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P00705 (LYSC1_ANAPL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 79. 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 C-1

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase C
OrganismAnas platyrhynchos (Domestic duck) (Anas boschas) [Complete proteome]
Taxonomic identifier8839 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeAnseriformesAnatidaeAnas

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Subcellular location

Secreted.

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
   Cellular componentSecreted
   DomainSignal
   Molecular functionAntimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
   PTMDisulfide bond
   Technical termComplete proteome
Direct protein sequencing
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

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 1818 Ref.2 Ref.3
Chain19 – 147129Lysozyme C-1
PRO_0000018494

Sites

Active site531 By similarity
Active site701 By similarity

Amino acid modifications

Disulfide bond24 ↔ 145 Ref.4
Disulfide bond48 ↔ 133 Ref.4
Disulfide bond82 ↔ 98 Ref.4
Disulfide bond94 ↔ 112 Ref.4

Natural variations

Natural variant431L → I in DL3.
Natural variant551G → S in DL1 and lysozyme II.
Natural variant751Q → E in lysozyme II.
Natural variant891R → G in DL1 and lysozyme II.
Natural variant971P → R in DL3.

Sequences

Sequence LengthMass (Da)Tools
P00705 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: B0F2B6A9F7DA3978

FASTA14716,363
        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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS DL-1; DL-2 AND DL-3C.
Strain: Pekin breed.

Cross-references

Sequence databases

PIRLZDK. D92574.

3D structure databases

ProteinModelPortalP00705.
SMRP00705. Positions 19-147.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEP00705.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG052297.

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 nameLYSC1_ANAPL
AccessionPrimary (citable) accession number: P00705
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 22, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries