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Q06283 (LYSC2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified August 10, 2010. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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-2
EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Gene names
Name:LYZ2
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length147 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.

Tissue specificity

Stomach-specific.

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 ruminant gastric lysozymes, which digest symbiotic bacteria coming with cud from the rumen, are much more resistant to inactivation by pepsin than are other lysozymes.

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Ontologies

Keywords
   Biological processDigestion
   DomainSignal
   Molecular functionAntimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
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

   Molecular functionlysozyme activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 147129Lysozyme C-2
PRO_0000018455

Sites

Active site531 By similarity
Active site711 By similarity

Amino acid modifications

Disulfide bond24 ↔ 145 Ref.2
Disulfide bond48 ↔ 133 Ref.2
Disulfide bond83 ↔ 99 Ref.2
Disulfide bond95 ↔ 113 Ref.2

Secondary structure

1 ............................ 147
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q06283-1 [UniParc].

Last modified January 1, 1999. Version 2.
Checksum: B0A38B9ECE1E66BE

FASTA14716,304
        10         20         30         40         50         60 
MKALVILGFL FLSVAVQGKV FERCELARTL KKLGLDGYKG VSLANWLCLT KWESSYNTKA 

        70         80         90        100        110        120 
TNYNPSSEST DYGIFQINSK WWCNDGKTPN AVDGCHVSCS ELMENDIAKA VACAKHIVSE 

       130        140 
QGITAWVAWK SHCRDHDVSS YVEGCTL

« Hide

References

[1]"Characterization of the cow stomach lysozyme genes: repetitive DNA and concerted evolution."
Irwin D.M., White R.T., Wilson A.C.
J. Mol. Evol. 37:355-366(1993) [PubMed: 8308905] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"X-ray crystallography and structural stability of digestive lysozyme from cow stomach."
Nonaka Y., Akieda D., Aizawa T., Watanabe N., Kamiya M., Kumaki Y., Mizuguchi M., Kikukawa T., Demura M., Kawano K.
FEBS J. 276:2192-2200(2009) [PubMed: 19348005] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 19-147, DISULFIDE BONDS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M95098 Unassigned DNA. Translation: AAC37311.1.
IPIIPI00718701.
PIRLZBO. C34277.
RefSeqNP_851342.1.
UniGeneBt.29367.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z2FX-ray1.50A19-147[»]
ProteinModelPortalQ06283.
ModBaseSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Genome annotation databases

EnsemblENSBTAT00000007924; ENSBTAP00000007924; ENSBTAG00000026088; Bos taurus. [Genome view]
GeneID280849.
KEGGbta:280849.

Organism-specific databases

CTD280849.

Phylogenomic databases

HOVERGENHBG052297.
InParanoidQ06283.

Enzyme and pathway databases

BRENDA3.2.1.17. 251.

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 nameLYSC2_BOVIN
AccessionPrimary (citable) accession number: Q06283
Entry history
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: January 1, 1999
Last modified: August 10, 2010
This is version 72 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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