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P05105 (LYS_HYACE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysozyme

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase
OrganismHyalophora cecropia (Cecropia moth)
Taxonomic identifier7123 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaSaturniidaeSaturniinaeAttaciniHyalophora

Protein attributes

Sequence length139 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 diversityPolymorphism
   DomainSignal
   Molecular functionAntimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological_processcell 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_functionlysozyme activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 139120Lysozyme
PRO_0000018506

Sites

Active site511 By similarity
Active site691 By similarity

Amino acid modifications

Disulfide bond25 ↔ 139 By similarity
Disulfide bond46 ↔ 129 By similarity
Disulfide bond81 ↔ 95 By similarity
Disulfide bond91 ↔ 109 By similarity

Natural variations

Natural variant341L → R in lysozyme-2.
Natural variant851T → S in lysozyme-2 and lysozyme-3.

Sequences

Sequence LengthMass (Da)Tools
P05105 [UniParc].

Last modified May 1, 1992. Version 2.
Checksum: E8AF5C2CE561F641

FASTA13915,877
        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 

« Hide

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.
PIRLZWK. A24649.
A38744.

3D structure databases

ProteinModelPortalP05105.
SMRP05105. Positions 20-139.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLYS_HYACE
AccessionPrimary (citable) accession number: P05105
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: May 1, 1992
Last modified: October 16, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries