Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P00697 (LYSC1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Gene names
Name:Lyz1
Synonyms:Lyz
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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. 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

Secreted.

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

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionAntimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
Milk protein
   PTMDisulfide bond
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell wall macromolecule catabolic process

Inferred from electronic annotation. Source: InterPro

cytolysis

Inferred from electronic annotation. Source: UniProtKB-KW

defense response to Gram-negative bacterium

Inferred from mutant phenotype PubMed 2840982. Source: RGD

defense response to Gram-positive bacterium

Inferred from mutant phenotype PubMed 2840982. Source: RGD

   Cellular_componentGolgi cis cisterna

Inferred from direct assay PubMed 9208328. Source: RGD

Golgi stack

Inferred from direct assay PubMed 9208328. Source: RGD

cytoplasm

Inferred from direct assay PubMed 9208328. Source: RGD

endoplasmic reticulum lumen

Inferred from direct assay PubMed 9208328. Source: RGD

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

microvillus

Inferred from direct assay PubMed 9208328. Source: RGD

rough endoplasmic reticulum lumen

Inferred from direct assay PubMed 9208328. Source: RGD

secretory granule

Inferred from direct assay PubMed 9208328. Source: RGD

trans-Golgi network transport vesicle

Inferred from direct assay PubMed 9208328. Source: RGD

   Molecular_functionhydrolase activity, acting on glycosyl bonds

Inferred from mutant phenotype PubMed 2840982. Source: RGD

lysozyme activity

Inferred from direct assay PubMed 12965127. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.2
Chain19 – 148130Lysozyme C-1
PRO_0000018484

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

Experimental info

Sequence conflict201I → T AA sequence Ref.2
Sequence conflict641N → D AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P00697 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: 8E6E986539BD3EEE

FASTA14816,729
        10         20         30         40         50         60 
MKALLVLGFL LLSASVQAKI YERCQFARTL KRNGMSGYYG VSLADWVCLA QHESNYNTQA 

        70         80         90        100        110        120 
RNYNPGDQST DYGIFQINSR YWCNDGKTPR AKNACGIPCS ALLQDDITQA IQCAKRVVRD 

       130        140 
PQGIRAWVAW QRHCKNRDLS 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] [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.
PIRLZRT. A40729.
UniGeneRn.2283.

3D structure databases

ProteinModelPortalP00697.
SMRP00697. Positions 19-148.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000007747.

Chemistry

BindingDBP00697.
ChEMBLCHEMBL2297.

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

PTM databases

PhosphoSiteP00697.

Proteomic databases

PaxDbP00697.
PRIDEP00697.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:3026. rat.

Organism-specific databases

RGD3026. Lyz.

Phylogenomic databases

eggNOGNOG85133.
HOGENOMHOG000037357.
HOVERGENHBG052297.
InParanoidP00697.
PhylomeDBP00697.

Gene expression databases

GenevestigatorP00697.

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...

Entry information

Entry nameLYSC1_RAT
AccessionPrimary (citable) accession number: P00697
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1994
Last modified: April 16, 2014
This is version 113 of the entry and version 2 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries