P05105 (LYS_HYACE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Lysozyme EC=3.2.1.17 Alternative name(s): 1,4-beta-N-acetylmuramidase
Organism	Hyalophora cecropia (Cecropia moth)
Taxonomic identifier	7123 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Amphiesmenoptera › Lepidoptera › Glossata › Neolepidoptera › Heteroneura › Ditrysia › Obtectomera › Bombycoidea › Saturniiformes › Saturniidae › Saturniinae › Attacini › Hyalophora

Protein attributes

Sequence length	139 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.
Polymorphism	3 allelic variants of cecropia moth lysozyme have been found. The sequence shown is that of lysozyme 1.
Sequence similarities	Belongs to the glycosyl hydrolase 22 family.
Sequence caution	The sequence AAA29190.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA26542.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
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 – 19	19	By similarity
	Chain	20 – 139	120	Lysozyme		PRO_0000018506
Sites
	Active site	51	1	By similarity
	Active site	69	1	By similarity
Amino acid modifications
	Disulfide bond	25 ↔ 139		By similarity
	Disulfide bond	46 ↔ 129		By similarity
	Disulfide bond	81 ↔ 95		By similarity
	Disulfide bond	91 ↔ 109		By similarity
Natural variations
	Natural variant	34	1	L → R in lysozyme-2.
	Natural variant	85	1	T → S in lysozyme-2 and lysozyme-3.

Sequences

	Sequence		Length	Mass (Da)
	P05105 [UniParc]. Last modified May 1, 1992. Version 2. Checksum: E8AF5C2CE561F641	FASTA	139	15,877
	10 20 30 40 50 60 MTKYVILLAV LAFALHCDAK RFTRCGLVQE LRRLGFDETL MSNWVCLVEN ESGRFTDKIG 70 80 90 100 110 120 KVNKNGSRDY GLFQINDKYW CSKGTTPGKD CNVTCNQLLT DDISVAATCA KKIYKRHKFD 130 AWYGWKNHCQ HGLPDISDC

References

[1]	"Organization and expression of the immunoresponsive lysozyme gene in the giant silk moth, Hyalophora cecropia." Sun S.-C., Aasling B., Faye I. J. Biol. Chem. 266:6644-6649(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Amino acid and cDNA sequences of lysozyme from Hyalophora cecropia." Engstroem A., Xanthopoulos K.G., Boman H.G., Bennich H. EMBO J. 4:2119-2122(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 13-139.
[3]	"On the primary structures of lysozyme, cecropins and attacins from Hyalophora cecropia." Boman H.G., Faye I., von Hofsten P., Kockum K., Lee J.-Y., Xanthopoulos K.G., Bennich H., Engstroem A., Merrifield R.B., Andreu D. Dev. Comp. Immunol. 9:551-558(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 13-139.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M60914 Genomic DNA. Translation: AAA29189.1. X02765 mRNA. Translation: CAA26542.1. Different initiation. M34923 mRNA. Translation: AAA29190.1. Different initiation.
PIR	LZWK. A24649. A38744.
3D structure databases
ProteinModelPortal	P05105.
SMR	P05105. Positions 20-139.
ModBase	Search...
Protein family/group databases
CAZy	GH22. Glycoside Hydrolase Family 22.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR001916. Glyco_hydro_22. IPR019799. Glyco_hydro_22_CS. IPR000974. Glyco_hydro_22_lys. IPR023346. Lysozyme-like_dom. [Graphical view]
Pfam	PF00062. Lys. 1 hit. [Graphical view]
PRINTS	PR00137. LYSOZYME. PR00135. LYZLACT.
SMART	SM00263. LYZ1. 1 hit. [Graphical view]
SUPFAM	SSF53955. SSF53955. 1 hit.
PROSITE	PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit. PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LYS_HYACE

Accession

Primary (citable) accession number: P05105

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	May 1, 1992
Last modified:	April 3, 2013
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)