P17607 (LYSC1_SHEEP)
Reviewed,
UniProtKB/Swiss-Prot
Last modified
August 10, 2010.
Version 78.
History...
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 | Ovis aries (Sheep) |
| Taxonomic identifier | 9940 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis |
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 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. |
| Subunit structure | Monomer. |
| Subcellular location | Secreted By similarity. |
| Tissue specificity | Expressed in stomach. |
| 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 1A/1B/1C is shown. |
| Sequence similarities | Belongs to the glycosyl hydrolase 22 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Digestion |
| Cellular component | Secreted |
| 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 cytolysisInferred from electronic annotation. Source: UniProtKB-KW defense response to bacteriumInferred from electronic annotation. Source: UniProtKB-KW digestionInferred 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 | By similarity | ||||||||
| Chain | 19 – 147 | 129 | Lysozyme C-1 | PRO_0000018488 | |||||||
Sites | |||||||||||
| Active site | 53 | 1 | By similarity | ||||||||
| Active site | 71 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 24 ↔ 145 | By similarity | |||||||||
| Disulfide bond | 48 ↔ 133 | By similarity | |||||||||
| Disulfide bond | 83 ↔ 99 | By similarity | |||||||||
| Disulfide bond | 95 ↔ 113 | By similarity | |||||||||
Natural variations | |||||||||||
| Natural variant | 32 | 1 | E → K in isozyme 3A and isozyme 4A/4B. | ||||||||
| Natural variant | 37 | 1 | G → D in isozyme 4A/4B. | ||||||||
| Natural variant | 55 | 1 | S → G in isozyme 3A. | ||||||||
| Natural variant | 101 | 1 | E → A in isozyme 2A, isozyme 3A and isozyme 4A/4B. | ||||||||
| Natural variant | 106 | 1 | N → D in isozyme 2A, isozyme 3A and isozyme 4A/4B. | ||||||||
| Natural variant | 108 | 1 | A → E in isozyme 2A, isozyme 3A and isozyme 4A/4B. | ||||||||
| Natural variant | 146 | 1 | S → T in isozyme 2A, isozyme 3A and isozyme 4A/4B. | ||||||||
Sequences
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References
| [1] | "Mosaic evolution of ruminant stomach lysozyme genes." Wen Y., Irwin D.M. Mol. Phylogenet. Evol. 13:474-482(1999) [PubMed: 10620405] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [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: 2318875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-147. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF170555 AF170554 Genomic DNA. Translation: AAD51636.1.M32492 mRNA. Translation: AAA31557.1. M32493 mRNA. Translation: AAA31558.1. M32494 mRNA. Translation: AAA31559.1. M32495 mRNA. Translation: AAA31560.1. M32496 mRNA. Translation: AAA31561.1. M32497 mRNA. Translation: AAA31562.1. M32498 mRNA. Translation: AAA31563.1. |
| PIR | D35558. E35558. F35558. |
| UniGene | Oar.378. Oar.379. Oar.380. |
3D structure databases | |
| ProteinModelPortal | P17607. |
| SMR | P17607. Positions 19-147. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH22. Glycoside Hydrolase Family 22. |
Phylogenomic databases | |
| HOVERGEN | HBG052297. |
Enzyme and pathway databases | |
| BRENDA | 3.2.1.17. 271. |
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_SHEEP | ||||||||
| Accession | Primary (citable) accession number: P17607 Secondary accession number(s): Q9TUN2 | ||||||||
| 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 |

Clusters with


