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P12066 (LYSC_AXIAX) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 79. 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/C-2

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase C
OrganismAxis axis (Axis deer) (Chital)
Taxonomic identifier30531 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraCervidaeCervinaeAxis

Protein attributes

Sequence length129 AA.
Sequence statusComplete.
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.

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.

The sequence of isozyme 1 is shown.

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 129129Lysozyme C-1/C-2
PRO_0000208843

Sites

Active site351 By similarity
Active site531 By similarity

Amino acid modifications

Disulfide bond6 ↔ 127 By similarity
Disulfide bond30 ↔ 115 By similarity
Disulfide bond65 ↔ 81 By similarity
Disulfide bond77 ↔ 95 By similarity

Natural variations

Natural variant661D → N in isozyme 2.
Natural variant881N → D in isozyme 2.
Natural variant901D → A in isozyme 2.
Natural variant941T → A in isozyme 2.
Natural variant1171G → H in isozyme 2.

Sequences

Sequence LengthMass (Da)Tools
P12066 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: A0AA48E69C2EB383

FASTA12914,446
        10         20         30         40         50         60 
KVFERCELAR TLKELGLDGY KGVSLANWLC LTKWESSYNT KATNYNPGSE STDYGIFQIN 

        70         80         90        100        110        120 
SKWWCDDGKT PNAVDGCHVA CSELMENNID KAVTCAKQIV REQGITAWVA WKSHCRGHDV 


SSYVEGCTL 

« Hide

References

[1]"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.
Tissue: Stomach.
[2]"Concerted evolution of ruminant stomach lysozymes. Characterization of lysozyme cDNA clones from sheep and deer."
Irwin D.M., Wilson A.C.
J. Biol. Chem. 265:4944-4952(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOZYMES 1 AND 2).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M32499 mRNA. Translation: AAA30344.1.
M32500 mRNA. Translation: AAA30345.1.
PIRG35558.
H35558.

3D structure databases

ProteinModelPortalP12066.
SMRP12066. Positions 1-129.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG052297.

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_AXIAX
AccessionPrimary (citable) accession number: P12066
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: October 16, 2013
This is version 79 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