LSY13_CAEEL
ID LSY13_CAEEL Reviewed; 247 AA.
AC A3QMD7; A0A0K3AXE0;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=ING family member lsy-13 {ECO:0000303|PubMed:20923973};
DE AltName: Full=Laterally symmetric protein 13 {ECO:0000312|WormBase:T06A10.4a};
GN Name=lsy-13 {ECO:0000312|WormBase:T06A10.4a};
GN ORFNames=T06A10.4 {ECO:0000312|WormBase:T06A10.4a};
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, AND TISSUE SPECIFICITY.
RX PubMed=20923973; DOI=10.1534/genetics.110.123661;
RA O'Meara M.M., Zhang F., Hobert O.;
RT "Maintenance of neuronal laterality in Caenorhabditis elegans through MYST
RT histone acetyltransferase complex components LSY-12, LSY-13 and LIN-49.";
RL Genetics 186:1497-1502(2010).
CC -!- FUNCTION: Required to initiate and then maintain lateralized gene
CC expression in the ASE sensory neurons (PubMed:20923973). Involved in
CC determining cell fate in the ASE neurons (PubMed:20923973).
CC {ECO:0000269|PubMed:20923973}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H160}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:T06A10.4a};
CC IsoId=A3QMD7-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:T06A10.4b};
CC IsoId=A3QMD7-2; Sequence=VSP_061561;
CC -!- TISSUE SPECIFICITY: Expressed widely, including in the two ASE neurons.
CC {ECO:0000269|PubMed:20923973}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000305}.
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DR EMBL; BX284604; CAM36369.1; -; Genomic_DNA.
DR EMBL; BX284604; CTQ86663.1; -; Genomic_DNA.
DR PIR; T33654; T33654.
DR RefSeq; NP_001299962.1; NM_001313033.1.
DR RefSeq; NP_502999.1; NM_070598.6.
DR SMR; A3QMD7; -.
DR STRING; 6239.T06A10.4; -.
DR EPD; A3QMD7; -.
DR PaxDb; A3QMD7; -.
DR PeptideAtlas; A3QMD7; -.
DR EnsemblMetazoa; T06A10.4a.1; T06A10.4a.1; WBGene00020287.
DR UCSC; T06A10.4; c. elegans.
DR WormBase; T06A10.4a; CE19561; WBGene00020287; lsy-13.
DR WormBase; T06A10.4b; CE50543; WBGene00020287; lsy-13.
DR eggNOG; KOG1973; Eukaryota.
DR GeneTree; ENSGT00940000169515; -.
DR HOGENOM; CLU_1116623_0_0_1; -.
DR InParanoid; A3QMD7; -.
DR OMA; HFTCIGM; -.
DR OrthoDB; 1434088at2759; -.
DR PhylomeDB; A3QMD7; -.
DR Reactome; R-CEL-3214847; HATs acetylate histones.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00020287; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; A3QMD7; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR028651; ING_fam.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10333; PTHR10333; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Metal-binding; Nucleus; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..247
FT /note="ING family member lsy-13"
FT /id="PRO_0000456040"
FT ZN_FING 175..224
FT /note="PHD-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-51"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-51"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-51"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-51"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-51"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-51"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-51"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-51"
FT VAR_SEQ 1..75
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_061561"
SQ SEQUENCE 247 AA; 28136 MW; 2BDC71DF4FAD0B71 CRC64;
MEIDDCVIDM IQVFSKINRE VPEKAKKAIV EIERLDILAK KEMEVAKKHK IEFFANYEEM
TAEQKTKAFT FMQKKMAKVS EYSDQKIEIA SGLKVLLKDV YGKFMEEEQK FIENLNKIPK
APETPPSSSP SVRSHRKKKL SEGDDDAPSS VDEKKRGRKK KPESEKAVAA AEPPKMYCWC
QLDKNDTMIE CENPGCKYGW FHFTCIGMIT APAGDWYCTN ECRAQGLAAV AEAPQKAPQR
KGLKKKK
