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Reviewed, UniProtKB/Swiss-Prot Q05820 (LYSC2_RAT)

Last modified February 9, 2010. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative lysozyme C-2
    EC=3.2.1.17
Alternative name(s):
    1,4-beta-N-acetylmuramidase C
Gene names
Name: Lyz2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length148 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceUncertain.

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.

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.

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Caution

Could be the product of a pseudogene. Lyz1 has been shown to be expressed, but not Lyz2.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 148130Putative lysozyme C-2
PRO_0000018485

Sites

Active site531 By similarity
Active site711 By similarity

Amino acid modifications

Disulfide bond24 ↔ 146 By similarity
Disulfide bond48 ↔ 134 By similarity
Disulfide bond83 ↔ 99 By similarity
Disulfide bond95 ↔ 113 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q05820-1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 2855279E91CCC083

FASTA14816,618
        10         20         30         40         50         60 
MKALLVLGFL LLSASVQAKV FKHCELARIL RSSALAGYRG VSLENWMCMA QHESNFDTEA 

        70         80         90        100        110        120 
INYNSTDQST DYGIFQINSR YWCNDGKTPR AVNACGIPCS ALLQDDITQA IQCAKRVVRD 

       130        140 
PQGIRAWVAW QRHCQNRDLS GYIRNCGV 

« Hide

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: 8081549] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L12458 Genomic DNA. Translation: AAA41552.1.
IPIIPI00193370.
PIRB40729.
UniGeneRn.162941

3D structure databases

SMRQ05820. Positions 19-148.
ModBaseSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEQ05820.

Phylogenomic databases

HOVERGENQ05820.

Enzyme and pathway databases

BRENDA3.2.1.17. 248.

Gene expression databases

GenevestigatorQ05820.

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLYSC2_RAT
AccessionPrimary (citable) accession number: Q05820
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: February 9, 2010
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents