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P12067 (LYSC1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 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

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 length128 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.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 128128Lysozyme C-1
PRO_0000208853

Sites

Active site351 By similarity
Active site511 By similarity

Amino acid modifications

Disulfide bond6 ↔ 126 By similarity
Disulfide bond30 ↔ 114 By similarity
Disulfide bond63 ↔ 79 By similarity
Disulfide bond75 ↔ 93 By similarity

Sequences

Sequence LengthMass (Da)Tools
P12067 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: FD169D39228DF774

FASTA12814,668
        10         20         30         40         50         60 
KVYDRCEFAR ILKKSGMDGY RGVSLANWVC LAKWESDFNT KAINRNVGST DYGIFQINSR 

        70         80         90        100        110        120 
YWCNDGKTPK AVNACHISCK VLLDDDLSQD IECAKRVVRD PQGIKAWVAW RTHCQNKDVS 


QYIRGCKL 

« 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]Echetebu Z.O., Nevils M., Roberts R.M., Trout W.E.
Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-128.
Tissue: Spleen.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L14853 mRNA. Translation: AAA74656.1.
UniGeneSsc.670.

3D structure databases

ProteinModelPortalP12067.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG85133.
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 nameLYSC1_PIG
AccessionPrimary (citable) accession number: P12067
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 13, 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