LYSC_RABIT
ID LYSC_RABIT Reviewed; 130 AA.
AC P16973;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Lysozyme C;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase C;
GN Name=LYZ;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Kidney;
RX PubMed=2361954; DOI=10.1093/oxfordjournals.jbchem.a123032;
RA Ito Y., Yamada H., Nakamura S., Imoto T.;
RT "Purification, amino acid sequence, and some properties of rabbit kidney
RT lysozyme.";
RL J. Biochem. 107:236-241(1990).
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 PIR; JC2506; JC2506.
DR PIR; JX0104; JX0104.
DR PIR; JX0367; JX0367.
DR AlphaFoldDB; P16973; -.
DR SMR; P16973; -.
DR STRING; 9986.ENSOCUP00000011947; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR PRIDE; P16973; -.
DR eggNOG; ENOG502S1S1; Eukaryota.
DR InParanoid; P16973; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; IDA:CACAO.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; 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; Direct protein sequencing;
KW Disulfide bond; Glycosidase; Hydrolase; Reference proteome; Secreted.
FT CHAIN 1..130
FT /note="Lysozyme C"
FT /id="PRO_0000208855"
FT DOMAIN 1..130
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 35
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 6..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 30..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 65..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 77..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
SQ SEQUENCE 130 AA; 14722 MW; 000A3330EDB26C25 CRC64;
KIYERCELAR TLKKLGLDGY KGVSLANWMC LAKWESSYNT RATNYNPGDK STDYGIFQIN
SRYWCNDGKT PRAVNACHIP CSDLLKDDIT QAVACAKRVV SDPQGIRAWV AWRNHCQNQD
LTPYIRGCGV
