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Protein

Lysozyme C-1

Gene

Lyz1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.PROSITE-ProRule annotation1 Publication

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei53 – 531PROSITE-ProRule annotation
Active sitei71 – 711PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • cytolysis Source: UniProtKB-KW
  • defense response to Gram-negative bacterium Source: UniProtKB
  • defense response to Gram-positive bacterium Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C-1 (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Lysozyme C type P
Gene namesi
Name:Lyz1
Synonyms:Lzp-s
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:96902. Lyz1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818By similarityAdd
BLAST
Chaini19 – 148130Lysozyme C-1PRO_0000018473Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 146PROSITE-ProRule annotation
Disulfide bondi48 ↔ 134PROSITE-ProRule annotation
Disulfide bondi83 ↔ 99PROSITE-ProRule annotation
Disulfide bondi95 ↔ 113PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP17897.
PaxDbiP17897.
PRIDEiP17897.

PTM databases

PhosphoSiteiP17897.

Expressioni

Tissue specificityi

Expressed strongly only in small intestine.

Gene expression databases

BgeeiP17897.
CleanExiMM_LYZ1.
GenevisibleiP17897. MM.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi201260. 1 interaction.
IntActiP17897. 1 interaction.
STRINGi10090.ENSMUSP00000089800.

Structurei

3D structure databases

ProteinModelPortaliP17897.
SMRiP17897. Positions 19-148.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 22 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG85133.
GeneTreeiENSGT00550000074398.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
InParanoidiP17897.
KOiK13915.
OMAiLYWCQAD.
OrthoDBiEOG7BW0M5.
PhylomeDBiP17897.
TreeFamiTF324882.

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
IPR030056. Lysozyme_C.
[Graphical view]
PANTHERiPTHR11407:SF22. PTHR11407:SF22. 1 hit.
PfamiPF00062. Lys. 1 hit.
[Graphical view]
PRINTSiPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTiSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17897-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKALLTLGLL LLSVTAQAKV YNRCELARIL KRNGMDGYRG VKLADWVCLA
60 70 80 90 100
QHESNYNTRA TNYNRGDRST DYGIFQINSR YWCNDGKTPR SKNACGINCS
110 120 130 140
ALLQDDITAA IQCAKRVVRD PQGIRAWVAW RTQCQNRDLS QYIRNCGV
Length:148
Mass (Da):16,794
Last modified:November 1, 1990 - v1
Checksum:iD849A9D02A49EDE6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51547 mRNA. Translation: CAA35922.1.
BC061129 mRNA. Translation: AAH61129.1.
CCDSiCCDS48695.1.
PIRiS09229.
RefSeqiNP_038618.1. NM_013590.4.
UniGeneiMm.177539.

Genome annotation databases

EnsembliENSMUST00000092162; ENSMUSP00000089800; ENSMUSG00000069515.
GeneIDi17110.
KEGGimmu:17110.
UCSCiuc007hdc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51547 mRNA. Translation: CAA35922.1.
BC061129 mRNA. Translation: AAH61129.1.
CCDSiCCDS48695.1.
PIRiS09229.
RefSeqiNP_038618.1. NM_013590.4.
UniGeneiMm.177539.

3D structure databases

ProteinModelPortaliP17897.
SMRiP17897. Positions 19-148.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201260. 1 interaction.
IntActiP17897. 1 interaction.
STRINGi10090.ENSMUSP00000089800.

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

PTM databases

PhosphoSiteiP17897.

Proteomic databases

MaxQBiP17897.
PaxDbiP17897.
PRIDEiP17897.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000092162; ENSMUSP00000089800; ENSMUSG00000069515.
GeneIDi17110.
KEGGimmu:17110.
UCSCiuc007hdc.2. mouse.

Organism-specific databases

CTDi17110.
MGIiMGI:96902. Lyz1.

Phylogenomic databases

eggNOGiNOG85133.
GeneTreeiENSGT00550000074398.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
InParanoidiP17897.
KOiK13915.
OMAiLYWCQAD.
OrthoDBiEOG7BW0M5.
PhylomeDBiP17897.
TreeFamiTF324882.

Miscellaneous databases

NextBioi291254.
PROiP17897.
SOURCEiSearch...

Gene expression databases

BgeeiP17897.
CleanExiMM_LYZ1.
GenevisibleiP17897. MM.

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
IPR030056. Lysozyme_C.
[Graphical view]
PANTHERiPTHR11407:SF22. PTHR11407:SF22. 1 hit.
PfamiPF00062. Lys. 1 hit.
[Graphical view]
PRINTSiPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTiSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiLYZ1_MOUSE
AccessioniPrimary (citable) accession number: P17897
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: June 24, 2015
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.