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P79158 (LYSC_CALJA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 75. 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
Synonyms:LZM
OrganismCallithrix jacchus (White-tufted-ear marmoset) [Reference proteome]
Taxonomic identifier9483 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniPlatyrrhiniCebidaeCallitrichinaeCallithrix

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.

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
PRO_0000018459

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
P79158 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: C79BB37557B1E951

FASTA14816,602
        10         20         30         40         50         60 
MKVLIILGLV LLSVMVQGKV FERCELARTL KRFGLDGYRG ISLANWMCLA KWESDYNTRA 

        70         80         90        100        110        120 
TNYNPGDQST DYGIFQINSH YWCNNGRTPG AVNACHISCN ALLQDDITEA VACAKRVVRD 

       130        140 
PQGIRAWVAW KAHCQNRDVS QYVQGCGV 

« Hide

References

[1]"Episodic adaptive evolution of primate lysozymes."
Messier W., Stewart C.B.
Nature 385:151-154(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Blood.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U76923 mRNA. Translation: AAB41203.1.
RefSeqXP_002752792.1. XM_002752746.2.

3D structure databases

ProteinModelPortalP79158.
SMRP79158. Positions 19-148.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEP79158.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCJAT00000003379; ENSCJAP00000003201; ENSCJAG00000001788.
GeneID100393686.

Organism-specific databases

CTD4069.

Phylogenomic databases

HOGENOMHOG000037357.
HOVERGENHBG052297.
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 nameLYSC_CALJA
AccessionPrimary (citable) accession number: P79158
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: February 19, 2014
This is version 75 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