[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2738070 [NCBI, ExPASy, EBI, Israel, Japan] Irwin D.M., Wilson A.C.; "Multiple cDNA sequences and the evolution of bovine stomach lysozyme."; J. Biol. Chem. 264:11387-11393(1989).
[2]	PROTEIN SEQUENCE OF 19-147 (2B). PubMed=6470012 [NCBI, ExPASy, EBI, Israel, Japan] Jolles P., Schoentgen F., Jolles J., Dobson D.E., Prager E.M., Wilson A.C.; "Stomach lysozymes of ruminants. II. Amino acid sequence of cow lysozyme 2 and immunological comparisons with other lysozymes."; J. Biol. Chem. 259:11617-11625(1984).
[3]	SEQUENCE REVISION TO 116 (2B). DOI=10.1007/BF02602933; PubMed=2504928 [NCBI, ExPASy, EBI, Israel, Japan] Jolles J., Jolles P., Bowman B.H., Prager E.M., Stewart C.-B., Wilson A.C.; "Episodic evolution in the stomach lysozymes of ruminants."; J. Mol. Evol. 28:528-535(1989).

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: 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.
MISCELLANEOUS: 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.
MISCELLANEOUS: Three non-allelic lysozymes C are present in the gastric mucosa of cattle.
MISCELLANEOUS: The sequence of isozyme 2B is shown.
SIMILARITY: Belongs to the glycosyl hydrolase 22 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M26246; AAA30627.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M26245; AAA30626.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M26242; AAA30632.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M26241; AAA30628.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M26243; AAA30629.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M26244; AAA30630.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M26240; AAA30631.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001073808.1; -.
NP_776529.1; -.

UniGene

Bt.29367

3D structure databases

HSSP

P00695; 1LZ6. [HSSP ENTRY / PDB]

ModBase

P04421.

Ontologies

GO:0019835;	Biological process: cytolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0042742;	Biological process: defense response to bacterium (inferred from electronic annotation from UniProtKB-KW).
GO:0007586;	Biological process: digestion (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001916; Glyco_hydro_22.
IPR000974; Glyco_hydro_22_lys.
Graphical view of domain structure.

Pfam

PF00062; Lys; 1.
Pfam graphical view of domain structure.

PRINTS

PR00137; LYSOZYME.
PR00135; LYZLACT.

SMART

SM00263; LYZ1; 1.
SMART graphical view of domain structure.

PROSITE

PS00128; LACTALBUMIN_LYSOZYME_1; 1.
PS51348; LACTALBUMIN_LYSOZYME_2; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSBTAG00000026088; Bos taurus. [Contig view]

GeneID

281289; -.
781349; -.

KEGG

bta:281289; -.
bta:781349; -.

Phylogenomic databases

HOVERGEN

P04421; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Antimicrobial; Bacteriolytic enzyme; Digestion; Direct protein sequencing; Glycosidase; Hydrolase; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`
`CHAIN`	`19 147`	`129`	`Lysozyme C.`	`PRO_0000018453`
`ACT_SITE`	`53 53`		`By similarity.`
`ACT_SITE`	`71 71`		`By similarity.`
`DISULFID`	`24 145`		`By similarity.`
`DISULFID`	`48 133`		`By similarity.`
`DISULFID`	`83 99`		`By similarity.`
`DISULFID`	`95 113`		`By similarity.`
`VARIANT`	`3 3`	`1`	`A -> T (in isozyme 2A).`
`VARIANT`	`5 5`	`1`	`V -> I (in isozyme 1 and isozyme 3).`
`VARIANT`	`17 17`	`1`	`Q -> K (in isozyme 2C).`
`VARIANT`	`45 45`	`1`	`N -> S (in isozyme 2D).`
`VARIANT`	`66 66`	`1`	`S -> G (in isozyme 1).`
`VARIANT`	`106 106`	`1`	`D -> E (in isozyme 1).`
`VARIANT`	`116 116`	`1`	`H -> Q (in isozyme 1).`
`VARIANT`	`143 143`	`1`	`E -> Q (in isozyme 3).`

Sequence information

Length: 147 AA [This is the length of the unprocessed precursor]

Molecular weight: 16373 Da [This is the MW of the unprocessed precursor]

CRC64: C678E7EECE1E66BF [This is a checksum on the sequence]

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

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

       130        140 
QGITAWVAWK SHCRDHDVSS YVEGCTL

P04421 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools