ILYS3_CAEEL
ID ILYS3_CAEEL Reviewed; 139 AA.
AC O76357;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Invertebrate-type lysozyme 3 {ECO:0000305};
DE EC=3.2.1.17 {ECO:0000305|PubMed:27525822};
DE AltName: Full=1,4-beta-N-acetylmuramidase {ECO:0000305};
DE Flags: Precursor;
GN Name=ilys-3 {ECO:0000312|WormBase:C45G7.3};
GN ORFNames=C45G7.3 {ECO:0000312|WormBase:C45G7.3};
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 TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=20617181; DOI=10.1371/journal.ppat.1000982;
RA Irazoqui J.E., Troemel E.R., Feinbaum R.L., Luhachack L.G.,
RA Cezairliyan B.O., Ausubel F.M.;
RT "Distinct pathogenesis and host responses during infection of C. elegans by
RT P. aeruginosa and S. aureus.";
RL PLoS Pathog. 6:E1000982-E1000982(2010).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=27525822; DOI=10.1371/journal.ppat.1005826;
RA Gravato-Nobre M.J., Vaz F., Filipe S., Chalmers R., Hodgkin J.;
RT "The invertebrate lysozyme effector ILYS-3 is systemically activated in
RT response to danger signals and confers antimicrobial protection in C.
RT elegans.";
RL PLoS Pathog. 12:E1005826-E1005826(2016).
CC -!- FUNCTION: Has bacteriolytic activity against Gram-positive bacteria.
CC Plays a role in defense against bacterial pathogens. Involved in
CC pharyngeal grinder function by enabling proper lysis of ingested
CC bacteria. {ECO:0000269|PubMed:27525822}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC between N-acetyl-D-glucosamine residues in chitodextrins.;
CC EC=3.2.1.17; Evidence={ECO:0000305|PubMed:27525822};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.5-5. {ECO:0000269|PubMed:27525822};
CC -!- SUBCELLULAR LOCATION: Late endosome lumen
CC {ECO:0000269|PubMed:27525822}. Recycling endosome lumen
CC {ECO:0000269|PubMed:27525822}. Lysosome lumen
CC {ECO:0000269|PubMed:27525822}. Secreted {ECO:0000269|PubMed:27525822}.
CC Note=Predominantly localizes to the recycling endosomal network in the
CC basolateral region of intestinal cells. Secreted in the intestinal
CC lumen only during dauer arrest stage, aging, or starvation.
CC {ECO:0000269|PubMed:27525822}.
CC -!- TISSUE SPECIFICITY: Expressed in pharynx grinder muscle pm7, isthmus
CC marginal cell mc2 and pharyngeal muscle cell pm5, intestinal cells and
CC at lower levels in coelomocytes and epidermis (PubMed:27525822).
CC Expressed at low levels in intestine (PubMed:20617181).
CC {ECO:0000269|PubMed:20617181, ECO:0000269|PubMed:27525822}.
CC -!- DEVELOPMENTAL STAGE: Expression levels are low throughout larval stages
CC and then increase in adults. Intestinal expression starts at the L1
CC larval stage, declines at the L2 larval stage and increases again in L4
CC larvae and adults. Highly expressed in the intestinal lumen of dauer
CC larvae and, old and no longer self-fertile adults.
CC {ECO:0000269|PubMed:27525822}.
CC -!- INDUCTION: Induced in the intestine by Gram-positive bacteria
CC M.nematophilum CBX102 and UV336 and M.luteus DMS20030 infection but not
CC by Gram-negative bacterium P.aeruginosa PAO1 infection
CC (PubMed:27525822). Induced in the intestine, pharynx and vulva by Gram-
CC positive bacterium S.aureus infection (PubMed:20617181). Induced by
CC Gram-positive bacterium B.subtilis (PubMed:20617181). Induced by
CC starvation (PubMed:27525822). {ECO:0000269|PubMed:20617181,
CC ECO:0000269|PubMed:27525822}.
CC -!- DISRUPTION PHENOTYPE: Slight reduction in brood size. 24 percent
CC reduction in lifespan which is further reduced upon M.nematophilum
CC CBX102 bacterial infection. Impaired food digestion characterized by
CC the accumulation of unlysed E.coli in the intestine. Accumulation of
CC unlysed bacteria is stronger upon M.nematophilum CBX102 infection.
CC {ECO:0000269|PubMed:27525822}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family. Type-I
CC lysozyme subfamily. {ECO:0000255|PROSITE-ProRule:PRU01257}.
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DR EMBL; BX284604; CCD65531.1; -; Genomic_DNA.
DR PIR; T33137; T33137.
DR RefSeq; NP_500206.1; NM_067805.4.
DR AlphaFoldDB; O76357; -.
DR SMR; O76357; -.
DR STRING; 6239.C45G7.3; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR MEROPS; S81.001; -.
DR PaxDb; O76357; -.
DR PeptideAtlas; O76357; -.
DR EnsemblMetazoa; C45G7.3.1; C45G7.3.1; WBGene00016670.
DR GeneID; 177033; -.
DR KEGG; cel:CELE_C45G7.3; -.
DR UCSC; C45G7.3; c. elegans.
DR CTD; 177033; -.
DR WormBase; C45G7.3; CE24850; WBGene00016670; ilys-3.
DR eggNOG; ENOG502SAEY; Eukaryota.
DR GeneTree; ENSGT00940000166559; -.
DR HOGENOM; CLU_130604_1_0_1; -.
DR InParanoid; O76357; -.
DR OMA; DCNGDNA; -.
DR OrthoDB; 1343143at2759; -.
DR PhylomeDB; O76357; -.
DR PRO; PR:O76357; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00016670; Expressed in adult organism and 1 other tissue.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0031906; C:late endosome lumen; IDA:UniProtKB.
DR GO; GO:0043202; C:lysosomal lumen; IDA:UniProtKB.
DR GO; GO:0034777; C:recycling endosome lumen; IDA:UniProtKB.
DR GO; GO:0003796; F:lysozyme activity; IDA:UniProtKB.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd16890; lyz_i; 1.
DR InterPro; IPR008597; Invert_lysozyme.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR PANTHER; PTHR11195; PTHR11195; 1.
DR Pfam; PF05497; Destabilase; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS51909; LYSOZYME_I; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Bacteriolytic enzyme; Digestion; Disulfide bond;
KW Endosome; Glycosidase; Hydrolase; Lysosome; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..139
FT /note="Invertebrate-type lysozyme 3"
FT /evidence="ECO:0000255"
FT /id="PRO_5004159989"
FT DOMAIN 19..138
FT /note="I-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT ACT_SITE 28
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT ACT_SITE 39
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT BINDING 51..57
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8IU26"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8IU26"
FT BINDING 113..115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8IU26"
FT DISULFID 20..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT DISULFID 23..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT DISULFID 25..31
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT DISULFID 36..45
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT DISULFID 58..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT DISULFID 76..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT DISULFID 98..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
SQ SEQUENCE 139 AA; 14995 MW; 41E32BE61CA88593 CRC64;
MFVKSLVFLT IAVAYASADC LHCICMRESG CKPIGCNMDV GSLSCGYYQI KLPYYEDCGQ
PTKKSGETTE AAWKRCANDL SCATTCVENY YNRYKSQCAG TGQGACEVMA RNHNGGPQGC
KHSGTLGYWN GIKSCCGCS
