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P12067 (LYSC1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified August 10, 2010. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
Customize displayNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

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)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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

Keywords
   Biological processDigestion
   Cellular componentSecreted
   Molecular functionAntimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
   PTMDisulfide bond
   Technical termDirect protein sequencing
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

digestion

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: EC

Complete GO annotation...

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
P12067-1 [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: 2504928] [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...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Genome annotation databases

EnsemblENSSSCT00000000530; ENSSSCP00000000522; ENSSSCG00000000492; Sus scrofa. [Genome view]

Phylogenomic databases

HOVERGENHBG052297.

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 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: August 10, 2010
This is version 69 of the entry and version 1 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·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents