LYS1_CAEEL
ID LYS1_CAEEL Reviewed; 298 AA.
AC O62415;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Lysozyme-like protein 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=lys-1 {ECO:0000312|WormBase:Y22F5A.4};
GN ORFNames=Y22F5A.4 {ECO:0000312|WormBase:Y22F5A.4};
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, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12176330; DOI=10.1016/s0960-9822(02)00928-4;
RA Mallo G.V., Kurz C.L., Couillault C., Pujol N., Granjeaud S., Kohara Y.,
RA Ewbank J.J.;
RT "Inducible antibacterial defense system in C. elegans.";
RL Curr. Biol. 12:1209-1214(2002).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21209831; DOI=10.1371/journal.pone.0015902;
RA Jensen V.L., Simonsen K.T., Lee Y.H., Park D., Riddle D.L.;
RT "RNAi screen of DAF-16/FOXO target genes in C. elegans links pathogenesis
RT and dauer formation.";
RL PLoS ONE 5:E15902-E15902(2010).
RN [4] {ECO:0000305}
RP INDUCTION.
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).
CC -!- FUNCTION: Involved in resistance to Gram-negative bacterium
CC S.marcescens and to bacterium Gram-positive S.aureus infection.
CC {ECO:0000269|PubMed:12176330, ECO:0000269|PubMed:21209831}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle lumen
CC {ECO:0000269|PubMed:12176330}. Note=Localizes in vesicles in the apical
CC region of intestinal cells. {ECO:0000269|PubMed:12176330}.
CC -!- TISSUE SPECIFICITY: Expressed in intestine, IL2 and IL6 neurons and
CC some neurons in the head ganglia. {ECO:0000269|PubMed:12176330}.
CC -!- INDUCTION: Induced by Gram-negative bacteria S.marcescens and
CC B.thuringiensis infection. {ECO:0000269|PubMed:12176330,
CC ECO:0000269|PubMed:21931778}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a reduction in
CC survival in response to bacterium S.aureus infection.
CC {ECO:0000269|PubMed:21209831}.
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; CAA16323.1; -; Genomic_DNA.
DR PIR; T26554; T26554.
DR RefSeq; NP_505642.1; NM_073241.3.
DR AlphaFoldDB; O62415; -.
DR SMR; O62415; -.
DR DIP; DIP-26293N; -.
DR IntAct; O62415; 5.
DR STRING; 6239.Y22F5A.4.2; -.
DR CAZy; GH25; Glycoside Hydrolase Family 25.
DR EPD; O62415; -.
DR PaxDb; O62415; -.
DR PeptideAtlas; O62415; -.
DR EnsemblMetazoa; Y22F5A.4.1; Y22F5A.4.1; WBGene00003090.
DR GeneID; 179428; -.
DR KEGG; cel:CELE_Y22F5A.4; -.
DR UCSC; Y22F5A.4.1; c. elegans.
DR CTD; 179428; -.
DR WormBase; Y22F5A.4; CE16605; WBGene00003090; lys-1.
DR eggNOG; ENOG502S5RB; Eukaryota.
DR GeneTree; ENSGT00970000195882; -.
DR HOGENOM; CLU_073372_1_0_1; -.
DR InParanoid; O62415; -.
DR OMA; ITGNWAT; -.
DR OrthoDB; 1437716at2759; -.
DR PhylomeDB; O62415; -.
DR PRO; PR:O62415; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003090; Expressed in larva and 4 other tissues.
DR GO; GO:0045177; C:apical part of cell; IDA:WormBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
DR GO; GO:0060205; C:cytoplasmic vesicle lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; IEA:InterPro.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEP: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; IEA:InterPro.
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; Cytoplasmic vesicle; Immunity; Innate immunity;
KW Reference proteome; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..298
FT /note="Lysozyme-like protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5004159237"
FT DOMAIN 59..277
FT /note="Ch-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
SQ SEQUENCE 298 AA; 32379 MW; 2AB1984E5BD234BF CRC64;
MLKLAFVTFL FALASARPQD VDSNRVVALP QDNFEVTDIG FEKIKAEPAP EVVNNDASYA
YAVDISVPTT VSQMNCLKTS RYAAVFIRGF TPFGSGAFDT TSVTSIRNAY SAGLGIEVYM
TPQPLSSLQG YQQLDALYNG LNGNGITIRS VWIQVTSPAN WQKSATTNVN FLNSIISRAK
QYGLTVGIYT NQYDWSQITG NWATLSSDVL LWYWHVLGGG VTGETPATFD DFRAFGSFKK
ASVKQFAQVE SVCSLTVNRD VYVVGIPAAA SSKNTDFFTQ EDISSNNKKI VVGGVIGV
