Reviewed, UniProtKB/Swiss-Prot P81708 (LYSC1_CANFA)

Names and origin

Protein names	Recommended name:     Lysozyme C, milk isozyme     EC=3.2.1.17 Alternative name(s):     1,4-beta-N-acetylmuramidase C
Organism	Canis familiaris (Dog)
Taxonomic identifier	9615 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	129 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 By similarity.
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.
Cofactor	Binds 1 calcium ion per subunit.
Subunit structure	Monomer By similarity.
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 By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 22 family.

Ontologies

Keywords
Ligand	Calcium
Molecular function	Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase Milk protein
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell 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
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW lysozyme activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 129

129

Lysozyme C, milk isozyme

PRO_0000208845

Regions

Calcium binding

81 – 92

12

By similarity

Sites

Active site

35

1

By similarity

Active site

53

1

By similarity

Amino acid modifications

Disulfide bond

6 ↔ 127

By similarity

Disulfide bond

30 ↔ 115

By similarity

Disulfide bond

65 ↔ 80

By similarity

Disulfide bond

76 ↔ 94

By similarity

Secondary structure

1

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129

Helix Strand Turn

Details...

Helix

5 – 13

9

Turn

14 – 16

3

Helix

25 – 35

11

Beta strand

48 – 51

4

Turn

55 – 58

4

Turn

61 – 64

4

Beta strand

68 – 70

3

Helix

80 – 83

4

Beta strand

84 – 86

3

Helix

89 – 99

11

Helix

104 – 107

4

Helix

109 – 114

6

Turn

115 – 117

3

Turn

121 – 126

6

Sequences

	Sequence		Length	Mass (Da)
	P81708-1 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: 64CD8C3F9C80359A	FASTA	129	14,471
	10 20 30 40 50 60 KIFSKCELAR KLKSMGMDGF HGYSLANWVC MAEYESNFNT QAFNGRNSNG SSDYGIFQLN 70 80 90 100 110 120 SKWWCKSNSH SSANACNIMC SKFLDDNIDD DIACAKRVVK DPNGMSAWVA WVKHCKGKDL SKYLASCNL

References

[1]	"Sequences of two highly divergent canine type c lysozymes: implications for the evolutionary origins of the lysozyme/alpha-lactalbumin superfamily." Grobler J.A., Rao K.R., Pervaiz S., Brew K. Arch. Biochem. Biophys. 313:360-366(1994) [PubMed: 8080284] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Milk.
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

S48641.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EL1	X-ray	1.90	A/B	1-129	[»]
1I56	NMR	-	A	1-129	[»]
1QQY	X-ray	1.85	A	1-129	[»]
2CWI	X-ray	1.94	A/B	1-129	[»]
2Z2E	X-ray	2.01	A/B	1-129	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH22. Glycoside Hydrolase Family 22.

Genome annotation databases

Ensembl

ENSCAFG00000008948. Canis familiaris. [Contig view]

Phylogenomic databases

HOVERGEN

P81708.

OMA

P81708. ICNIKCE.

Enzyme and pathway databases

BRENDA

3.2.1.17. 463.

Family and domain databases

InterPro

IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
[Graphical view]

Pfam

PF00062. Lys. 1 hit.
[Graphical view]

PRINTS

PR00137. LYSOZYME.
PR00135. LYZLACT.

SMART

SM00263. LYZ1. 1 hit.
[Graphical view]

PROSITE

PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

LYSC1_CANFA

Accession

Primary (citable) accession number: P81708

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)