apoptosis in cells that are not fated to die
CC (PubMed:16154558). Together with ceh-34 activates proapoptotic factor
CC egl-1 expression to promote motor neuron M4 sister cell apoptosis
CC (PubMed:20713707). Also promotes apoptosis of I1 pharyngeal neuron
CC sister cell (PubMed:20713707). Plays a role in locomotion and fertility
CC (PubMed:16154558). May play a role in resistance to heat and oxidative
CC stresses (PubMed:25108328). May cooperate with the transcription
CC factors vab-3 and ceh-32 to repress transcription factor ets-5
CC expression in non BAG neuronal cells (PubMed:30890567).
CC {ECO:0000250|UniProtKB:Q05201, ECO:0000269|PubMed:16154558,
CC ECO:0000269|PubMed:19427847, ECO:0000269|PubMed:20713707,
CC ECO:0000269|PubMed:25108328, ECO:0000269|PubMed:30890567}.
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:0000255|RuleBase:RU362036};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|RuleBase:RU362036};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|RuleBase:RU362036};
CC -!- SUBUNIT: Interacts (via C-terminus) with ceh-34 (via N-terminus).
CC {ECO:0000269|PubMed:19427847, ECO:0000269|PubMed:20713707}.
CC -!- INTERACTION:
CC O17670; Q11103: C02F12.8; NbExp=3; IntAct=EBI-311862, EBI-317531;
CC O17670; Q94165: ceh-34; NbExp=3; IntAct=EBI-311862, EBI-2413136;
CC O17670; H2KZ78: CELE_C35E7.2; NbExp=3; IntAct=EBI-311862, EBI-317600;
CC O17670; Q9XXU2: CELE_C53C7.3; NbExp=3; IntAct=EBI-311862, EBI-317612;
CC O17670; Q9N4P3: CELE_ZK121.2; NbExp=3; IntAct=EBI-311862, EBI-317902;
CC O17670; Q21127: meg-2; NbExp=3; IntAct=EBI-311862, EBI-317734;
CC O17670; Q10923: ntl-2; NbExp=3; IntAct=EBI-311862, EBI-313231;
CC O17670; Q10666: pop-1; NbExp=4; IntAct=EBI-311862, EBI-317870;
CC O17670; Q9XZI6: unc-11; NbExp=4; IntAct=EBI-311862, EBI-311866;
CC O17670; O17894: unc-39; NbExp=5; IntAct=EBI-311862, EBI-317698;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16154558,
CC ECO:0000269|PubMed:19427847}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:C49A1.4a};
CC IsoId=O17670-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C49A1.4b};
CC IsoId=O17670-2; Sequence=VSP_059346;
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscles (PubMed:25108328).
CC Expressed in BAG sensory neurons and in other head neurons
CC (PubMed:30890567). {ECO:0000269|PubMed:25108328,
CC ECO:0000269|PubMed:30890567}.
CC -!- DEVELOPMENTAL STAGE: Expression starts at the embryonic bean stage in
CC several anterior cells and continues until hatching (PubMed:16154558).
CC Between the 1.5-fold and pretzel embryonic stages, expressed in a
CC subset of pharyngeal cells and several anterior body wall muscle cells
CC (PubMed:16154558). Expressed in the M lineage-derived coelomocyte
CC precursor cells M.dlpa and M.drpa and in the 6 differentiated
CC coelomocytes throughout development (PubMed:19427847). Expressed in the
CC M4 motor neuron sister cell (PubMed:20713707).
CC {ECO:0000269|PubMed:16154558, ECO:0000269|PubMed:19427847,
CC ECO:0000269|PubMed:20713707}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in severe lethal
CC arrest at an early larval stage (PubMed:16154558). The pharyngeal
CC structure is disorganized and the anterior tip is thinner
CC (PubMed:16154558). The phenotype is more severe in a pax-6 (ju468)
CC mutant background (PubMed:16154558). RNAi-mediated knockdown in L1
CC larvae causes a decrease in resistance to heat or oxidative stresses
CC characterized by a reduced lifespan, reduced heat shock protein hsp-
CC 16.2 expression and increased reactive oxygen species (ROS) production
CC (PubMed:25108328). {ECO:0000269|PubMed:16154558,
CC ECO:0000269|PubMed:25108328}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. EYA family.
CC {ECO:0000255|RuleBase:RU362036}.
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DR EMBL; BX284601; CAB05707.2; -; Genomic_DNA.
DR EMBL; BX284601; CAI79139.1; -; Genomic_DNA.
DR PIR; T20047; T20047.
DR RefSeq; NP_001021055.1; NM_001025884.4. [O17670-1]
DR RefSeq; NP_001021056.1; NM_001025885.2.
DR AlphaFoldDB; O17670; -.
DR SMR; O17670; -.
DR DIP; DIP-26060N; -.
DR IntAct; O17670; 119.
DR STRING; 6239.C49A1.4a; -.
DR MoonDB; O17670; Predicted.
DR PaxDb; O17670; -.
DR EnsemblMetazoa; C49A1.4a.1; C49A1.4a.1; WBGene00001377. [O17670-1]
DR EnsemblMetazoa; C49A1.4b.1; C49A1.4b.1; WBGene00001377. [O17670-2]
DR EnsemblMetazoa; C49A1.4b.2; C49A1.4b.2; WBGene00001377. [O17670-2]
DR EnsemblMetazoa; C49A1.4b.3; C49A1.4b.3; WBGene00001377. [O17670-2]
DR GeneID; 173293; -.
DR KEGG; cel:CELE_C49A1.4; -.
DR UCSC; C49A1.4a; c. elegans.
DR CTD; 173293; -.
DR WormBase; C49A1.4a; CE36113; WBGene00001377; eya-1. [O17670-1]
DR WormBase; C49A1.4b; CE15722; WBGene00001377; eya-1. [O17670-2]
DR eggNOG; KOG3107; Eukaryota.
DR GeneTree; ENSGT00950000182978; -.
DR InParanoid; O17670; -.
DR OMA; QCASANN; -.
DR OrthoDB; 1150654at2759; -.
DR PhylomeDB; O17670; -.
DR Reactome; R-CEL-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR SignaLink; O17670; -.
DR PRO; PR:O17670; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001377; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:WormBase.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:WormBase.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0048598; P:embryonic morphogenesis; IMP:WormBase.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0007501; P:mesodermal cell fate specification; IMP:WormBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:WormBase.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:1904747; P:positive regulation of apoptotic process involved in development; IMP:UniProtKB.
DR GO; GO:1900036; P:positive regulation of cellular response to heat; IMP:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; IBA:GO_Central.
DR GO; GO:1902884; P:positive regulation of response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0048729; P:tissue morphogenesis; IMP:WormBase.
DR CDD; cd02601; HAD_Eya; 1.
DR Gene3D; 3.40.50.12350; -; 1.
DR InterPro; IPR042577; EYA_dom_metazoan.
DR InterPro; IPR038102; EYA_dom_sf.
DR InterPro; IPR028472; EYA_fam.
DR PANTHER; PTHR10190; PTHR10190; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Hydrolase; Magnesium;
KW Metal-binding; Nucleus; Protein phosphatase; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..503
FT /note="Eyes absent homolog 1"
FT /id="PRO_0000443422"
FT ACT_SITE 237
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT ACT_SITE 239
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT BINDING 237
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O00167"
FT VAR_SEQ 1..34
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_059346"
SQ SEQUENCE 503 AA; 54522 MW; 53720CB133525C5C CRC64;
MLPDSEGQKL KTFLLGTGTT LDPSLDPTGN SNFSMATTSD SSTIWTALPA SQPGDKDIPT
VDLAAISEAY GSTSSTTSLT SSVTSQYQYN SYPQYAMYTS ANPANYYQQV TANLRAGTTA
FPYSLTTPSY YGSYPVDYTS AAAAYQNPYY TNLRGGTAAP YYNPLNATTA AAYASVASSV
LGTDAVNLGT SSDGSTGVPS TVTSFSLKEK KPKVSKKKKT GSCSPGDETY ARVFIWDIDD
IAVISRNYLA SVTHTNEFYA RAANSVSHLM ERIALNNFAD VNEFLEGDIT NIEDAVVDET
TMDSGPIDNL RGLDVMRRVA PKYSAFRQFY TENSTKNDVA GFKQEQNGFN FELLERVGFG
AREATELYQS AIQLQTLPNF GQRWPCAQRC MDLVVEKSKL SAEKYANVVL SNDGLVLGAA
QLMISGLNSS VPVENIYSIS KQGKESVFEK IQSRFGKKCS FICITSGDTA NSAKRLNIPV
WPLNSNTDLD KLYSALDNFL LGG
