Reviewed, UniProtKB/Swiss-Prot P00705 (LYSC1_ANAPL)

Names and origin

Protein names	Recommended name:     Lysozyme C-1     EC=3.2.1.17 Alternative name(s):     1,4-beta-N-acetylmuramidase C
Organism	Anas platyrhynchos (Domestic duck) (Anas boschas)
Taxonomic identifier	8839 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Anseriformes › Anatidae › Anas

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
Catalytic activity	Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Miscellaneous	Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides. The sequence of the DL-2 variant of lysozyme C from Pekin duck is shown. As only one lysozyme, or any combination of 2 lysozymes, but never all 3, occurred in one egg, the existence of 3 alleles at one locus has been suggested. The amino acid compositions of DL-1, DL-2, and DL-3 are identical with those of lysozymes A, B, and C, respectively. DL-1 and DL-2 are electrophoretically and immunologically indistinguishable from lysozymes A and B, respectively.
Sequence similarities	Belongs to the glycosyl hydrolase 22 family.

Ontologies

Keywords
Domain	Signal
Molecular function	Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	lysozyme activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Ref.2 Ref.3
	Chain	19 – 147	129	Lysozyme C-1		PRO_0000018494
Sites
	Active site	53	1	By similarity
	Active site	70	1	By similarity
Amino acid modifications
	Disulfide bond	24 ↔ 145		Ref.4
	Disulfide bond	48 ↔ 133		Ref.4
	Disulfide bond	82 ↔ 98		Ref.4
	Disulfide bond	94 ↔ 112		Ref.4
Natural variations
	Natural variant	43	1	L → I in DL3.
	Natural variant	55	1	G → S in DL1 and lysozyme II.
	Natural variant	75	1	Q → E in lysozyme II.
	Natural variant	89	1	R → G in DL1 and lysozyme II.
	Natural variant	97	1	P → R in DL3.

Sequences

	Sequence		Length	Mass (Da)
	P00705-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: B0F2B6A9F7DA3978	FASTA	147	16,363
	10 20 30 40 50 60 MKALLTLVFC LLPLAAQGKV YSRCELAAAM KRLGLDNYRG YSLGNWVCAA NYESGFNTQA 70 80 90 100 110 120 TNRNTDGSTD YGILQINSRW WCDNGKTPRS KNACGIPCSV LLRSDITEAV RCAKRIVSDG 130 140 DGMNAWVAWR NRCRGTDVSK WIRGCRL

References

[1]	"Evolutionary shift in the site of cleavage of prelysozyme." Weisman L.S., Krummel B.M., Wilson A.C. J. Biol. Chem. 261:2309-2313(1986) [PubMed: 3511061] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-18. Strain: Pekin breed.
[2]	"Chemical and immunological properties and amino acid sequences of three lysozymes from Peking-duck egg white." Kondo K., Fujio H., Amano T. J. Biochem. 91:571-587(1982) [PubMed: 7068576] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-147 (DL-1; DL-2 AND DL-3). Strain: Pekin breed.
[3]	"Multiple forms of duck-egg white lysozyme. Primary structure of two duck lysozymes." Hermann J., Jolles J., Jolles P. Eur. J. Biochem. 24:12-17(1971) [PubMed: 5138644] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-147 (LYSOZYME II).
[4]	"The disulfide bridges of duck egg-white lysozyme II." Hermann J., Jolles J., Jolles P. Arch. Biochem. Biophys. 158:355-358(1973) [PubMed: 4580844] [Abstract] Cited for: DISULFIDE BONDS.
[5]	"Multiple lysozymes of duck egg white." Prager E.M., Wilson A.C. J. Biol. Chem. 246:523-530(1971) [PubMed: 5542021] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS DL-1; DL-2 AND DL-3C. Strain: Pekin breed.

Cross-references

Sequence databases
PIR	LZDK. D92574.
3D structure databases
HSSP	HSSP built from PDB template 1AT6 based on UniProtKB P00698.
SMR	P00705. Positions 19-147.
ModBase	Search...
Protein family/group databases
CAZy	GH22. Glycoside Hydrolase Family 22.
Phylogenomic databases
HOVERGEN	P00705.
Enzyme and pathway databases
BRENDA	3.2.1.17. 3217.
Family and domain databases
InterPro	IPR001916. Glyco_hydro_22. IPR019799. Glyco_hydro_22_CS. IPR000974. Glyco_hydro_22_lys. [Graphical view]
Pfam	PF00062. Lys. 1 hit. [Graphical view]
PRINTS	PR00137. LYSOZYME. PR00135. LYZLACT.
SMART	SM00263. LYZ1. 1 hit. [Graphical view]
PROSITE	PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit. PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LYSC1_ANAPL

Accession

Primary (citable) accession number: P00705

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)