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Reviewed, UniProtKB/Swiss-Prot P37155 (LYSC_FELCA)

Last modified July 28, 2009. Version 51. 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:
    Lysozyme C
    EC=3.2.1.17
Alternative name(s):
    1,4-beta-N-acetylmuramidase C
Gene names
Name: LYZ
OrganismFelis catus (Cat) (Felis silvestris catus)
Taxonomic identifier9685 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis

Protein attributes

Sequence length20 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›20›20Lysozyme C
PRO_0000208850

Experimental info

Non-terminal residue201

Sequences

Sequence LengthMass (Da)Tools
P37155-1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: EB8824EA59425E13

FASTA202,314
        10         20 
KIFTKCELAR KLRAEGMDGF 

« Hide

References

[1]"Feline whey proteins: identification, isolation and initial characterization of alpha-lactalbumin, beta-lactoglobulin and lysozyme."
Halliday J.A., Bell K., McKenzie H.A., Shaw D.C.
Comp. Biochem. Physiol. 95B:773-779(1990) [PubMed: 2344734] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Milk.

Cross-references

Sequence databases

PIRA60525.

3D structure databases

HSSPHSSP built from PDB template 1EL1 based on UniProtKB P81708.
ModBaseSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Phylogenomic databases

HOVERGENP37155.

Enzyme and pathway databases

BRENDA3.2.1.17. 273949.

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLYSC_FELCA
AccessionPrimary (citable) accession number: P37155
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 28, 2009
This is version 51 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