P00705 (LYSC1_ANAPL)
Reviewed,
UniProtKB/Swiss-Prot
Last modified
August 10, 2010.
Version 73.
History...
Clusters with 
Names and origin
| Protein names | Recommended name: Lysozyme C-1 EC=3.2.1.17 Alternative name(s): 1,4-beta-N-acetylmuramidase C |
| 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 | 147 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| 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. |
| Subcellular location | |
| 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 component | Secreted |
| Domain | Signal |
| Molecular function | Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase |
| PTM | Disulfide bond |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro cytolysisInferred from electronic annotation. Source: UniProtKB-KW defense response to bacteriumInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| 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 | Ref.2 Ref.3 | ||||||||
| Chain | 19 – 147 | 129 | Lysozyme C-1 | PRO_0000018494 | |||||||
Sites | |||||||||||
| Active site | 53 | 1 | By similarity | ||||||||
| Active site | 70 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 24 ↔ 145 | Ref.4 | |||||||||
| Disulfide bond | 48 ↔ 133 | Ref.4 | |||||||||
| Disulfide bond | 82 ↔ 98 | Ref.4 | |||||||||
| Disulfide bond | 94 ↔ 112 | Ref.4 | |||||||||
Natural variations | |||||||||||
| Natural variant | 43 | 1 | L → I in DL3. | ||||||||
| Natural variant | 55 | 1 | G → S in DL1 and lysozyme II. | ||||||||
| Natural variant | 75 | 1 | Q → E in lysozyme II. | ||||||||
| Natural variant | 89 | 1 | R → G in DL1 and lysozyme II. | ||||||||
| Natural variant | 97 | 1 | P → R in DL3. | ||||||||
Sequences
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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: 3511061] [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: 7068576] [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: 5138644] [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: 4580844] [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: 5542021] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS DL-1; DL-2 AND DL-3C. Strain: Pekin breed. |
Cross-references
Sequence databases | |
|---|---|
| PIR | LZDK. D92574. |
3D structure databases | |
| ProteinModelPortal | P00705. |
| SMR | P00705. Positions 19-147. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH22. Glycoside Hydrolase Family 22. |
Proteomic databases | |
| PRIDE | P00705. |
Phylogenomic databases | |
| HOVERGEN | HBG052297. |
Enzyme and pathway databases | |
| BRENDA | 3.2.1.17. 3217. |
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 | LYSC1_ANAPL | ||||||||
| Accession | Primary (citable) accession number: P00705 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |
