LYSC2_PIG
ID LYSC2_PIG Reviewed; 146 AA.
AC P12068;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Lysozyme C-2;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase C;
DE Flags: Precursor;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8728388; DOI=10.1006/mpev.1996.0025;
RA Yu M., Irwin D.M.;
RT "Evolution of stomach lysozyme: the pig lysozyme gene.";
RL Mol. Phylogenet. Evol. 5:298-308(1996).
RN [2]
RP PROTEIN SEQUENCE OF 19-146.
RC TISSUE=Stomach;
RX PubMed=2504928; DOI=10.1007/bf02602933;
RA Jolles J., Jolles P., Bowman B.H., Prager E.M., Stewart C.-B., Wilson A.C.;
RT "Episodic evolution in the stomach lysozymes of ruminants.";
RL J. Mol. Evol. 28:528-535(1989).
CC -!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those in
CC tissues and body fluids are associated with the monocyte-macrophage
CC system and enhance the activity of immunoagents.
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;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MISCELLANEOUS: Lysozyme C is capable of both hydrolysis and
CC transglycosylation; it shows also a slight esterase activity. It acts
CC rapidly on both peptide-substituted and unsubstituted peptidoglycan,
CC and slowly on chitin oligosaccharides.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR EMBL; U28757; AAB16862.1; -; Genomic_DNA.
DR RefSeq; NP_999557.2; NM_214392.2.
DR AlphaFoldDB; P12068; -.
DR SMR; P12068; -.
DR STRING; 9823.ENSSSCP00000000522; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR PaxDb; P12068; -.
DR PeptideAtlas; P12068; -.
DR PRIDE; P12068; -.
DR GeneID; 100157211; -.
DR KEGG; ssc:100157211; -.
DR CTD; 4069; -.
DR eggNOG; ENOG502S1S1; Eukaryota.
DR HOGENOM; CLU_111620_0_1_1; -.
DR InParanoid; P12068; -.
DR OrthoDB; 1551203at2759; -.
DR TreeFam; TF324882; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P12068; SS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; IBA:GO_Central.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR001916; Glyco_hydro_22.
DR InterPro; IPR019799; Glyco_hydro_22_CS.
DR InterPro; IPR000974; Glyco_hydro_22_lys.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR030056; Lysozyme_C.
DR PANTHER; PTHR11407; PTHR11407; 1.
DR PANTHER; PTHR11407:SF28; PTHR11407:SF28; 1.
DR Pfam; PF00062; Lys; 1.
DR PRINTS; PR00137; LYSOZYME.
DR PRINTS; PR00135; LYZLACT.
DR SMART; SM00263; LYZ1; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE 1: Evidence at protein level;
KW Antimicrobial; Bacteriolytic enzyme; Digestion; Direct protein sequencing;
KW Disulfide bond; Glycosidase; Hydrolase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:2504928"
FT CHAIN 19..146
FT /note="Lysozyme C-2"
FT /id="PRO_0000018479"
FT DOMAIN 19..146
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 24..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 48..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 81..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 93..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
SQ SEQUENCE 146 AA; 16484 MW; C2986F5CAAAF49F4 CRC64;
MKTLLVLALL LLSVSVQAKV YDRCEFARIL KKSGMDGYRG VSLANWVCLA KWESDFNTKA
INHNVGSTDY GIFQINSRYW CNDGKTPKAV NACHISCKVL LDDDLSQDIE CAKRVVRDPL
GVKAWVAWRA HCQNKDVSQY IRGCKL
