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P17607 (LYSC1_SHEEP) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. 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
OrganismOvis aries (Sheep) [Reference proteome]
Taxonomic identifier9940 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis

Protein attributes

Sequence length147 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.

Subcellular location

Secreted By similarity.

Tissue specificity

Expressed in stomach.

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 1A/1B/1C is shown.

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Ontologies

Keywords
   Biological processDigestion
   Cellular componentSecreted
   DomainSignal
   Molecular functionAntimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 147129Lysozyme C-1
PRO_0000018488

Sites

Active site531 By similarity
Active site711 By similarity

Amino acid modifications

Disulfide bond24 ↔ 145 By similarity
Disulfide bond48 ↔ 133 By similarity
Disulfide bond83 ↔ 99 By similarity
Disulfide bond95 ↔ 113 By similarity

Natural variations

Natural variant321E → K in isozyme 3A and isozyme 4A/4B.
Natural variant371G → D in isozyme 4A/4B.
Natural variant551S → G in isozyme 3A.
Natural variant1011E → A in isozyme 2A, isozyme 3A and isozyme 4A/4B.
Natural variant1061N → D in isozyme 2A, isozyme 3A and isozyme 4A/4B.
Natural variant1081A → E in isozyme 2A, isozyme 3A and isozyme 4A/4B.
Natural variant1461S → T in isozyme 2A, isozyme 3A and isozyme 4A/4B.

Sequences

Sequence LengthMass (Da)Tools
P17607 [UniParc].

Last modified January 27, 2003. Version 2.
Checksum: 065D72BC42B0A6E0

FASTA14716,195
        10         20         30         40         50         60 
MKALIILGLL CLSVAVQGKV FERCELARTL KELGLDGYKG VSLANWLCLT KWESSYNTKA 

        70         80         90        100        110        120 
TNYNPGSEST DYGIFQINSK WWCNDGKTPN AVDGCHVSCS ELMENNIAKA VACAKHIVSE 

       130        140 
QGITAWVAWK SHCRDHDVSS YVEGCSL 

« Hide

References

[1]"Mosaic evolution of ruminant stomach lysozyme genes."
Wen Y., Irwin D.M.
Mol. Phylogenet. Evol. 13:474-482(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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] OF 19-147.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF170555 expand/collapse EMBL AC list , AF170552, AF170553, AF170554 Genomic DNA. Translation: AAD51636.1.
M32492 mRNA. Translation: AAA31557.1.
M32493 mRNA. Translation: AAA31558.1.
M32494 mRNA. Translation: AAA31559.1.
M32495 mRNA. Translation: AAA31560.1.
M32496 mRNA. Translation: AAA31561.1.
M32497 mRNA. Translation: AAA31562.1.
M32498 mRNA. Translation: AAA31563.1.
PIRD35558.
E35558.
F35558.
UniGeneOar.378.
Oar.379.
Oar.380.

3D structure databases

ProteinModelPortalP17607.
SMRP17607. Positions 19-147.
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 nameLYSC1_SHEEP
AccessionPrimary (citable) accession number: P17607
Secondary accession number(s): Q9TUN2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 27, 2003
Last modified: July 9, 2014
This is version 84 of the entry and version 2 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