P12066 (LYSC_AXIAX) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 78.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Lysozyme C-1/C-2 EC=3.2.1.17 Alternative name(s): 1,4-beta-N-acetylmuramidase C |
| Organism | Axis axis (Axis deer) (Chital) |
| Taxonomic identifier | 30531 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Cervidae › Cervinae › Axis![]() |
Protein attributes
| Sequence length | 129 AA. |
| Sequence status | Complete. |
| 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. |
| 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. The sequence of isozyme 1 is shown. |
| Sequence similarities | Belongs to the glycosyl hydrolase 22 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Digestion |
| 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 digestionInferred 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 129 | 129 | Lysozyme C-1/C-2 | PRO_0000208843 | |||||||
Sites | |||||||||||
| Active site | 35 | 1 | By similarity | ||||||||
| Active site | 53 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 6 ↔ 127 | By similarity | |||||||||
| Disulfide bond | 30 ↔ 115 | By similarity | |||||||||
| Disulfide bond | 65 ↔ 81 | By similarity | |||||||||
| Disulfide bond | 77 ↔ 95 | By similarity | |||||||||
Natural variations | |||||||||||
| Natural variant | 66 | 1 | D → N in isozyme 2. | ||||||||
| Natural variant | 88 | 1 | N → D in isozyme 2. | ||||||||
| Natural variant | 90 | 1 | D → A in isozyme 2. | ||||||||
| Natural variant | 94 | 1 | T → A in isozyme 2. | ||||||||
| Natural variant | 117 | 1 | G → H in isozyme 2. | ||||||||
Sequences
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References
| [1] | "Episodic evolution in the stomach lysozymes of ruminants." Jolles J., Jolles P., Bowman B.H., Prager E.M., Stewart C.-B., Wilson A.C. J. Mol. Evol. 28:528-535(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Stomach. |
| [2] | "Concerted evolution of ruminant stomach lysozymes. Characterization of lysozyme cDNA clones from sheep and deer." Irwin D.M., Wilson A.C. J. Biol. Chem. 265:4944-4952(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOZYMES 1 AND 2). |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M32499 mRNA. Translation: AAA30344.1. M32500 mRNA. Translation: AAA30345.1. |
| PIR | G35558. H35558. |
3D structure databases | |
| ProteinModelPortal | P12066. |
| SMR | P12066. Positions 1-129. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH22. Glycoside Hydrolase Family 22. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG052297. |
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 | LYSC_AXIAX | ||||||||
| Accession | Primary (citable) accession number: P12066 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
