Reviewed, UniProtKB/Swiss-Prot P00706 (LYSC3_ANAPL)

Names and origin

Protein names	Recommended name:     Lysozyme C-3     EC=3.2.1.17 Alternative name(s):     1,4-beta-N-acetylmuramidase
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	129 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Sequence similarities	Belongs to the glycosyl hydrolase 22 family.

Ontologies

Keywords
Molecular function	Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall 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
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular function	lysozyme activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 129	129	Lysozyme C-3		PRO_0000208859
Sites
	Active site	35	1	By similarity
	Active site	52	1	By similarity
Amino acid modifications
	Disulfide bond	6 ↔ 127
	Disulfide bond	30 ↔ 115
	Disulfide bond	64 ↔ 80
	Disulfide bond	76 ↔ 94
Natural variations
	Natural variant	37	1	S → G in 30% of the molecules.

Sequences

	Sequence		Length	Mass (Da)
	P00706-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 4A859252D260FA46	FASTA	129	14,507
	10 20 30 40 50 60 KVYERCELAA AMKRLGLDNY RGYSLGNWVC AANYESSFNT QATNRNTDGS TDYGILEINS 70 80 90 100 110 120 RWWCDNGKTP RAKNACGIPC SVLLRSDITE AVKCAKRIVS DGDGMNAWVA WRNRCKGTDV SRWIRGCRL

References

[1]	"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. Strain: Kaki duck. Tissue: Egg white.

Cross-references

Sequence databases
PIR	LZDK3. A00861.
3D structure databases
HSSP	HSSP built from PDB template 1AT6 based on UniProtKB P00698.
SMR	P00706. Positions 1-129.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P00706.
Family and domain databases
InterPro	IPR001916. Glyco_hydro_22. 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

LYSC3_ANAPL

Accession

Primary (citable) accession number: P00706

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	November 25, 2008
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)