ID LYS2_CAEEL Reviewed; 279 AA. AC O62416; DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 29-MAY-2024, entry version 133. DE RecName: Full=Lysozyme-like protein 2 {ECO:0000305}; DE Flags: Precursor; GN Name=lys-2 {ECO:0000312|WormBase:Y22F5A.5}; GN ORFNames=Y22F5A.5 {ECO:0000312|WormBase:Y22F5A.5}; 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, INDUCTION, AND DISRUPTION PHENOTYPE. RX PubMed=21931778; DOI=10.1371/journal.pone.0024619; RA Boehnisch C., Wong D., Habig M., Isermann K., Michiels N.K., Roeder T., RA May R.C., Schulenburg H.; RT "Protist-type lysozymes of the nematode Caenorhabditis elegans contribute RT to resistance against pathogenic Bacillus thuringiensis."; RL PLoS ONE 6:E24619-E24619(2011). RN [3] {ECO:0000305} RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE. RX PubMed=25274306; DOI=10.1038/nature13818; RA Pellegrino M.W., Nargund A.M., Kirienko N.V., Gillis R., Fiorese C.J., RA Haynes C.M.; RT "Mitochondrial UPR-regulated innate immunity provides resistance to RT pathogen infection."; RL Nature 516:414-417(2014). CC -!- FUNCTION: Involved in resistance to Gram-positive bacteria P.aeruginosa CC or B.thuringiensis infection. {ECO:0000269|PubMed:21931778, CC ECO:0000269|PubMed:25274306}. CC -!- TISSUE SPECIFICITY: Expressed in intestine. CC {ECO:0000269|PubMed:25274306}. CC -!- INDUCTION: Induced in response to Gram-positive bacterium P.aeruginosa CC infection and to mitochondrial stress in the intestine CC (PubMed:25274306). Induced in response to Gram-positive bacterium CC B.thuringiensis (B-18247) infection (PubMed:21931778). CC {ECO:0000269|PubMed:21931778, ECO:0000269|PubMed:25274306}. CC -!- DISRUPTION PHENOTYPE: Reduced survival following bacterium CC B.thuringiensis (B-18247) infection (PubMed:21931778). RNAi-mediated CC knockdown causes a reduction in survival following bacterium CC P.aeruginosa infection (PubMed:25274306). {ECO:0000269|PubMed:21931778, CC ECO:0000269|PubMed:25274306}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family. CC {ECO:0000255|PROSITE-ProRule:PRU01252, ECO:0000305}. CC -!- CAUTION: Lacks conserved active site residues, suggesting it has no CC catalytic activity. {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; BX284605; CAA16324.1; -; Genomic_DNA. DR PIR; T26555; T26555. DR RefSeq; NP_505643.1; NM_073242.5. DR AlphaFoldDB; O62416; -. DR SMR; O62416; -. DR DIP; DIP-25152N; -. DR IntAct; O62416; 2. DR STRING; 6239.Y22F5A.5.1; -. DR EPD; O62416; -. DR PaxDb; 6239-Y22F5A-5; -. DR PeptideAtlas; O62416; -. DR EnsemblMetazoa; Y22F5A.5.1; Y22F5A.5.1; WBGene00003091. DR GeneID; 179429; -. DR KEGG; cel:CELE_Y22F5A.5; -. DR UCSC; Y22F5A.5; c. elegans. DR AGR; WB:WBGene00003091; -. DR CTD; 179429; -. DR WormBase; Y22F5A.5; CE16606; WBGene00003091; lys-2. DR eggNOG; ENOG502S5RB; Eukaryota. DR GeneTree; ENSGT00970000195882; -. DR HOGENOM; CLU_073372_1_0_1; -. DR InParanoid; O62416; -. DR OMA; QYAQVET; -. DR OrthoDB; 2877671at2759; -. DR PhylomeDB; O62416; -. DR PRO; PR:O62416; -. DR Proteomes; UP000001940; Chromosome V. DR Bgee; WBGene00003091; Expressed in larva and 4 other cell types or tissues. DR GO; GO:0003796; F:lysozyme activity; ISS:WormBase. DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:WormBase. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:WormBase. DR GO; GO:0045087; P:innate immune response; IMP:WormBase. DR GO; GO:0009253; P:peptidoglycan catabolic process; ISS:WormBase. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd06416; GH25_Lys1-like; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR002053; Glyco_hydro_25. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR23208; LYSOZYME PROTEIN; 1. DR PANTHER; PTHR23208:SF21; LYSOZYME-LIKE PROTEIN 2; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1. PE 2: Evidence at transcript level; KW Antimicrobial; Immunity; Innate immunity; Reference proteome; Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..279 FT /note="Lysozyme-like protein 2" FT /evidence="ECO:0000255" FT /id="PRO_5004159432" FT DOMAIN 47..265 FT /note="Ch-type lysozyme" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252" SQ SEQUENCE 279 AA; 30291 MW; 1A451F6351F08E4E CRC64; MIKLLVSFTI LFVLSSARPQ EIDSNQAAIA NTEANEAPVI VNNDASMGNA VDFSFPTNVQ VMNCLKKAKY QVVFLRGFVP TGNGAFDSNC VGNIRNAYSA GLGIETYMTP QPISSWQGYQ QLDLLYNGLN NNGITIRSVW IQVTSPANWP NNPTANVNFI NSIISRAQQY GLSVGIYTNQ YDWSQITGNS ANINSNVMLW YWNVLGGGTS GETKPTFADF RAFGPFKKAS VKQYAQVETV CNLVVNRDVY AVGIPAAAPK TEVNMADGEK IVVGGFVGN //