P11941 (LYSC2_ONCMY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Lysozyme C II EC=3.2.1.17 Alternative name(s): 1,4-beta-N-acetylmuramidase C Lysozyme type II
Organism	Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Taxonomic identifier	8022 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Actinopterygii › Actinopteri › Neopterygii › Teleostei › Elopocephala › Clupeocephala › Euteleostei › Protacanthopterygii › Salmoniformes › Salmonoidei › Salmonidae › Salmoninae › Oncorhynchus

Protein attributes

Sequence length	144 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. Has antibacterial activity against the Gram positive bacterium P.citreus. Has no antibacterial activity against the Gram negative bacteria E.coli and Y.ruckeri. Does not have hemolytic activity against trout erythrocytes. Ref.5
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. Ref.5
Subcellular location	Secreted.
Sequence similarities	Belongs to the glycosyl hydrolase 22 family.
Biophysicochemical properties	pH dependence: Optimum pH is 4.5-5.5. No activity above pH 8.8. Ref.5 Temperature dependence: Optimum temperature is 33-49 degrees Celsius. Retains 25% of its maximal activity after heating 10 minutes at 80 degrees Celsius.
Mass spectrometry	Molecular mass is 14252 Da from positions 16 - 144. Determined by MALDI. Ref.5

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Antibiotic Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase
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
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	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

Signal peptide

1 – 15

15

Ref.4 Ref.5

Chain

16 – 144

129

Lysozyme C II

PRO_0000018501

Sites

Active site

50

1

Active site

67

1

Amino acid modifications

Disulfide bond

21 ↔ 142

Disulfide bond

45 ↔ 130

Disulfide bond

79 ↔ 95

Disulfide bond

91 ↔ 109

Experimental info

Sequence conflict

94

1

R → H in AAG34564. Ref.3

Sequence conflict

101

1

A → D in AAG34564. Ref.3

Secondary structure

1

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144

Helix Strand Turn

Details...

Helix

20 – 29

10

Helix

40 – 51

12

Beta strand

58 – 60

3

Beta strand

66 – 68

3

Turn

69 – 72

4

Turn

75 – 77

3

Helix

95 – 98

4

Beta strand

99 – 102

4

Helix

104 – 113

10

Helix

119 – 122

4

Helix

124 – 129

6

Turn

130 – 132

3

Helix

136 – 138

3

Turn

139 – 141

3

Sequences

	Sequence		Length	Mass (Da)
	P11941 [UniParc]. Last modified April 1, 1993. Version 2. Checksum: BF945ADCDCC2D668	FASTA	144	15,737
	10 20 30 40 50 60 MRAVVVLLLV AVASAKVYDR CELARALKAS GMDGYAGNSL PNWVCLSKWE SSYNTQATNR 70 80 90 100 110 120 NTDGSTDYGI FQINSRYWCD DGRTPGAKNV CGIRCSQLLT ADLTVAIRCA KRVVLDPNGI 130 140 GAWVAWRLHC QNQDLRSYVA GCGV

References

[1]	"cDNA and amino acid sequences of rainbow trout (Oncorhynchus mykiss) lysozymes and their implications for the evolution of lysozyme and lactalbumin." Dautingny A., Prager E.M., Pham-Dinh D., Jolles J., Pakdel F., Grinde B., Jolles P. J. Mol. Evol. 32:187-198(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Molecular characterization of lysozyme type II gene from rainbow trout (Oncorhynchus mykiss): an evidence of a duplicate gene." Mitra A., Foster-Frey J., Wells K.D., Rexroad C.E. III, Wall R.J. Anim. Biotechnol. 14:7-12(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Kamploop. Tissue: Kidney.
[3]	"A new genetic variant of lysozyme from rainbow trout." Mitra A., Wells K.D., Rexroad C.E. III, Wall R.J. Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[4]	"Purification and characterization of two lysozymes from rainbow trout (Salmo gairdneri)." Grinde B., Jolles J., Jolles P. Eur. J. Biochem. 173:269-273(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 16-50.
[5]	"Two novel muramidases from skin mucosa of rainbow trout (Oncorhynchus mykiss)." Fernandes J.M.O., Kemp G.D., Smith V.J. Comp. Biochem. Physiol. 138B:53-64(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 16-30, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY. Tissue: Skin mucus.
[6]	"Refined crystal structure of lysozyme from the rainbow trout (Oncorhynchus mykiss)." Karlsen S., Eliassen B.E., Hansen L.K., Larsen R.L., Riise B.W., Smalaas A.O., Hough E., Grinde B. Acta Crystallogr. D 51:354-367(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[7]	"Structural studies on the binding of 4-methylumbelliferone glycosides of chitin to rainbow trout lysozyme." Vollan V.B., Hough E., Karlsen S. Acta Crystallogr. D 55:60-66(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X59491 mRNA. Translation: CAA42084.1.
AF322106 Genomic DNA. Translation: AAG45933.1.
AF452171 Genomic DNA. Translation: AAL48290.1.
AF321519 mRNA. Translation: AAG34564.1.

PIR

I51047.

RefSeq

NP_001118188.1. NM_001124716.1.

UniGene

Omy.11916.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BB6	X-ray	2.00	A	16-144	[»]
1BB7	X-ray	2.00	A	16-144	[»]
1LMC	X-ray	2.00	A	16-144	[»]
1LMN	X-ray	1.80	A	16-144	[»]
1LMO	X-ray	1.80	A	16-144	[»]
1LMP	X-ray	2.00	A	16-144	[»]
1LMQ	X-ray	1.60	A	16-144	[»]

ProteinModelPortal

P11941.

SMR

P11941. Positions 16-144.

ModBase

Search...

Protein family/group databases

CAZy

GH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDE

P11941.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

100136768.

Organism-specific databases

CTD

17105.

Phylogenomic databases

HOVERGEN

HBG052297.

Family and domain databases

InterPro

IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]

Pfam

PF00062. Lys. 1 hit.
[Graphical view]

PRINTS

PR00137. LYSOZYME.
PR00135. LYZLACT.

SMART

SM00263. LYZ1. 1 hit.
[Graphical view]

SUPFAM

SSF53955. SSF53955. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

EvolutionaryTrace

P11941.

Entry information

Entry name

LYSC2_ONCMY

Accession

Primary (citable) accession number: P11941
Secondary accession number(s): P83333, Q9DDK3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	April 1, 1993
Last modified:	April 3, 2013
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program