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P30201 (LYSC_MACMU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. 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

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Gene names
Name:LYZ
OrganismMacaca mulatta (Rhesus macaque) [Reference proteome]
Taxonomic identifier9544 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Protein attributes

Sequence length148 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

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
   Cellular componentSecreted
   DomainSignal
   Molecular functionAntimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
Milk protein
   PTMDisulfide bond
   Technical termComplete proteome
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

   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 By similarity
Chain19 – 148130Lysozyme C
PRO_0000018470

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
P30201 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: AF4EE1B3A33F4765

FASTA14816,408
        10         20         30         40         50         60 
MKAVIILGLV LLSVTVQGKI FERCELARTL KRLGLDGYRG ISLANWVCLA KWESNYNTQA 

        70         80         90        100        110        120 
TNYNPGDQST DYGIFQINSH YWCNNGKTPG AVNACHISCN ALLQDNIADA VTCAKRVVSD 

       130        140 
PQGIRAWVAW RNHCQNRDVS QYVQGCGV 

« Hide

References

[1]"Stomach lysozyme gene of the langur monkey: tests for convergence and positive selection."
Swanson K.W., Irwin D.M., Wilson A.C.
J. Mol. Evol. 33:418-425(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary gland.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60236 mRNA. Translation: CAA42796.1.
RefSeqNP_001095203.1. NM_001101733.1.
UniGeneMmu.1820.

3D structure databases

ProteinModelPortalP30201.
SMRP30201. Positions 19-148.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9544.ENSMMUP00000011770.

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMMUT00000012553; ENSMMUP00000011770; ENSMMUG00000008987.
GeneID718361.
KEGGmcc:718361.

Organism-specific databases

CTD4069.

Phylogenomic databases

eggNOGNOG85133.
GeneTreeENSGT00550000074398.
HOGENOMHOG000037357.
HOVERGENHBG052297.
InParanoidP30201.
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...

Other

NextBio19979000.

Entry information

Entry nameLYSC_MACMU
AccessionPrimary (citable) accession number: P30201
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 95 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries