Reviewed, UniProtKB/Swiss-Prot P79180 (LYSC_HYLLA)

Names and origin

Protein names

Recommended name:
    Lysozyme C
    EC=3.2.1.17
Alternative name(s):
    1,4-beta-N-acetylmuramidase C

Gene names

Name:	LYZ
Synonyms:	LZM

Organism

Hylobates lar (Common gibbon)

Taxonomic identifier

9580 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hylobatidae › Hylobates

Protein attributes

Sequence length	148 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Subunit structure	Monomer.
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
Domain	Signal
Molecular function	Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase
PTM	Disulfide bond
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	By similarity
	Chain	19 – 148	130	Lysozyme C		PRO_0000018468
Sites
	Active site	53	1	By similarity
	Active site	71	1	By similarity
Amino acid modifications
	Disulfide bond	24 ↔ 146		By similarity
	Disulfide bond	48 ↔ 134		By similarity
	Disulfide bond	83 ↔ 99		By similarity
	Disulfide bond	95 ↔ 113		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P79180-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 19A62932D0784822	FASTA	148	16,676
	10 20 30 40 50 60 MKALIILGLV LLSVMVQAKV FERCELARTL KRLGMDGYRG ISLANWMCLA KWESGYNTRA 70 80 90 100 110 120 TNYNPGDRST DYGIFQINSR YWCNDGKTPG AVNACHLSCN ALLQDNIADA VACAKRVVRD 130 140 PQGIRAWVAW RNRCQNRDLR QYIQGCGV

References

[1]	"Episodic adaptive evolution of primate lysozymes." Messier W., Stewart C.B. Nature 385:151-154(1997) [PubMed: 8990116] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Blood.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U76915 mRNA. Translation: AAB41206.1.
3D structure databases
SMR	P79180. Positions 19-148.
ModBase	Search...
Protein family/group databases
CAZy	GH22. Glycoside Hydrolase Family 22.
Phylogenomic databases
HOVERGEN	P79180.
Enzyme and pathway databases
BRENDA	3.2.1.17. 285274.
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

LYSC_HYLLA

Accession

Primary (citable) accession number: P79180

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 1997
Last modified:	November 24, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)