Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P11941 (LYSC2_ONCMY) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 II

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Lysozyme type II
OrganismOncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Taxonomic identifier8022 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiEuteleosteiProtacanthopterygiiSalmoniformesSalmonidaeSalmoninaeOncorhynchus

Protein attributes

Sequence length144 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. 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 componentSecreted
   DomainSignal
   Molecular functionAntibiotic
Antimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
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

   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 – 1515 Ref.4 Ref.5
Chain16 – 144129Lysozyme C II
PRO_0000018501

Sites

Active site501
Active site671

Amino acid modifications

Disulfide bond21 ↔ 142
Disulfide bond45 ↔ 130
Disulfide bond79 ↔ 95
Disulfide bond91 ↔ 109

Experimental info

Sequence conflict941R → H in AAG34564. Ref.3
Sequence conflict1011A → D in AAG34564. Ref.3

Secondary structure

......................... 144
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11941 [UniParc].

Last modified April 1, 1993. Version 2.
Checksum: BF945ADCDCC2D668

FASTA14415,737
        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 

« Hide

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.
PIRI51047.
RefSeqNP_001118188.1. NM_001124716.1.
UniGeneOmy.11916.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BB6X-ray2.00A16-144[»]
1BB7X-ray2.00A16-144[»]
1LMCX-ray2.00A16-144[»]
1LMNX-ray1.80A16-144[»]
1LMOX-ray1.80A16-144[»]
1LMPX-ray2.00A16-144[»]
1LMQX-ray1.60A16-144[»]
ProteinModelPortalP11941.
SMRP11941. Positions 16-144.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEP11941.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100136768.

Organism-specific databases

CTD17105.

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...

Other

EvolutionaryTraceP11941.

Entry information

Entry nameLYSC2_ONCMY
AccessionPrimary (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: October 16, 2013
This is version 93 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries