P00697 (LYSC1_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 106.
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 EC=3.2.1.17 Alternative name(s): 1,4-beta-N-acetylmuramidase C | ||||
| Gene names |
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| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 148 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. In the intestine they may also have a digestive function. |
| 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 | |
| Tissue specificity | Expressed in lung, small intestine and spleen. |
| 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. Rat has two lysozymes, type 1 and type 2 of which only type 1 is expressed; type 2 being probably a pseudogene. |
| Sequence similarities | Belongs to the glycosyl hydrolase 22 family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 18 | 18 | Ref.2 | ||||||||
| Chain | 19 – 148 | 130 | Lysozyme C-1 | PRO_0000018484 | |||||||
Sites | |||||||||||
| Active site | 53 | 1 | By similarity | ||||||||
| Active site | 71 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 24 ↔ 146 | By similarity | |||||||||
| Disulfide bond | 48 ↔ 134 | By similarity | |||||||||
| Disulfide bond | 83 ↔ 99 | By similarity | |||||||||
| Disulfide bond | 95 ↔ 113 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 20 | 1 | I → T AA sequence Ref.2 | ||||||||
| Sequence conflict | 64 | 1 | N → D AA sequence Ref.2 | ||||||||
Sequences
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References
| [1] | "Evolution of rodent lysozymes: isolation and sequence of the rat lysozyme genes." Yeh T.C., Wilson A.C., Irwin D.M. Mol. Phylogenet. Evol. 2:65-75(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Sprague-Dawley. |
| [2] | "Primary structure of rat lysozyme." White T.J., Mross G.A., Osserman E.F., Wilson A.C. Biochemistry 16:1430-1436(1977) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-148. Strain: Wistar. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L12459 Genomic DNA. Translation: AAA41551.1. |
| IPI | IPI00211927. |
| PIR | LZRT. A40729. |
| UniGene | Rn.2283. |
3D structure databases | |
| ProteinModelPortal | P00697. |
| SMR | P00697. Positions 19-148. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10116.ENSRNOP00000007747. |
Protein family/group databases | |
| CAZy | GH22. Glycoside Hydrolase Family 22. |
PTM databases | |
| PhosphoSite | P00697. |
Proteomic databases | |
| PaxDb | P00697. |
| PRIDE | P00697. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| UCSC | RGD:3026. rat. |
Organism-specific databases | |
| RGD | 3026. Lyz. |
Phylogenomic databases | |
| eggNOG | NOG85133. |
| HOGENOM | HOG000037357. |
| HOVERGEN | HBG052297. |
| InParanoid | P00697. |
Gene expression databases | |
| ArrayExpress | P00697. |
| Genevestigator | P00697. |
| GermOnline | ENSRNOG00000005825. Rattus norvegicus. |
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... |
Other | |
| BindingDB | P00697. |
| ChEMBL | CHEMBL2297. |
Entry information
| Entry name | LYSC1_RAT | ||||||||
| Accession | Primary (citable) accession number: P00697 | ||||||||
| 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
