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P17897 (LYZ1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysozyme C-1

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Lysozyme C type P
Gene names
Name:Lyz1
Synonyms:Lzp-s
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length148 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Lyz1 is active against a range of Gram-postive and Gram-negative bacteria. Less effective than Lyz2 in killing Gram-negative bacteria. Lyz1 and Lyz2 are equally effective in killing Gram-positive bacteria. Ref.5

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.

Tissue specificity

Expressed strongly only in small intestine.

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

Signal peptide1 – 1818 By similarity
Chain19 – 148130Lysozyme C-1
PRO_0000018473

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
P17897 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: D849A9D02A49EDE6

FASTA14816,794
        10         20         30         40         50         60 
MKALLTLGLL LLSVTAQAKV YNRCELARIL KRNGMDGYRG VKLADWVCLA QHESNYNTRA 

        70         80         90        100        110        120 
TNYNRGDRST DYGIFQINSR YWCNDGKTPR SKNACGINCS ALLQDDITAA IQCAKRVVRD 

       130        140 
PQGIRAWVAW RTQCQNRDLS QYIRNCGV 

« Hide

References

« Hide 'large scale' references
[1]"Recent origin of the P lysozyme gene in mice."
Cortopassi G.A., Wilson A.C.
Nucleic Acids Res. 18:1911-1911(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
Tissue: Small intestine.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart and Lung.
[3]"Repetitive sequence involvement in the duplication and divergence of mouse lysozyme genes."
Cross M., Renkawitz R.
EMBO J. 9:1283-1288(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-45.
[4]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 69-80, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[5]"Comparison of the microbicidal and muramidase activities of mouse lysozyme M and P."
Markart P., Faust N., Graf T., Na C.-L., Weaver T.E., Akinbi H.T.
Biochem. J. 380:385-392(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X51547 mRNA. Translation: CAA35922.1.
BC061129 mRNA. Translation: AAH61129.1.
PIRS09229.
RefSeqNP_038618.1. NM_013590.4.
UniGeneMm.177539.

3D structure databases

ProteinModelPortalP17897.
SMRP17897. Positions 19-148.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201260. 1 interaction.
IntActP17897. 1 interaction.
STRING10090.ENSMUSP00000089800.

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

PTM databases

PhosphoSiteP17897.

Proteomic databases

PaxDbP17897.
PRIDEP17897.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000092162; ENSMUSP00000089800; ENSMUSG00000069515.
GeneID17110.
KEGGmmu:17110.
UCSCuc007hdc.2. mouse.

Organism-specific databases

CTD17110.
MGIMGI:96902. Lyz1.

Phylogenomic databases

eggNOGNOG85133.
GeneTreeENSGT00550000074398.
HOGENOMHOG000037357.
HOVERGENHBG052297.
InParanoidP17897.
KOK13915.
OMAWESSFNT.
OrthoDBEOG7BW0M5.
PhylomeDBP17897.
TreeFamTF324882.

Gene expression databases

BgeeP17897.
CleanExMM_LYZ1.
GenevestigatorP17897.

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio291254.
PROP17897.
SOURCESearch...

Entry information

Entry nameLYZ1_MOUSE
AccessionPrimary (citable) accession number: P17897
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: April 16, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries