LYS2_CAEEL
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 03-AUG-2022, entry version 126.
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}.
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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; -.
DR EPD; O62416; -.
DR PaxDb; O62416; -.
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 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; 1437716at2759; -.
DR PhylomeDB; O62416; -.
DR PRO; PR:O62416; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003091; Expressed in larva and 4 other 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 InterPro; IPR002053; Glyco_hydro_25.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR SUPFAM; SSF51445; SSF51445; 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
