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P12068 (LYSC2_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. 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-2

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase C
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length146 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.

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.

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.

Ontologies

Keywords
   Biological processDigestion
   Cellular componentSecreted
   DomainSignal
   Molecular functionAntimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
   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 bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

digestion

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionlysozyme activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.2
Chain19 – 146128Lysozyme C-2
PRO_0000018479

Sites

Active site531 By similarity
Active site691 By similarity

Amino acid modifications

Disulfide bond24 ↔ 144 By similarity
Disulfide bond48 ↔ 132 By similarity
Disulfide bond81 ↔ 97 By similarity
Disulfide bond93 ↔ 111 By similarity

Sequences

Sequence LengthMass (Da)Tools
P12068 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: C2986F5CAAAF49F4

FASTA14616,484
        10         20         30         40         50         60 
MKTLLVLALL LLSVSVQAKV YDRCEFARIL KKSGMDGYRG VSLANWVCLA KWESDFNTKA 

        70         80         90        100        110        120 
INHNVGSTDY GIFQINSRYW CNDGKTPKAV NACHISCKVL LDDDLSQDIE CAKRVVRDPL 

       130        140 
GVKAWVAWRA HCQNKDVSQY IRGCKL 

« Hide

References

[1]"Evolution of stomach lysozyme: the pig lysozyme gene."
Yu M., Irwin D.M.
Mol. Phylogenet. Evol. 5:298-308(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Episodic evolution in the stomach lysozymes of ruminants."
Jolles J., Jolles P., Bowman B.H., Prager E.M., Stewart C.-B., Wilson A.C.
J. Mol. Evol. 28:528-535(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-146.
Tissue: Stomach.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U28757 Genomic DNA. Translation: AAB16862.1.
RefSeqNP_999557.2. NM_214392.2.
UniGeneSsc.670.

3D structure databases

ProteinModelPortalP12068.
SMRP12068. Positions 19-144.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000000530; ENSSSCP00000000522; ENSSSCG00000000492.
GeneID100157211.
KEGGssc:100157211.

Organism-specific databases

CTD4069.

Phylogenomic databases

GeneTreeENSGT00550000074398.
HOVERGENHBG052297.
KOK13915.
OMALQDNIAD.
OrthoDBEOG7BW0M5.
TreeFamTF324882.

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 nameLYSC2_PIG
AccessionPrimary (citable) accession number: P12068
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 94 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