P81710 (LYSC2_HORSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 56.
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, spleen isozyme EC=3.2.1.17 Alternative name(s): 1,4-beta-N-acetylmuramidase C |
| Organism | Equus caballus (Horse) [Reference proteome] |
| Taxonomic identifier | 9796 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus › ![]() |
Protein attributes
| Sequence length | 33 AA. |
| Sequence status | Fragment. |
| 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 By similarity. |
| 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 By similarity. |
| 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 By similarity. |
| Sequence similarities | Belongs to the glycosyl hydrolase 22 family. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacteriumInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | lysozyme activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Sequences of two highly divergent canine type c lysozymes: implications for the evolutionary origins of the lysozyme/alpha-lactalbumin superfamily." Grobler J.A., Rao K.R., Pervaiz S., Brew K. Arch. Biochem. Biophys. 313:360-366(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Spleen. |
Cross-references
3D structure databases | |
|---|---|
| ProteinModelPortal | P81710. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| eggNOG | NOG85133. |
| HOGENOM | HOG000037357. |
| InParanoid | P81710. |
| OrthoDB | EOG48KRCP. |
Family and domain databases | |
| InterPro | IPR001916. Glyco_hydro_22. [Graphical view] |
| Pfam | PF00062. Lys. 1 hit. [Graphical view] |
| PROSITE | PS00128. LACTALBUMIN_LYSOZYME_1. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LYSC2_HORSE | ||||||||
| Accession | Primary (citable) accession number: P81710 | ||||||||
| 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
