Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P12069 (LYSC3_PIG)

Last modified October 13, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Lysozyme C-3
    EC=3.2.1.17
Alternative name(s):
    1,4-beta-N-acetylmuramidase C
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length148 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.

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 Ref.2
Chain19 – 148130Lysozyme C-3
PRO_0000018480

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
P12069-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 76AA67BFABBD64E6

FASTA14816,711
        10         20         30         40         50         60 
MKTLLVLALL LLSVSVQAKV YDRCEFARIL KKSGMDGYRG VSLANWVCLA KWESNFNTKA 

        70         80         90        100        110        120 
TNYNPGSQST DYGIFQINSR YWCNDGKTPK AVNACHISCK VLLDDDLSQD IECAKRVVRD 

       130        140 
PQGIKAWVAW KAHCQNKDVS QYIRGCKL 

« Hide

References

[1]Echetebu Z.O., Nevils M., Bixby J.A., Roberts R.M., Trout W.E.
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 2504928] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-148.
Tissue: Stomach.

Cross-references

Sequence databases

U44435 mRNA. Translation: AAA86644.1.
PIRS10047.
RefSeqNP_999557.1.
UniGeneSsc.53737

3D structure databases

HSSPHSSP built from PDB template 1IVM based on UniProtKB P08905.
ModBaseSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Genome annotation databases

GeneID100157211.
KEGGssc:100157211.

Phylogenomic databases

HOVERGENP12069.

Enzyme and pathway databases

BRENDA3.2.1.17. 249.

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLYSC3_PIG
AccessionPrimary (citable) accession number: P12069
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 1, 1997
Last modified: October 13, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents